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299 Cards in this Set
- Front
- Back
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Microfilaments
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Actin and myosin
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Actin
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structural microfilaments, composed of F actin
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F actin
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G actins polymerized into a double helix
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G actin
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monomeric actin subunits
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Tropomysoin
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a regulatory alpha helix in muscle that wraps around F actin myofilaments
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Troponins (C,T,I)
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regulatory subunits that respond to Ca to interact with tropomyosin and induce muscle contraction
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spectrin
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actin crosslinking protein that forms networks in erythrocytes
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dystrophin
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actin crosslinking proteins that forms networks in striated muscle
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myosin
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a structural microfilament as well as a motor protein for actin
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actomyosin
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actin and myosin associated with each other
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stress fibers
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bundles of actinmyosin anchored to the basal surgace of fibroblasts, which are themselves atached to the substratum. These fibers produce trension across a cell layer.
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Microtubules
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polymers of alpa and beta tubulin
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Tau and MAP (microtubular associated proteins)
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microtubuluar croslinking proteins that form networks
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Dynein
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a mucrotubule motor protein for flagella, cilia, axons and kinetochores
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Intermediate filaments
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structural components of the cytoskeleton. Intermediate filaments are complexes composed of proteins that all have similar alpha helical cores, but distinctive terminal domains
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Keratin
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a major intermediate filament of epithelial cells
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Nuclear lamins
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intermediate filaments supporting the nuclear membrane
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Collagens
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extracellular matrix fibers that resist stretching composed of 3 helicies coiled around each other in a triple helix
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Elastin
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stretchable extracellular matrix fibers that provide tissues with pliability
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Fibrillin
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glycoprotein microfibrils that provide a scaffold for assembly of elastic fibers
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glycosaminoglycans
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polysaccharides of the extracellular matrix compose of disaccharide repeats of modified sugars
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hyaluronans
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a particularly large glycosaminoglycan that exists free in the excellular matrix
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proteoglycans
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extracellular matrix components, composed of core proteins attached to one or more glycosaminoglycan
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heparin
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a regulator proteoglycan control inflammation
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laminin
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extravellular matrix crosslinking protein formin networks in the basal lamina
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fibronectin
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extracellular matrix crosslinking pritein with multiple binding domains for different factors
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integrin
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the transmembrane protein for hemidesosomes and adhesoin plaques. it is bound by an adaptor protein or plaque on the cytoplasmic sid of the membrane and fibronectin on the extracellular side
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ankyrin
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a membrane-microfilament binding protein that binds spectrin in eruthrocyetes and desmin from muscle sacromeres
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adapter proteins
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factors that link actomyosin filaments to integrin in adhesion plaques or cadherin in belt desmosomes
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cadherins
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a family of calcium dependent transmembrane proteins taht rie similar cells together. one of the cadherins is used in belt desmosomes
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spot desmosomes
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isolated "spot welds" joining the intermediate filament cytoskeletons of two cells at their lateral surfaces
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hemidesmosomes
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structures that ancor the intermediate filament cytoskelotons of an epithelial cell to the basal lamina
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membrane-microhilament binding proteins
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membrane associated roteins taht anchor the microfilament cutoskeleon to the plasma membrane by binding actin crosslinking proteins
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adesion plaques
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structures that anchor microfilament stress fibers to the basal surface of many cells, particularly epithelial cells
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zonula occludens
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thin bands od membrane around the apical perimeters of epithelial cells, help together by proteins sucj as ccludin and claudin. They seal cells to prevent diffusion of molecules across the epithelium.
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zonula adherens
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rows of structures anchoring actin microfilaments to the apical surface of epithelial cells, just beneath th tight junction
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circumferential belt
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microfilament bundles (actin and myosin) that encircle the apical perimeter of epithelial cells that the level of the belt desmosomes
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gap junctions
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transmembrane complexes that allow for diffusion of small molecules between cells to vesicles
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G1 phase
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the period following mitosis or meiosis with no DNA replicaiton
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G0 phase
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an arrested G1 phase. cells which cease to divide are usally in a permanent G0 phase
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S phase
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The period of DNA replication
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G2 phase
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The period between the completion of DNA reliction and the onset of mitosis or meiosis
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Chromatids
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dupicated chromosomal strands produced by DNA replication. These are not considered different chromosomes becase they have identical genes.
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Homologs
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matching chromosomes from different parents
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Bipartite
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joined chromatids, observed in mitoses and meiosis
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bivalent
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chromatids and homologs, joined during meiosis
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tetrads
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Synonymous term for bivalents, referring to the four strands held together
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Synapsis
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The process of holding homologs together at different points along their lengths
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Synaptinemal complex
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a laffer like structure that forms between homologs to produce synapsis and mediate crossing over
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chiasma
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X shaped formations produced where homolofs are held together by synapsis
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crossing over
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a process by which sectoins of homologs are exchanged
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Ploidy
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The number of complete sets of chromosomes in a genome
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n
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number of chromosome strands per homolog
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haploid
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to have one set of chromosomes (gmates
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diploid
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To have two sets of chromosomes. One set from mother one from father. somatic cells. 2n>interphase>4n>mitosis>2n
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cytokinesis
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division of the cytoplasm and plasma membrane
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Karyokinesis
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nuclear division. completed in telophase, begun in prophase.
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Prophase I
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Leptonema to Diakinesis
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Leptonema (letotene phase)
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spindle formation, cormosomal condenstaion and nuclear membrane dissociation all begin. Sister chromatids already tied together into bipartites
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Zygonema (zygotene phase)
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synapsis begins. Synaptinemal complexes form, holding tetrads together along their lengths
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pachynema (pachytene phase)
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Synapsis complete, holding homologs together as parallel strands. Crossing over occurs. The synaptinemal complexes moves down the bivalents, exchanging DNA strands and randomizing the combination of paternal and maternal genes along each chromatid
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Diplonema (diplotene phase)
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Homologs repel each other. Chiasma become visible where the homolofs are still held by synapsis. Synaptinemal complexes move to the ends of the chromosomes and dissociate. In mammalian females, ooxutes arrest for years waiting for menstruual cycle.
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Diakinesis
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All chiasma released by dissociation of synaptinemal complexes. Chromosome condensation completeld, so that the four chromatids appear as discrete units. Spindle formation and nuclear membrane breakdown completed. Tetrads move to metaphase plane.
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Are microflimaments motile?
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Yes
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Are microtubules motile?
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Yes
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Are intermediate filaments motile?
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No
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What energy do microfilaments use?
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ATP
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What energy do microtubules use?
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GTP
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What energy do intermediate filaments use?
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None they are not motile only structural
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what makes up microfilaments?
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actin and myosin
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what makes up microtubules?
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alpha dn beta tubulin
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what makes up intermediate filaments?
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Keratins and Nuclear Lamins
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Which classes are used for structure?
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All. Microfilaments, microtubules and intermediate filaments.
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Assembly of actin
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G actins polymerize into double helical F actins due to ATP hydrolysis.
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What controls muscle contraction?
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Actin binding proteins such as tropomyosin and troponis C, T and I
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Tromomyosin
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rope like alpha helicies that wrap around F actins
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troponins C, T and I
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Regulatory subunits binding to both tropomysosin and actin
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What are the crosslinking proteins for Microfilaments?
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Spectrin and Dystrophin
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Spectrin
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actin crosslinking protein that forms networks in erythrocytes
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Dystrophin
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dorm striated muscle networks
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Microvilli are an example of what?
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A structurl utilization of Actin. Microvilli are finger like progections of plasma membrane, supported by internal actin bundles.
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Where are microvilli found?
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They increase surface area of plasma membrane and are on all cells but are abundant on the brush border of intestinal epithelium.
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what are stereocilia?
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microvilli of the inner ear, incolved in audio reception.
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what is the most common isoform of myosin?
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myosin II. used in muscle contraction
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What kind of chains is mysoin made out of?
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light and heavy
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what is a heavy myosin chain?
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alpha helix and globular head. The heads provide the motor force.
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what is a light myosin chain?
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homologous to troponin C and serve as regulatory factors controlling contrcation of the globular heads.
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how do myosin chains associate?
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two heavy chains coil around each other using ATP.
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is there polarization in mysoin formation?
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Yes. all globular heads point to the inside.
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Explain the sliding filament model
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ATP hydrolysis activates a conformational change in the mysoin heads caing the myosin to chawl along the actin.
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what role does Ca have in contraction?
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Ca binds to troponin C causing it to interact with troponin T and I and shift tropomysoin to the center of the thin myofilament. this exposes myosin binding sites of actin for sliding filament contraction.
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other Ca responsive molecules
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calmodulin, caldesmon and myosin light chains which interact with myosin heavy chains or troponins to control contraction of globular heads.
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examples of microfilament mediated motility
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intracellular membrane trafficking, muscle, contractile ring of cytokinesis, ameboid motion and stress fibers.
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sacromeres
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actomyosin repeats
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explain the assembly of microtubules
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alpha dn beta tubulin bind each other to form dmers. These dimers bind end to end to form hollow microtubules.
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Are microtubules polarized?
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Yes. The beta subunits face the + end.
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what are protofilaments?
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rows of alpha and beta dimers. there are 13 of them.
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what end do to alpah and beta complexes add to more often?
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beta or + end.
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is polarization and depolarization a continuous process?
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Yes
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what kind of energy do microtubules need and when?
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tubulin uses GTP for energy. GTP is used when adding dimers to end of a growing microtubule
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what tubulin subunit hydrolized GTP?
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beta.
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what is the target of chemotherapy?
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microtubules. specifically they interupt microtubule assembly. This works because tumor cells are proliferating fo much faster. Mitotic spindles stop forming. This affects all cells and therefore, they give largest dose possible.
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how do microtubules form networks?
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they use MAPs and tau
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Anterograde transport
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from cell to synapse
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retrograde transport
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synapse to cell body
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9 + 2 arrangement
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9 microtubule doublets with a central microtubule doublet Dynein arms between the doublets create the motor force with ATP hydrolosis. This is enclosed by a plasma membrane
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Mitotic apparatus
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all microtubules and associated factors involved with chromatid separation
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centrosome
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a small organelle consisting of a perpendicular pair of centriles surrounded by a matrix of two proteins
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Microtubular organizaing centers (MTOC)
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centers for the initiation of microtubule formation. Microtubules frow by adding subinits to preassembled tubulin, so they require some source of tubulin to serve as nucleation centers. In animal cells centriles probably serve this purpose. howeve, plant centrosomes lack centrioles so some other structure must serve as their MTOC.
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mitotic apparatus
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spindle and asters
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mitotic spindle
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spindle shaped complexes of microtubules which serve to seperate daughter chromosomes during mitosis
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asters
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an area at each end of the spindle where the microtubules converge
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What are the three microtubules that the mitotic apparatus is made of?
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astral MT, polar MT and kinetochore MT.
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what is astral MT?
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compose the aster, they radiate from the center
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what is polar MT?
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exted halfway across the spindle
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what is kinetochore MT?
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exten across the entire spindle, from aster to aster.
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how does the keneticore MT retract during MT?
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through depolarization
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Kinetochore
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a protein structure joining centromeres to th microtubules of the spindle
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what are all intermediate filaments made of?
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alpha helical cores
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what are examples of intermediate filaments?
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keratins, nuclear lamins and desmin
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what is desmin?
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links z disks of striated muscle sarcomeres to each other and to the plasma membrane
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how do you used intermediate filaments in cancer diagnosis?
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cells have the same IF from the original cell
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is there polarity in the buliding of intermidiate filaments?
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NO beaucse of anti parallel formation
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is energy used in the formation of intermediate filaments?
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NO
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what cross links intermediate filaments?
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IFAPs (intermediate filament associated proteins) and Ankyrin
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at what phosphorylation state do lamins dissociate?
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when they are phosphorylated
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what is B lamin?
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It is anchored to the inner membrane of the nucleus by an isoprenyl side group
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what happens to lamins A and C after phosphorylation?
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They go into the cytosol
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what happens to lamin B after phosphorylation?
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stays bound to vessils
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what is the function of the extracellular matrix?
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To provide shap abd resiliency to tissues and organs. It also provides a medium for cells to interact.
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What are the major components of the extracellular matrix?
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collagen, elastin, hyalyronan and proteoglycans.
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What is the structure of collagen?
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3 left handed helical polypeptides. These associate into a right handed triple helix.
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What is trpocollagens?
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3 left handed helical polypeptides which associate into a right handed triple helix.
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What amino acid alowes tfor the heft handed helicies?
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proline.
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what residue is found every 3rd amino acid and what does it do?
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glycine which helps the protein turn into a helix.
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why does a dietery deficiency in Vitamin C cause scurvy?
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Vitamin C is a cofactor for the enzyme which makes hydroxyproline. if you do not have it, you can not hydroxylate the abundant prolines which lessens the non-covalent interactions in collagen.
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are there glucose-galactose disaccharides attached to collagen?
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Yes. This process is refered to as glycosylation.
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What enzyme crosslinks collagen?
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lysyl oxidae.
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where does the assembly of collagen take place?
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outside the cell because it would be to lange inside.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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collagen fibril
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crosslinked tropocollagen
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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collagen fibril
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crosslinked tropocollagen
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what produces fibrosis?
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overproduction of collagen
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what causes Ehlers-Danls syndrome (rubber-man syndrome)?
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Mutations results in underproduction of collagen or incomplete processing of different collagens.
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what produces fibrosis?
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overproduction of collagen
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what is osteogenesis imprefecta (brittle bone syndrome)?
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This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
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when is osteogeneis imprefecta most dangerous?
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during birth or before birth
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what causes Ehlers-Danls syndrome (rubber-man syndrome)?
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Mutations results in underproduction of collagen or incomplete processing of different collagens.
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what is osteogenesis imprefecta (brittle bone syndrome)?
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This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
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can osteogenesis imprefecta be misdiagnosed as abuse in children?
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Yes because there are so many fractures.
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when is osteogeneis imprefecta most dangerous?
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during birth or before birth
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can osteogenesis imprefecta be misdiagnosed as abuse in children?
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Yes because there are so many fractures.
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What is the function of elastin?
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provides tissue with the ability to return to their original size and shape.
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What is the function of elastin?
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provides tissue with the ability to return to their original size and shape.
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Is elastin in the aortic arch?
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Yes it is most abundant in that area.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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Is elastin in the aortic arch?
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Yes it is most abundant in that area.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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where is collagen produced?
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primarly fibroblasts and chondroblasts and osteoblasts.
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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collagen fibril
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crosslinked tropocollagen
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collagen fibril
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crosslinked tropocollagen
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collagen fibril
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crosslinked tropocollagen
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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Do you have tropocollagen inside the cell?
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No this term is only for when collagen is outside of the cell
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collagen fibril
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crosslinked tropocollagen
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what produces fibrosis?
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overproduction of collagen
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what produces fibrosis?
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overproduction of collagen
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collagen fibril
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crosslinked tropocollagen
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what produces fibrosis?
|
overproduction of collagen
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collagen fibril
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crosslinked tropocollagen
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collagen fibril
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crosslinked tropocollagen
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collagen fibril
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crosslinked tropocollagen
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collagen fibril
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crosslinked tropocollagen
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collagen fibril
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crosslinked tropocollagen
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collagen fibril
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crosslinked tropocollagen
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what is the function of the extracellular matrix?
|
To provide shap abd resiliency to tissues and organs. It also provides a medium for cells to interact.
|
|
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what produces fibrosis?
|
overproduction of collagen
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
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collagen fibril
|
crosslinked tropocollagen
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
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collagen fibril
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crosslinked tropocollagen
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
What are the major components of the extracellular matrix?
|
collagen, elastin, hyalyronan and proteoglycans.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what produces fibrosis?
|
overproduction of collagen
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
what causes Ehlers-Danls syndrome (rubber-man syndrome)?
|
Mutations results in underproduction of collagen or incomplete processing of different collagens.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
What is the structure of collagen?
|
3 left handed helical polypeptides. These associate into a right handed triple helix.
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when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
What is trpocollagens?
|
3 left handed helical polypeptides which associate into a right handed triple helix.
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can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
Is elastin in the aortic arch?
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Yes it is most abundant in that area.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
what is osteogenesis imprefecta (brittle bone syndrome)?
|
This is a mutation in Type 1 collagen which intereferes with the triple helix assembly. This mutation is caused by the substitution of glycines for other bulky residues.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
What amino acid alowes tfor the heft handed helicies?
|
proline.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
when is osteogeneis imprefecta most dangerous?
|
during birth or before birth
|
|
|
what residue is found every 3rd amino acid and what does it do?
|
glycine which helps the protein turn into a helix.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
can osteogenesis imprefecta be misdiagnosed as abuse in children?
|
Yes because there are so many fractures.
|
|
|
What is the function of elastin?
|
provides tissue with the ability to return to their original size and shape.
|
|
|
why does a dietery deficiency in Vitamin C cause scurvy?
|
Vitamin C is a cofactor for the enzyme which makes hydroxyproline. if you do not have it, you can not hydroxylate the abundant prolines which lessens the non-covalent interactions in collagen.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
are there glucose-galactose disaccharides attached to collagen?
|
Yes. This process is refered to as glycosylation.
|
|
|
What enzyme crosslinks collagen?
|
lysyl oxidae.
|
|
|
Is elastin in the aortic arch?
|
Yes it is most abundant in that area.
|
|
|
where does the assembly of collagen take place?
|
outside the cell because it would be to lange inside.
|
