My Histology-Conn.tissue/bone/cart.

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Connective Tissue

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Forms a continuum w/other tissues to maintain a functionally intergrated body, consists of cells and ECM but mostly ECM. Provides structural support for body storage of metabolites, defense and protection, immune response, inflammation, allergic response, repair by fibrous scar

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ECM of Connective Tissue

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consists of fiber and ground substance. The 3 fibers are collagen, reticular and elastic fibers.

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Collagen

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extracellular fibrillar protein, most abundant, principal structural component of conn. tissue. Flexible and high tensile strength, produced by fibroblasts, chondroblasts, and osteoblasts. 20 different types

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Collagen fibrils

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form collagen and reticular fibers. Formed by tropocollagen molecules, unique banding pattern due to alignment of molecules, make up hyline cartilage, cant be viewed in light microscope

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tropocollagen

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makes up collagen fibrils, formed by a triple helix of collagen molecules (3 chains) polymerized laterally and head to tail to created the unique banding pattern

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type 1 collagen

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most abundant, banded fibrils-->fibers-->bundles (only one with bundles) found in the dermis of the skin, tendons, ligaments, fascia, bone, and conn. tissue proper.

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type 2 collagen

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found only in cartilage, made of banded fibrils, glassy apperance, cant be viewed in a light microscope.

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type 3 collagen

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banded fibrils-->reticular fibers form supporting framework for cells of various tissue and organs ex. loose conn. tissue, walls of blood vessels, lymphoid tissue, bone marrow, smooth muscle, nerves, lungs, delicate organs.

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type 4 collagen

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no banded fibrils but a sheet like meshwork of beaded filaments found in the basal lamina

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Ehlers-Danlos syndrome

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1/5000 births, congenital disorder, impaired extracellular modification of collagen, produces defective fibers, usually skin hyper elasticity, loose unstable joints, low muscle tone, weakness and bone abnormalities

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elastic fibers

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allows tissues to stretch and distention, thinner than collagen, arranged in branching pattern to form network , more refractile than surrounding tissue, composed to two types of fibrillar proteins: elastin and fibrillin

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elastin

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hydrophobic domain (causes coiling in aqueous enviro), cross linked by covalent bonds, forms fibers of variable length or lamellar layers (blood vessels) contributes to elasticity of conn. tissue

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fibrillin

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mold for elastic fibers, glycoprotein that forms microfibrils that surround developing elastic fibers, provides substrate for their assembly

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Marfans syndrome

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mutation in fibrillin gene, cardio, skeletal and ocular defects, common occurance

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ground substance

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fills spaces between fibers in the ECM. composed of glucosaminoglycans (GAGs), proteoglycans, multiadhesive glycoproteins

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GAG's

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most abundant substance in ground substance, long chain unbranched highly negative charged polysaccharides. The neg charge makes them hydrophilic so they bind with water and form a gel (to resist compression and allow quick diffusion)

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elastic fibers

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allows tissues to stretch and distention, thinner than collagen, arranged in branching pattern to form network , more refractile than surrounding tissue, composed to two types of fibrillar proteins: elastin and fibrillin

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Types of GAGs

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Hyaluronic acid, chondroitin sulfate, dermatan sulfate, keratan sulfate, heparan sulfate (the sulfates attache to protein to form proteogylcans)

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elastin

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hydrophobic domain (causes coiling in aqueous enviro), cross linked by covalent bonds, forms fibers of variable length or lamellar layers (blood vessels) contributes to elasticity of conn. tissue

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Hyaluronic acid

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-always present in ECM, very long, no sulfate, does not for

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fibrillin

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mold for elastic fibers, glycoprotein that forms microfibrils that surround developing elastic fibers, provides substrate for their assembly

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Marfans syndrome

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mutation in fibrillin gene, cardio, skeletal and ocular defects, common occurance

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Proteoglycans

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brush like formation of GAGs and core protein, attached non covalently to hyaluronic acid by link protein, forms gel state of ECM

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Multiadhesive glycoproteins

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cross links between collage, ECM and cells, stabilizes ECM, binds ECM to transmembrane proteins from integrin family (hemidesmosomes and focal adhesions)

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ground substance

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fills spaces between fibers in the ECM. composed of glucosaminoglycans (GAGs), proteoglycans, multiadhesive glycoproteins

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GAG's

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most abundant substance in ground substance, long chain unbranched highly negative charged polysaccharides. The neg charge makes them hydrophilic so they bind with water and form a gel (to resist compression and allow quick diffusion)

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Types of GAGs

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Hyaluronic acid, chondroitin sulfate, dermatan sulfate, keratan sulfate, heparan sulfate (the sulfates attache to protein to form proteogylcans)

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Hyaluronic acid

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-always present in ECM, very long, no sulfate, does not for

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Proteoglycans

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brush like formation of GAGs and core protein, attached non covalently to hyaluronic acid by link protein, forms gel state of ECM

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Multiadhesive glycoproteins

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cross links between collage, ECM and cells, stabilizes ECM, binds ECM to transmembrane proteins from integrin family (hemidesmosomes and focal adhesions)

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Fibronectin

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most abundant multi. glycoprotein, contains binding domains for collagen type 1/2/3, GAGs, fibrin, integrin, and others, can assemble into fibers, is a dimer

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Laminin

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basement membrane, binding site for collage type 4, integrins and others

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connective tissue cell types

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resident and transient

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resident (fixed) cells

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undergo mitosis w/in the conn. tissue and spend most of their lives there (fibroblasts, adipocytes, macrophages, mastcells)