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44 Cards in this Set

  • Front
  • Back
Eye metabolism
The eye is comprised of living tissue that have energy and material needs. These needs are met through conventional metabolic pathways
Tears
bathe exterior of cornea
Aqueous humor
bathes interior of cornea
Composed of salts, albumin, globulin, glucose, others..
Brings nutrients to lens and removes metabolic waste
Vitreous Humor
Gelatinous
Cornea
Part of the CNS!!
High activity of glutathione reductase
Permeable to oxygen
-ROS!
-Correction by glutathione
Metabolic fuel of Cornea
Glucose
30% ATP form glycolysis
65% ATP from PPS
-Interconversion to provide glycolysis intermediates
Lens
ALIVE!!
No blood supply
Metabolically active
Nutrients and waste: aqueous humor
Crystallins
Proteins that make the lens
Epithelia surrounding lens
Makes enzymes, albuminoids, and membrane proteins
Lens Protection
Na+/K+ pumps, glutathione, proteins synthesis, and other metabolic events
Lens Sensitivity
Sensitive to:
-Redox rxns
-Osmolarity
-High lvls of metabolites
-UV radiation
Energy for Lens
Seems to come from peripheral cells
85% glycolysis
10% PPS
3% TCA/ETC
Lens Growth
From the periphery throughout life
From birth to 80 increases 3x in size and 1.5x thickness
Presbyopia
Loss of near vision
Cataract Causes
Only known disease of Lens
Senile cataracts:
Age related
Rearrangement of proteins in lens
Breakdown of protein molecules
Diabetic Cataracts:
Increased osmolarity due to activity of aldose reductase and polyol (aldose) dehydrogenase from elevated glucose
Results in increased sorbitol (unused and accumulates)
Changes osmolarity
Cataract Symptoms
Light scattering properties develop
No known cures
Side effect of cataract and surgical treatments is glaucoma
Energy for Retina
Anaerobic glycolysis, like the lens
Vascular tissue
Lactate dehydrogenase
-Can use NADH OR NADPH
Macula
Center of retina
Contains Fovea centralis - center of macula
Fovea Centralis
Avascular
Spot of greatest visual activity
Mitochondria and Rods and Cones
Mitochondria located in rods and cones not in outer segments where visual pigments are located
Light enters eye through
Lens
Reaches the outer segment of rods and cones
Signal transduction begins
Pigmented Epithelial Layer
Absorbs excess light and prevents reflection
Processes of Light
Photochemical
Kinetic
Biochemical
Electrical
Photon
A discrete particle of light
Rods and Cones
Photoreceptor cells
Proteins contain the prosthetic group 11-cis-retinal
Pigment in Rods
Rhodopsin
Pigment in Cones
Red, green, or blue
When Photon Strikes a Rod
11-cis-retinal is ISOMERIZED by the energy to all-trans-retinal
Isomerization of 11-cis-retinal
Happens in picoseconds
Results in a string of stepwise events
Creation of metarhodopsin
Disassociation of opsin and all-trans-retinal
restoration of 11-cis-retinal
ALL KINETIC OR MECHANICAL EVENTS
Metarhodopsin
Active molecule with half-life of 60 seconds
Complexes with TRANSDUCIN
Transducin
G PROTEIN
alpha subunit activates a phosphodiesterase
PDE changes cGMP to 5' GMP
-closes Na+ channels
-Change in membrane potential
-Electrical event
Termination and reset
Metarhodopsin is acted on by rhodopsin kinase
-Product has high affinity for arrestin
-Now cannot bind to transducin
-Allows ONE (ONLY ONE) cycle to happen
-Hydrolysis of the Pi restores the arrestin and then soon the rhodopsin
Rod Cells
can detect a signal as LOW as 5 photons
The signal, different form many neurons, is not an all or nothing event
Graded intensity from deviation from the -30mV steady state to -35mB and number of rods that fire
Differences between Rods and Cones
Cones are domain of color
Uses 11-cis-retinal but different pigments, rods use rhodopsin pigment
Each cone has one pigment
Rods are FAR MORE SENSITIVE
Cones respond FAR FASTER
-Rods for low light
-Cones for rapidly changing
Pases of Blood Coagulation
Procoagulation - Clot formation
Anticoagulation - Stopping clot formation
Fibrinolysis - Clot dissolution
Zymogens in Coagulation
FX to FXa
Key in phase one is to active FX to FXa
FXa
Responsible for prothrombin activation
Thrombin
A key enzyme in making the clot
Responsible for fibrin formation and a host of other factors
Tissue Factor
Activated during injury and acts as a receptor for FVII
Fibrinogen
Thrombin activates fibrinogen and a platelet receptor
Fibrinogen is cut by thrombin creating a molecule capable of aggregation
Sites of Fibrin aggregation activate platelets
Aided by a thrombin receptor (activated by thrombin)
Why Not anywhere else (Sites of fibrin aggregation that activate platelets)
No exposed receptors
Activators are not at a high enough concentration
Endothelium secrets postacyclin which inhibits platelet aggregation
Anticoagulation Phase
Beings IMMEDIATELY with coagulation phase
Inhibitors bind with active proteins and enzymes
Inhibitor activity increases and zymogens are activated
Anticoagulation phase increases as coagulation phase increases
Coagulation stops and complexes are removed by the liver
Fibrinolysis
Plasminogen has a high affinity for active fibrin
Tissue plasminogen activator activates plasminogen to plasmin
-TP-A also binds to fibrin
Plasmin hydrolyzes the clot to soluble proteins
In both clot formation and removal, proteins are used up, not recycled