title: Studies on the molecular organization of the lens.
abstract: Based on recent findings from our laboratories, we propose the working hypothesis that the macromolecular organization of the outer cortex is dependent upon a functional link which occurs between actin, gamma-crystallin and metabolism. This hypothesis is rooted in the following observations: (1) actin polymerization is energy-dependent; (2) exogenously added gamma-crystallin modifies the rate, extent and pattern of actin polymerization in vitro; (3) the metabolite L-alpha-glycerol phosphate appears to bind to gamma-crystallin, and (4) glycolytic enzymes occur in an organized array on actin filaments.
authors.affiliation: UMD-New Jersey Medical School, Newark.
authors.forename: P N
authors.initials: PN
authors.lastname: Farnsworth
authors.forename: T W
authors.initials: TW
authors.lastname: Schleich
authors.forename: B
authors.initials: B
authors.lastname: Groth-Vasselli
authors.forename: C L
authors.initials: CL
authors.lastname: Kuckel
mesh_terms: D000199:Actins / Q000378:metabolism; D003459:Crystallins / Q000502:physiology; D004058:Diffusion; D005994:Glycerophosphates / Q000378:metabolism; D006801:Humans; D007834:Lasers; D007908:Lens, Crystalline / Q000378:metabolism*; D008027:Light; D046911:Macromolecular Substances / Q000378:metabolism; D008962:Models, Theoretical; D010449:Peptide Mapping; D011108:Polymers / Q000096:biosynthesis; D012542:Scattering, Radiation
chemical_list: D000199:Actins; D003459:Crystallins; D005994:Glycerophosphates; D046911:Macromolecular Substances; D011108:Polymers; C029620:alpha-glycerophosphoric acid