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Biomedical subjects

R L Mathur

Publications and source records attributed to R L Mathur.

18 recordsLinked to original sources
PubMed1992

Investigation of lens glycolytic enzymes: species distribution and interaction with supramolecular order.

Distribution of several glycolytic enzymes in the lenses of different vertebrate species and their organization in the calf lenses were studied. Though no general pattern of enzyme activities in different species is discernible, high activities of TPI followed, in decreasing order, by GAPDH, enolase, PK, LDH and aldolase appear to be more common. Our observation on the unusually high activities of aldolase in the pig, enolase in the sheep and LDH in the duck lens are interesting in view of the already known dual function of LDH as an enzyme and a structural protein (epsilon-crystallin) in duck. Controlled treatment with detergents Brij-58 and Triton X-100 caused distinctly differential purturbations in the lens cells. In spite of fiber membrane disruption and partial actin dissolution by Brij-58, no significant increase in the release of glycolytic enzymes compared to control was observed. This suggests that none of the enzymes existed as a completely soluble and freely diffusible fraction. But treatment with a strong detergent (Triton X-100) caused the release of higher amounts of enzymes suggesting either a direct or indirect interaction with the cytomatrix components. Aldolase appears to be maximally bound in the cytosol followed by TPI, GAPDH, LDH and PK in decreasing order. Although thin lens slices were incubated with the detergents for a total period of 40 min and the loss of fiber architecture and organization confirmed by light microscopy, in the Triton X-100 treated tissues less than 25% of the total activity of any enzyme except TPI appeared in the bathing medium.(ABSTRACT TRUNCATED AT 250 WORDS)

Animals↗
PubMed1990

L-alpha-glycerophosphate binding to bovine gamma-crystallin: a potential link between metabolism and supramolecular order.

The highly selective nature of protein-ligand interactions provides a sensitive mechanism for the modulation of cellular activity by proteins. In the eye lens the supramolecular order of the lens crystallins, which is expected to be susceptible to protein electrostatic charge, in part defines transparency. The binding of charged ligands to proteins is one way of achieving an alteration in protein electrostatic charge. Evidence is presented that L-alpha-glycerophosphate, a major phosphorus metabolite of eye lens metabolism, binds to the globular protein, gamma-crystallin with moderately high affinity and in a positive cooperative manner. The following binding parameters were obtained from equilibrium measurements: minimum number of binding sites, n = 2; Kassoc = 6.2 +/- 0.5 x 10(3) M-1; cooperativity parameter, alpha H = 1.9 +/- 0.1. Interactive computer graphics display techniques were used to locate putative ligand binding sites, and in turn, to identify the possible molecular interactions responsible for the binding of ligand to protein at one of the sites. One putative binding site was located in the cleft between the two domains of gamma II-crystallin. Arginyl residues 79 and 147 are involved in ligand binding as are the peptide carbonyl oxygens of residues Tyrosyl-50 and Aspartyl-156. Five hydrogen bonds between the ligand and the protein structure are predicted for the binding of L-alpha-glycerophosphate, whereas only 3 occur for the binding of the "unnatural" D-enantiomorph. Modulation of both lens protein supramolecular organization and lens metabolism is predicted to be a consequence of L-alpha-glycerophosphate binding to gamma-crystallin in the lens.

Animals↗
PubMed1990

Effects of a tryptophan supplemented diet and U.V. radiation on the rat lens.

Rats maintained on a tryptophan supplemented diet and exposed to U.V. radiation showed decreased concentration of ascorbic acid in serum. In the lens, a small increase in the urea-mercaptoethanol soluble fraction was observed suggesting some oxidation of P-SH groups. The decreased concentrations of lens glutathione and ascorbic acid were accompanied with increased concentration of malondialdehyde suggesting increased oxidative stress. The activities of glutathione peroxidase decreased by about 40%. Though the activity of glutathione reductase decreased by about 58%, addition of FAD in the enzyme assay system showed restoration of lost activity. Additive effect of raised serum tryptophan concentration and ultraviolet radiation in causing damage to the eye lens is suggested.

Animals↗
PubMed1989

India-US case-control study of age-related cataracts. India-US Case-Control Study Group.

In a hospital-based case-control study of 1441 patients with age-related cataracts and 549 controls, we studied associations between types of cataract--nuclear, cortical, posterior subcapsular, and mixed--and a number of physiologic, behavioral, environmental, and biochemical variables. Using polychotomous logistic regression analysis, we found an increased risk of cataract with lower educational achievement (all types of cataract), decreased cloud cover at place of residence (all types), use of aspirin less than once a month (posterior subcapsular and mixed), diets low in selected nutrients (posterior subcapsular, nuclear, and mixed), higher blood pressure (nuclear and mixed), lower body mass index (nuclear and mixed), use of cheaper cooking fuels (cortical, nuclear, and mixed), and lower levels of an antioxidant index based on red blood cell levels of glutathione peroxidase and glucose-6-phosphate dehydrogenase and plasma levels of ascorbic acid and vitamin E (posterior subcapsular and mixed). All risks cited were significantly different from those for the other cataract types, a finding that emphasizes the need to investigate the epidemiology of specific types of cataract.

Adult↗
PubMed1983

Distribution of taurine in the crystalline lens of vertebrate species and in cataractogenesis.

Marked heterogeneity was observed in the distribution of taurine in different regions of the lens in various species. In general low taurine pools were observed in the nucleus of all species except frog and human. The distribution of taurine in human senile cataractous lenses at different stages of maturation showed decreased contents in all the regions except capsule epithelium as compared to the normal human lenses. This decrease is progressive upto the 'mature' stage of cataract. In rat lenses with galactose cataracts taurine contents decreased by about 83-94% of the normal values in the equatorial, anterior, posterior cortical and nuclear regions.

Animals↗
PubMed1983

Studies on synthesis and uptake of taurine in rat lens in vitro.

The occurrence of large taurine pool sizes in the crystalline lens was further elucidated by studying the in vitro synthesis and uptake of taurine in the rat lens. It was observed that a time- and concentration-dependent synthesis of taurine from methionine occurred in the rat lens. The time curve for uptake was linear up to 4 hr and was not saturated up to 40 mM concentration of taurine. The uptake was inhibited by ouabain, cyanide, Ca2+, GTP and cGMP but was not affected by ATP and cAMP. It is suggested that a dual mechanism exists for maintenance of high concentrations of taurine in the lens. Moreover, the uptake mechanism is energy-dependent.

Adenosine Triphosphate↗
PubMedDate not supplied

Clinico-biochemical study of experimental complicated cataracts.

Clinically observed complicated cataracts, generally do not have a definite causal factor. We studied the effects of E. coli toxin injected suprachoroidally, to simulate the effect of toxins released by extraocular organisms on the lens. 79.2% of eyes had a definable cataract at the end of the 6th week of observation. The biochemical changes portrayed an increased oxidative activity in the lens, evidenced by a fall in glutathione concentration, and the consequent tertiary reorientation of proteins to increase insoluble proteins, forming a cataract.

Animals↗