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R C Tripathi

Publications and source records attributed to R C Tripathi.

At least 55 records · Page 3Linked to original sources
PubMed1992

Identification and quantification of transferrin receptors on trabecular cells.

The authors identified and quantified the receptor for transferrin on trabecular meshwork (TM) cells cultured from porcine eyes by using two receptor assays. Flow-cytometric analysis of TM cells that were incubated with a monoclonal antibody to the transferrin receptor revealed such receptors, which decreased in number as the cells passed from the pre- to the post-confluent phase. Quantitative characterization by radioligand binding of 125I-transferrin to trabecular cells followed by Scatchard analysis showed that pre-confluent cultures expressed 23,839 +/- 6746 high-affinity receptors/cell and post-confluent cultures expressed 5104 +/- 3639 receptors/cell. The expression of the receptor for transferrin reflects the index of mitotic activity and can be correlated with the proliferative state of the trabecular cells. Further characterization of the receptors for transferrin in the TM may open up the possibility of a pharmacologic approach that enhances the TM cell population, which is known to decrease with age and in glaucomatous states of the eye.

Animals↗
PubMed1992

Quantitative and qualitative analyses of transferrin in aqueous humor from patients with primary and secondary glaucomas.

By using a highly sensitive and specific radioimmunoassay and the slot-blot technique, transferrin was quantified in fresh samples of aqueous humor from patients with primary open-angle glaucoma (POAG, n = 36) or secondary glaucoma (SG, n = 18). The levels were compared with those in aqueous humor obtained from age-matched patients without glaucoma (n = 33) and in primary and secondary aqueous humor from normal dogs (n = 10) in which breakdown of the blood-aqueous barrier was induced experimentally. The concentration of transferrin in the aqueous humor of human control subjects ranged from 0.3-3.4 mg/dl (mean +/- standard deviation, 1.36 +/- 0.66 mg/dl); in POAG samples, from 0.34 to greater than 10 mg/dl (2.07 +/- 1.90 mg/dl); and in SG samples, from 0.29 to greater than 10 mg/dl (2.79 +/- 2.24 mg/dl). The level of transferrin in secondary aqueous humor samples obtained from dogs was as much as ninefold greater than that in primary aqueous humor. The protein concentration in the human aqueous humor samples was 11.87 +/- 4.47 mg/dl for control subjects, 62.11 +/- 56.74 mg/dl for patients with POAG, and 124.53 +/- 152.67 mg/dl for those with SG. In dogs, the protein levels were 7.97 +/- 3.12 mg/dl for primary aqueous humor and 191.9 +/- 149.8 mg/dl for secondary aqueous humor. A significant correlation (r = 0.744, P less than 0.01) was found between total protein and transferrin contents in the samples of aqueous humor from patients with glaucoma but not in the samples from age-matched control subjects.(ABSTRACT TRUNCATED AT 250 WORDS)

Adult↗
PubMed1992

Analysis of glycoprotein deposits on disposable soft contact lenses.

By using gel electrophoresis, as well as Western blotting with specific antibodies or with the lectin concanavalin A, we characterized the types and amounts of proteins that are deposited on 58% ionic and 38% nonionic water-content disposable soft contact lenses (DSCLs) worn for 1 to 21 days by asymptomatic subjects with mild to moderate myopic refractive errors. The total amounts of protein eluted from the lenses ranged from 0.1 to 80 micrograms/lens. The amount of protein deposited on 58% water-content lenses was greater than that on 38% water-content DSCLs. We did not find a strict correlation between the amount of protein deposited and the duration of wear for either type of lens. The major polypeptide fractions detected had apparent molecular weights of 14, 17, 21, 30, and 60 kD. The fractions at 14 kD-bound antibodies specific for human lysozyme, and those at 17 kD corresponded to prealbumin. The 60 kD fraction included IgG heavy chains. The identity of the fractions at 21 kD and 30 kD is unknown. Because oligosaccharide side chains on the proteins attract microbes and facilitate their adherence, knowledge about the types of carbohydrate moieties in lens deposits can provide a rational approach to inhibiting or reversing microbial infection.

Blotting, Western↗
PubMed1991

The role of growth factors in the embryogenesis and differentiation of the eye.

The vertebrate eye is composed of a variety of tissues that, embryonically, have their derivation from surface ectoderm, neural ectoderm, neural crest, and mesodermal mesenchyme. During development, these different types of cells are subjected to complex processes of induction and suppressive interactions that bring about their final differentiation and arrangement in the fully formed eye. With the changing concept of ocular development, we present a new perspective on the control of morphogenesis at the cellular and molecular levels by growth factors that include fibroblast growth factors, epidermal growth factor, nerve growth factor, platelet-derived growth factor, transforming growth factors, mesodermal growth factors, transferrin, tumor necrosis factor, neuronotrophic factors, angiogenic factors, and antiangiogenic factors. Growth factors, especially transforming growth factor-beta, have a crucial role in directing the migration and developmental patterns of the cranial neural-crest cells that contribute extensively to the structures of the eye. Some growth factors also exert an effect on the developing ocular tissues by influencing the synthesis and degradation of the extracellular matrix. The mRNAs for the growth factors that are involved in the earliest aspects of the growth and differentiation of the fertilized egg are supplied from maternal sources until embryonic tissues are able to synthesize them. Subsequently, the developing eye tissues are exposed to both endogenous and exogenous growth factors that are derived from nonocular tissues as well as from embryonic fluids and the systemic circulation. The early interaction between the surface head ectoderm and the underlying chordamesoderm confers a lens-forming bias on the ectoderm; later, the optic vesicle elicits the final phase of determination and enhances differentiation by the lens. After the blood-ocular barrier is established, the internal milieu of the eye is controlled by the interactions among the intraocular tissues; only those growth factors that selectively cross the barrier or that are synthesized by the ocular tissues can influence further development and differentiation of the cells. An understanding of the tissue interactions that are regulated by growth factors could clarify the precise mechanism of normal and abnormal ocular development.

Animals↗
PubMed1991

Radioimmunoassay of epidermal growth factor in human lenses at various stages of development of cataract.

By using a highly specific and sensitive homologous radioimmunoassay, we found that the content of epidermal growth factor (EGF) in the lateral one-third of whole cataractous human lenses (age range 45-85 yr) extracted at elective intracapsular lens surgery, varied from undetectable to 106.25 pg mg-1 water soluble protein (WSP) (mean +/- S.D. = 39.70 +/- 38.90). When the lenses were grouped according to the stage of the cataract, i.e. immature (n = 3), mature (n = 4), and hypermature (n = 3), the means +/- S.D. were 92.56 +/- 26.23, 23.89 +/- 7.71, and 7.92 +/- 2.00 pg mg-1 WSP, respectively. In ten age-matched whole 'normal' lenses that we removed within 2-12 hr after death, the values in EGF of the lateral one-third of the lenses ranged from 2.91 to 36.40 pg mg-1 WSP (19.39 +/- 13.65). No correlation between the age of the lenses and the content of EGF could be demonstrated at the 95% confidence interval for the cataractous and 'normal' lenses. The quantity of endogenous EGF correlated significantly (P less than 0.01) with the clinical stage of the cataract and is probably related to the mitotic activity of the equatorial proliferative zone. We discuss the importance of EGF in normal and cataractous lenses and postulate that EGF in the lens is endogenous in origin.

Aged↗
PubMed1991

Mapping of Fc gamma receptors in the human and porcine eye.

By using an immunohistochemical technique, we detected a strong reaction product for Fc gamma receptors in the keratoconjunctival epithelium, uveal trabecular meshwork, optic nerve, and muscle walls of the retinal and ciliary vessels of infant human eyes; moderate staining was seen on the corneal endothelium, corneoscleral trabecular meshwork, non-pigmented ciliary epithelium, ciliary muscle fibers, endothelial lining of ocular blood vessels, as well as the anterior region of Muller cells, the outer nuclear layer, and pigment epithelium of the retina. In aged human and porcine eyes, the same structures stained somewhat less intensely than did those in infant human tissues. Primary cultures of porcine trabecular cells demonstrated a more intense immunoreaction product than did tertiary cultures. We discuss the possible role of Fc gamma receptors in various ocular inflammatory conditions and the implications of age-dependent expression by human trabecular cells in the pathogenesis of open-angle glaucoma.

Aged↗
PubMed1991

Intraocular pressure increases with fenoldopam, but not nitroprusside, in hypertensive humans.

Fenoldopam mesylate stimulates adenyl cyclase in porcine ocular trabecular meshwork and raises intraocular pressure in humans. To clarify whether this results from direct activation of the dopamine-1 receptor or indirectly from baroreflex sympathetic stimulation after blood pressure reduction, intraocular pressure was measured in 14 patients with accelerated/malignant hypertension, randomized between intravenous fenoldopam or sodium nitroprusside. Intraocular pressure was measured with a Perkins tonometer, before and at the twentieth minute of each dose increment. In seven patients with a mean blood pressure of 232/131 mm Hg treated with fenoldopam, intraocular pressure increased in a dose-dependent fashion, from 16 +/- 1 to 20 +/- 2 mm Hg (p less than 0.005). In contrast, seven patients with a mean blood pressure of 225/134 mm Hg treated with sodium nitroprusside exhibited no change in intraocular pressure (15 +/- 1 versus 14 +/- 1 mm Hg) despite similar blood pressure reduction. Increases in heart rate were not significantly different. Rates of urinary excretion of norepinephrine plus epinephrine increased significantly relative to baseline (p less than 0.05) but were not different between groups. These data suggest that the increase in intraocular pressure with fenoldopam results from specific activation of the dopamine-1 receptor and is not caused by baroreflex sympathetic stimulation. Because dopamine-1 receptors may modulate intraocular pressure, dopamine-1 receptor blockers might be useful therapy for glaucoma.

2,3,4,5-Tetrahydro-7,8-dihydroxy-1-phenyl-1H-3-ben↗
PubMed1991

Synthesis of a thrombospondin-like cytoadhesion molecule by cells of the trabecular meshwork.

Thrombospondin is a large extracellular-matrix protein that is released by smooth muscle cells and platelets and is distributed widely in mammalian brain. By using western blotting with a monoclonal antibody against the calcium-binding domain of thrombospondin, the authors detected a 180-kD glycated polypeptide in the trabecular meshwork tissue of normal human and porcine eyes. The epitope-bearing polypeptide was soluble in sodium dodecylsulfate/urea (SDS/urea), and apparently it was stabilized in part by disulfide bonding to the Triton X-100 and SDS/urea-insoluble pellet of this tissue. Treatment of the insoluble matrix with beta-mercaptoethanol led to an enriched extraction of the approximately 160-kD form of thrombospondin. On immunohistochemical study, the thrombospondin antibody also reacted positively with the extracellular matrix and intracellular structures of trabecular cells in primary monolayer culture. This suggested that the presence of thrombospondin in the trabecular meshwork was probably due to local synthesis. These findings are relevant to the establishment of a model in vitro for assessment of adhesion of trabecular cells. Because thrombospondin is a cell-substrate adhesion molecule, its role in the loss of cellularity that occurs in the trabecular meshwork of the aging eye and in eyes with primary open-angle glaucoma is worthy of further investigation.

Adult↗
PubMed1991

Rodent models of congenital and hereditary cataract in man.

Because the organogenesis and physiology of the lens are essentially similar in various mammals, an understanding of the etiology and pathogenesis of the formation of cataract in an animal model will enhance our knowledge of cataractogenesis in man. In this review, we summarize the background, etiology, and pathogenesis of cataracts that occur in rodents. The main advantages of using rodent mutants include the well-researched genetics of the animals and the comparative ease of breeding of large litters. Numerous rodent models of congenital and hereditary cataracts have been studied extensively. In mice, the models include the Cts strain, Fraser mouse, lens opacity gene (Lop) strain, Lop-2 and Lop-3 strains, Philly mouse, Nakano mouse, Nop strain, Deer mouse, Emory mouse, Swiss Webster strain, Balb/c-nct/nct mouse, and SAM-R/3 strain. The rat models include BUdR, ICR, Sprague-Dawley, and Wistar rats, the spontaneously hypertensive rat (SHR), the John Rapp inbred strain of Dahl salt-sensitive rat, as well as WBN/Kob, Royal College of Surgeons (RCS), and Brown-Norway rats. Other proposed models for the study of hereditary cataract include the degu and the guinea pig. Because of the ease of making clinical observations in vivo and the subsequent availability of the intact lens for laboratory analyses at different stages of cataract formation, these animals provide excellent models for clinicopathologic correlations, for monitoring of the natural history of the aging process and of metabolic defects, as well as for investigations on the effect of cataract-modulating agents and drugs, including the prospect of gene therapy.

Animals↗
PubMed1991

A direct correlation of the resolution of pseudophakic cystoid macular edema with acetazolamide therapy.

We report the case of a patient with pseudophakic cystoid macular edema whose visual acuity improved promptly with oral administration of 500 mg of acetazolamide extended-release capsules BID for two weeks. However, vision worsened again within two weeks of discontinuation of the treatment. On resumption of acetazolamide therapy for three weeks, and its slow withdrawal during the following three weeks, the macular edema eventually resolved, and vision returned to normal. Our observation provides a direct correlation of the resolution of pseudophakic cystoid macular edema with acetazolamide therapy and shows the importance of tapering the doses of this regimen.

Acetazolamide↗
PubMed1990

Expression of HLA by the human trabecular meshwork and corneal endothelium.

By using immunohistochemical techniques, we demonstrated that HLA class I (A, B and C) and HLA class II (DR), the major histocompatibility antigens in man, are expressed constitutively by cells of the trabecular meshwork/Schlemm's canal system and corneal endothelium, as well as by the conjunctival epithelium, Langerhans cells, vascular endothelium and uvea. Because clinical studies indicate that these antigens are involved in mediating corneal graft rejection and possibly in glaucomatous disease of the eye, the presence of both class I and II HLA in the corneal endothelium and in the trabecular cells has important implications for an understanding of immune disorders in the anterior segment of the eye. The presence of HLA on trabecular cells raises the possibility that these antigens potentiate the recognized role of Langerhans cells at the limbus and that they participate in, and/or regulate, the maintenance and defense of the aqueous outflow pathway. Our findings also open up the possibility of using HLA as a genetic marker in the determination of susceptibility to these disorders in man.

Adult↗
PubMed1990

Tau fraction of transferrin is present in human aqueous humor and is not unique to cerebrospinal fluid.

In view of the many similarities between the aqueous humor and the cerebrospinal fluid (CSF), we investigated whether the tau fraction of transferrin, which is believed to be specific for CSF, is also present in aqueous humor. Samples of aqueous humor and CSF from clinically normal individuals were analyzed by SDS-PAGE and isoelectric focusing (IEF), and probed with anti-transferrin antiserum and the lectin Limax flavus agglutinin. Specific bands which corresponded to transferrin and its tau fraction were detected in both fluids. After isolation of these bands by affinity chromatography with anti-transferrin antiserum, we detected a single, diffuse fraction at an apparent molecular weight of 80 kDa in both aqueous humor and CSF. Peptide mapping revealed no detectable difference in this fraction between the two fluids. The detection of the tau fraction in human aqueous humor indicates that this molecule cannot be considered a specific cerebrogenic marker as had been thought previously. In view of the known growth-promoting properties of transferrin, its isolation from both ocular and cranial fluids attains special significance.

Aged↗