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W S Argraves

Publications and source records attributed to W S Argraves.

77 records · Page 5Linked to original sources
PubMed1985

Primary structure of the telopeptide and a portion of the helical domain of chicken type II procollagen as determined by DNA sequence analysis.

A comparison of the nucleotide sequences of three new cDNA clones for chicken type II procollagen with the sequences of the other three types of chicken fibrillar procollagens reveals that the most conserved regions correlate with the positions of hydroxyproline, hydroxylysine, cysteine and lysine residues. On the basis of replacement-site-divergence calculations it is concluded that alpha 1(II) and alpha 1(I) procollagens diverged later than alpha 1(I) and alpha 2(I) procollagens.

Amino Acid Sequence↗
PubMedDate not supplied

Cellular interactions with fibronectin as a model for redundant binding of cells to other extracellular matrix proteins.

Perhaps the most studied property of fibronectin (Fn) is its ability to bind to cells. Interestingly, there are multiple mechanisms by which cells can bind Fn involving as many as ten different cell surface molecules and perhaps six distinct sites within Fn. This apparent redundant binding system is not only restricted to Fn since cells bind other extracellular matrix proteins such as laminin, vitronectin and fibrinogen in a similar manner. The many binding interactions between cells and Fn may serve as a model for understanding redundant binding between cells and other matrix proteins.

Animals↗
PubMedDate not supplied

Immunological localization of glycoprotein 330, low density lipoprotein receptor related protein and 39 kDa receptor associated protein in embryonic mouse tissues.

In this study we have immunologically examined the expression of the structurally and functionally related receptors, LRP and gp330, and their associated 39 kDa protein (RAP) in tissues of the embryonic mouse. One aim was to determine whether these proteins were coordinantly expressed. The data reveals that gp330 is expressed on the apical surfaces of many specialized absorptive epithelia most prominently, choroid plexus, ependyma, metanephric tubules, ear, thyroid, pericardium, and intestine. LRP was detected in all epithelia expressing gp330 with the exception of the epicardium and metanephric tubule epithelium. However, the subcellular pattern of LRP deposition in polarized epithelium was distinct from the apical pattern of gp330, perhaps indicating that LRP was either sequestered intracellularly or distributed basolaterally. The pattern of LRP expression in tissues of the mouse embryo was however much wider than that of gp330. Prominent expression of LRP was observed in skin, myocardium, mesenchyme, liver, pancreas, and marginal regions of the brain. In the developing liver, LRP was not detected in day 10.5 but was detected in megacaryocyte-like cells of 12.5 day and in hepatocytes of 14.5 day embryonic liver. RAP was observed to be coexpressed with either or both of the receptors but its subcellular pattern of distribution coincided with that of LRP. The coexpression of gp330 and LRP in epithelial cells and the observation that gp330 staining was always localized apically while LRP was distributed basolaterally or sequestered intracellularly suggests that these receptors have distinct functions in polarized epithelial cells.

Animals↗
PubMedDate not supplied

Low density lipoprotein receptor-related protein-1 expression in the testis: regulated expression in Sertoli cells.

The low density lipoprotein receptor-related protein (LRP-1) is a multiligand receptor capable of mediating endocytosis of a wide array of ligands that relate to both lipoprotein metabolism and proteinase regulation. Many of its ligands are proteinases, proteinase-inhibitor complexes, and lipoproteins known to be contained within the luminal fluid of the seminiferous tubules or in the interstitial spaces of the testis. Immunocytochemical analysis was performed to characterize the pattern of expression of LRP-1 in cells of the rat testis. Immunoperoxidase staining localized LRP-1 to the cytoplasm of Sertoli cells. The distribution and intensity of the Sertoli cell staining was found to vary according to the stages of the cycle of the seminiferous epithelium. Staining was weak in the basal cytoplasm of Sertoli cells during stages II-VIII and strong and granular in the supranuclear cytoplasm during stages XII-XIV and stage I of the cycle. Immunogold labeling showed gold particles associated with the basal and adluminal plasma membranes, with endocytic vesicles, and with endosome membranes. Labeling was also observed on the plasma membrane and membranes of the endocytic apparatus in macrophages and Leydig cells in the interstitial space. Infusion of 125I-Labeled LRP-1 antibody into seminiferous tubules followed by radioautography showed silver grains overlaying the ad-luminal plasma membrane of Sertoli cells at time 0 and in endocytic vesicles and endosomes in the supranuclear region of Sertoli cells 10-minutes postinjection. When the 125I-Labeled LRP-1 antibody was injected into the interstitial space, silver grains overlayed the basal plasma membrane and coated endocytic pits of Sertoli cells at time 0 and, at 10 minutes, the grains labeled endosomes located in the basal pole of Sertoli cells. 125I-Labeled LRP-1 antibody also labeled the plasma membrane and the endocytic apparatus of macrophages and Leydig cells. The absence of immunogold labeling and radioautographic silver grains within lysosomes of Sertoli cells, Leydig cells, and macrophages suggests that internalized LRP-1 is recycled back to the cell surface. The presence of LRP-1 in the endocytic compartment of these cells is consistent with its functioning in the clearance of proteases involved in seminiferous tubule remodeling and/ or the uptake of cholesterol-bound lipoproteins necessary for the biosynthesis of testosterone. In conclusion, the results of these studies demonstrated for the first time the presence of LRP-1 receptor in the endocytic compartments of Sertoli cells and interstitial cells of the rat testis.

Animals↗