Localization of clusterin in the epimembranous deposits of passive Heymann nephritis

Localization of clusterin in the epimembranous deposits of passive Heymann nephritis. The membrane attack complex of complement (MAC) plays an important role in the mediation of proteinuria in experimental membranous nephropathy induced by Heymann antiserum. SP-40,40 is a recently described serum protein which appears to inhibit the formation of cytolytic MAC in a manner analogous to S protein/vitronectin. SP-40,40 is homologous to proteins originally isolated from rat and ram seminal fluid (sulfated glycoprotein 2 and clusterin, respectively). By current convention, these proteins are considered clusterin homologues. The objective of this study was to examine the participation of rat clusterin in passive Heymann nephritis. Using an antibody to rat clusterin as an immunofluorescent probe, clusterin deposits were demonstrated along the glomerular capillary wall in an identical pattern to rat C3 and C5b-9. Decomplementation using cobra venom factor prevented proteinuria and intraglomerular MAC formation. The epimembranous clusterin were not detected in the complement-depleted animals. The role of clusterin in the mediation of glomerular injury remains unknown, but it is probably related to in situ formation of the terminal complement cascade where it may play a regulatory role

Relief of palmityl CoA inhibition of citrate synthase by long-chain acylcarnitine derivatives

Inhibition of citrate synthase by incubation with palmityl CoA could be in large part prevented by concomitant incubation of enzyme with (+)-palmitylcarnitine, (-)-palmitylcarnitine or DL-stearylcarnitine. DL-Octanylcarnitine was less effective while butyrylcarnitine was without any protective action. The molar ratio of palmitylcarnitine to palmityl CoA required for relief of palmityl CoA inhibition was lowered at elevated concentrations of albumin.Peer Reviewedhttp://deepblue.lib.umich.edu/bitstream/2027.42/33467/1/0000871.pd

Fibronectin Synthesis is a Marker for Peritubular Cell Contaminants in Sertoli Cell-Enriched Cultures

With indirect immunofluorescent microscopic techniques, we have shown that fibronectin is distributed primarily in or along the basal lamina of the seminiferous tubule boundary tissue in sections of testes from 20-day-old rats. Purified rat Sertoli cell-enriched aggregates, maintained in culture in the presence or absence of serum, exhibit no detectable immunofluorescence with fibronectin antibody, whereas purified peritubular cells in culture do have a positive reaction to fibronectin antibody. Peritubular cells in culture incorporate [35S] methionine into fibronectin which can be immunoprecipitated with a fibronectin antiserum, but Sertoli cells do not. We have used various criteria to estimate the degree of purity of Sertoli cell-enriched preparations. The presence of peritubular myoid cells in conventional Sertoli cell-enriched aggregates, cultured in the presence or absence of serum, can be detected with transmission electron microscopic examination, by the Feulgen staining procedure, and by the immunocytochemical identification of fibronectin. We describe a technique to purify Sertoli cells in conventional Sertoli cell-enriched preparations by treatment with hyaluronidase, resulting in a lesser number of peritubular cells by the above criteria, even in preparations cultured in the presence of serum. Data presented suggest that some of the products previously attributed exclusively to Sertoli cells in Sertoli cell-enriched preparations, particularly those cultured in the presence of serum, may have been contributed by peritubular cells