Synthesis and localization of two sulphated glycoproteins associated with basement membranes and the extracellular matrix.

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Abstract
Two sulfated glycoproteins (sgps) of apparent MW 180,000 and 150,000, are synthesized by murine PYS and PF HR9 [teratocarcinoma-derived] parietal endoderm and Swiss 3T3 [fibroblast] cells. The MW 150,000 sgp has a similar chemical structure to the sulfated glycoprotein, C, synthesized and laid down in Reichert''s membrane by mouse embryo parietal endoderm cells. Both the MW 180,000 and 150,000 sgps are deposited in the detergent-insoluble matrix of cultured cells, but they do not apparently undergo any disulfide-dependent intermolecular interactions and are not precursors or products of each other. They contain asparagine-linked oligosaccharides, but these are not the exclusive sites of sulfate labeling. Antiserum raised against the MW 150,000 sgp C of Reichert''s membranes was used in an immunohistochemical analysis of rat skin. In early fetal and adult skin the antigen is present only in basement membranes, but transiently before and after birth it is also found throughout the upper part of the dermis. This suggests that 150,000 sgp C is at times synthesized by nonepithelial cells and contributes to the extracellular matrix of mesenchymal tissues.