Study of the interaction between germ cells and Sertoli cells in vitro.
The nature of membrane components involved in the binding between Sertoli cells and pachytene spermatocytes in culture and the metabolic requirements for the binding to occur have been studied. Mild proteolytic digestion of germ cells by trypsin completely inhibited adhesion of germ cells to somatic monolayer. Protein synthesis and glycosylation were required to restore the adhesive properties of trypsin-treated germ cells, showing that surface molecules involved in the binding are glycoproteins. Trypsinization of germ cells after labelling causes a great reduction of several bands which become detectable again after 12 h of recovery from trypsin digestion. Among these, two bands with apparent molecular weight (MW) of 78 000 and 51 000 could be candidate components in cell adhesion.
D000818:Animals; D002448:Cell Adhesion; D002450:Cell Communication; D005944:Glucosamine / Q000378:metabolism; D006023:Glycoproteins / Q000502:physiology*; D008297:Male; D008565:Membrane Proteins / Q000502:physiology*; D010447:Peptide Hydrolases / Q000494:pharmacology; D014176:Protein Biosynthesis; D012313:RNA / Q000096:biosynthesis; D051381:Rats; D012708:Sertoli Cells / Q000502:physiology*; D013090:Spermatocytes / Q000378:metabolism / Q000502:physiology*; D013094:Spermatozoa / Q000502:physiology*
D006023:Glycoproteins; D008565:Membrane Proteins; D012313:RNA; D010447:Peptide Hydrolases; D005944:Glucosamine