Formation of mannosyl-lipids by an ectomannosyltransferase in suspensions of BALB/c fibroblasts.
A mannosyltransferase has been detected in suspensions of BALB/c fibroblasts incubated with GDP-[14C] mannose. The experimental evidence indicates the cell surface as the most likely site for the enzyme. The transferase synthesizes both glycolipids and glycoproteins. The lipid compounds have properties suggestive of lipid-linked mono- and oligosaccharides which can function as intermediates in glycoprotein synthesis. The formation of these compounds by a cell surface enzyme suggests that lipid-linked intermediates may play an important role in the glycosylation of membrane components.
D000249:Adenosine Monophosphate / Q000378:metabolism; D005347:Fibroblasts / Q000378:metabolism*; D006017:Glycolipids / Q000096:biosynthesis*; D006023:Glycoproteins / Q000096:biosynthesis; D006155:Guanosine Diphosphate Mannose / Q000378:metabolism; D006602:Hexosyltransferases / Q000378:metabolism*; D007700:Kinetics; D008364:Mannosyltransferases / Q000378:metabolism*; D008970:Molecular Weight; D009844:Oligosaccharides / Q000032:analysis; D011402:Pronase
D006017:Glycolipids; D006023:Glycoproteins; D009844:Oligosaccharides; D006155:Guanosine Diphosphate Mannose; D000249:Adenosine Monophosphate; D006602:Hexosyltransferases; D008364:Mannosyltransferases; D011402:Pronase