Post-translational modification of the beta-subunit of the human fibronectin receptor.
Monoclonal antibody DH12, directed against the beta-subunit of the fibronectin receptor recognizes a doublet of proteins (100 and 110 kDa) in Western blots of solubilized whole fibroblasts. Pulse-chase experiments with [35S]methionine in human skin fibroblasts suggested that the two proteins might be metabolically related as precursor (100 kDa) and product (110 kDa). Endo H digestion and [3H]fucose labeling suggested that maturation converted the high-mannose oligosaccharides (100 kDa) to the endoglycosidase H resistant complex type (110 kDa). This was supported by N-glycanase digestion and by chemical deglycosylation which showed a single polypeptide. Surface iodination of intact cells labeled only the presumed mature beta-subunit.
Jaspers
M
M
Center for Human Genetics, University of Leuven, Campus Gasthuisberg, Belgium.
de Strooper
B
B
Spaepen
M
M
van Leuven
F
F
David
G
G
van den Berghe
H
H
Cassiman
J J
JJ
D000911:Antibodies, Monoclonal / Q000276:immunology; D006023:Glycoproteins / Q000378:metabolism; D006801:Humans; D011498:Protein Precursors / Q000378:metabolism; D011499:Protein Processing, Post-Translational; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic / Q000276:immunology / Q000378:metabolism*
D000911:Antibodies, Monoclonal; D006023:Glycoproteins; D011498:Protein Precursors; D017469:Receptors, Fibronectin; D011971:Receptors, Immunologic