Glycosylation of stress glycoprotein GP62 in cells exposed to heat-shock and subculturing.
GP62 is a member of the stress glycoprotein family that was proposed to have a chaperone-like function in the heat-shock response. Using lectin blotting we have studied glycosylation of GP62 and determined that in addition to heat-shock, even simple subculturing of cells is a sufficient stimulus to provoke induction of GP62. Interestingly, both kinetics of induction and glycosylation of GP62 induced by subculturing were different than when GP62 was induced by heat-shock. While GP62 induced by heat-shock was recognized by SNA, DSA and PHA-E lectins, and not by BSA I, Con A, RCA I, SJA, UEA I, VVA, and WGA lectins, GP62 induced by subculturing was also recognized by RCA I and WGA lectins.
Dumić
J
J
Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and Biochemistry, University of Zagreb, Croatia.
Lauc
G
G
Flögel
M
M
D015153:Blotting, Western; D002241:Carbohydrates / Q000737:chemistry; D018929:Cell Culture Techniques / Q000379:methods; D006023:Glycoproteins / Q000737:chemistry* / Q000378:metabolism; D006031:Glycosylation / Q000528:radiation effects; D006360:Heat-Shock Proteins / Q000737:chemistry / Q000378:metabolism*; D018869:Heat-Shock Response / Q000502:physiology*; D006801:Humans; D037102:Lectins / Q000378:metabolism; D014407:Tumor Cells, Cultured; D014466:Ultraviolet Rays
D002241:Carbohydrates; D006023:Glycoproteins; D006360:Heat-Shock Proteins; D037102:Lectins