Dumić J, Lauc G, Flögel M
Department of Biochemistry and Molecular Biology, Faculty of Pharmacy and Biochemistry, University of Zagreb, Croatia.
Glycoconj J. 1999 Nov;16(11):685-9. doi: 10.1023/a:1007151208144.
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.
GP62是应激糖蛋白家族的成员，有人提出它在热休克反应中具有类似伴侣蛋白的功能。我们利用凝集素印迹法研究了GP62的糖基化，并确定除了热休克外，即使是简单的细胞传代培养也足以刺激GP62的诱导。有趣的是，传代培养诱导的GP62的诱导动力学和糖基化与热休克诱导时不同。热休克诱导的GP62可被SNA、DSA和PHA-E凝集素识别，而不被BSA I、Con A、RCA I、SJA、UEA I、VVA和WGA凝集素识别，传代培养诱导的GP62也可被RCA I和WGA凝集素识别。
