Glycosylation of stress glycoprotein GP62 in cells exposed to heat-shock and subculturing

Glycoconj J. 1999 Nov;16(11):685-9. doi: 10.1023/a:1007151208144.

Abstract

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.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Blotting, Western
  • Carbohydrates / chemistry
  • Cell Culture Techniques / methods
  • Glycoproteins / chemistry*
  • Glycoproteins / metabolism
  • Glycosylation / radiation effects
  • Heat-Shock Proteins / chemistry
  • Heat-Shock Proteins / metabolism*
  • Heat-Shock Response / physiology*
  • Humans
  • Lectins / metabolism
  • Tumor Cells, Cultured
  • Ultraviolet Rays

Substances

  • Carbohydrates
  • Glycoproteins
  • Heat-Shock Proteins
  • Lectins