PMID: 9421743Jan 9, 1998Paper

Protein glycosylation in rat fibroblast cells expressing deletion variants of the human hsp70 gene

International Journal of Hyperthermia : the Official Journal of European Society for Hyperthermic Oncology, North American Hyperthermia Group
K J HenleG C Li

Abstract

Elevated heat resistance is often associated with high cellular levels of hsp70. In the rat cell line, M21, increased heat resistance is associated with both the expression of an intact exogenous human hsp70 gene, and of an exogenous stress glycoprotein, GP62. In this study, we examined heat-stress induced alterations in protein glycosylation in two variant lines of M21 that contain specific deletions in the exogenous human hsp70 gene. The deletion mutant, MVH delta Sm, lacks the nucleolar localization sequence for human hsp70 gene, whereas the other mutant, MVH delta Bg, is characterized by deletion of the ATP binding domain in the human hsp70 gene. After heat induction, the MVH delta Sm mutants exhibited constitutive and heat-induced endogenous hsp70 mRNA levels, protein glycosylation, as well as hsp70 and GP62 protein levels comparable to those in the parent cell line, Rat-1. Cellular heat sensitivity of MVH delta Sm mutants was also similar to that of Rat-1 cells, although the mutant cells had a reduced capacity for thermotolerance development. On the other hand, MVH delta Bg mutants before thermotolerance induction, exhibited constitutive endogenous and human exogenous hsp70 mRNA levels similar to those in MVH delta Sm mut...Continue Reading

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