Comparison of tumor growth between hsp25- and hsp27-transfected murine L929 cells in nude mice.

Abstract

We have developed a novel system for examining the possible contribution of small heat shock proteins (hsp) to tumor growth. L929 fibrosarcoma cells, which do not express significant levels of endogenous hsp25, were stably transfected with either murine hsp25 or human hsp27. Both transfected genes were over-expressed and the respective proteins were phosphorylated in L929 cells. L929 cells transfected with hsp25 exhibited enhanced tumor growth compared to control transfected L929 cells upon s.c. injection into nude mice. In contrast, cells transfected with hsp27 exhibited delayed tumor progression in comparison to controls. Although these 2 heat shock genes and respective proteins are structurally very similar, they apparently exhibit distinct effects on tumor growth in this system.

• Authors: R V Blackburn, S S Galoforo, C M Berns, E P Armour, D McEachern, P M Corry, Y J Lee
• Journal: International journal of cancer. Journal international du cancer (Int J Cancer) Vol. 72 Issue 5 Pg. 871-7 (Sep 4 1997) ISSN: 0020-7136 [Print] UNITED STATES
• PMID: 9311607 (Publication Type: Comparative Study, Journal Article, Research Support, Non-U.S. Gov't, Research Support, U.S. Gov't, P.H.S.)

Chemical References

• HSP27 Heat-Shock Proteins
• HSPB1 protein, human
• Heat-Shock Proteins
• Hspb1 protein, mouse
• Intracellular Signaling Peptides and Proteins
• Neoplasm Proteins
• MAP-kinase-activated kinase 2
• Protein-Serine-Threonine Kinases

Topics

• Animals
• Blotting, Western
• Electrophoresis, Polyacrylamide Gel
• Fibrosarcoma (genetics, metabolism)
• HSP27 Heat-Shock Proteins
• Heat-Shock Proteins (genetics, metabolism, physiology)
• Humans
• Intracellular Signaling Peptides and Proteins
• Mice
• Mice, Nude
• Neoplasm Proteins (genetics, metabolism, physiology)
• Neoplasm Transplantation
• Phosphorylation
• Protein-Serine-Threonine Kinases (genetics, metabolism, physiology)
• Transfection
• Tumor Cells, Cultured