Vince Guerriero
Associate Professor
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Regulation of Chaperone Activity
All eukaryotic cells have a group of proteins called chaperones (also known as heat stress proteins, Hsps) that provide protection from various environmental stresses such as elevated temperatures, exposure to heavy metals, and hypoxia. The levels of these proteins increase when cells are exposed to stresses and the increased levels help the cells survive. The most studied has a molecular weight of 70 kDA and is therefore called Hsp70. Understanding the role of other proteins that can regulate Hsp70 is the main focus of research in my laboratory. An Hsp70 binding protein called HspBP1 has been identified and characterized. The three-dimensional structure of HspBP1 and HspBP1 complexed to Hsp70 has been solved. This resulting structure has provided insight into the mechanism of HspBP1 regulation of Hsp70 activity. Recent studies have shown that HspBP1 is both an intracellular and extracellular protein. A possible mechanism for HspBP1 secretion has been identified along with the regulation of the EGFR by HspBP1 . Further studies have shown that HspBP1 is elevated in numerous cancer cells including human breast cancer. In addition, patients with breast have elevated levels of HspBP1 in their serum. These studies have identified a novel Hsp70 binding protein and characterized the mechanism of Hsp70 regulation. In addition, HspBP1 could be a candidate for a cancer biomarker.
All eukaryotic cells have a group of proteins called chaperones (also known as heat stress proteins, Hsps) that provide protection from various environmental stresses such as elevated temperatures, exposure to heavy metals, and hypoxia. The levels of these proteins increase when cells are exposed to stresses and the increased levels help the cells survive. The most studied has a molecular weight of 70 kDA and is therefore called Hsp70. Understanding the role of other proteins that can regulate Hsp70 is the main focus of research in my laboratory. An Hsp70 binding protein called HspBP1 has been identified and characterized. The three-dimensional structure of HspBP1 and HspBP1 complexed to Hsp70 has been solved. This resulting structure has provided insight into the mechanism of HspBP1 regulation of Hsp70 activity. Recent studies have shown that HspBP1 is both an intracellular and extracellular protein. A possible mechanism for HspBP1 secretion has been identified along with the regulation of the EGFR by HspBP1 . Further studies have shown that HspBP1 is elevated in numerous cancer cells including human breast cancer. In addition, patients with breast have elevated levels of HspBP1 in their serum. These studies have identified a novel Hsp70 binding protein and characterized the mechanism of Hsp70 regulation. In addition, HspBP1 could be a candidate for a cancer biomarker.
Selected Publications
Souza AP, Albuquerque C, Torronteguy C, Frasson A, Maito F, Pereira L, Duval da Silva V, Zerwes F, Raynes D, Guerriero V, Bonorino C. Nov 2008. HspBP1 levels are elevated in breast tumor tissue and inversely related to tumor aggressiveness. Cell Stress Chaperones,2008 Nov 6;
Evdonin AL, Kinev AV, Tsupkina N, Guerriero V, Raynes DA, Medvedeva ND. Nov 2008. Extracellular HspBP1 and Hsp72 synergistically activate EGF receptor. Biol Cell,2008 Nov 5;
Raynes DA Thomson CA Stroster J Newton T Cuneo P Guerriero V. Jan 2006. Human serum contains detectable levels of the Hsp70 cochaperone HspBP1 and antibodies bound to HspBP1. J Immunoassay Immunochem, 27:251-64
Gottwald, E., Herschbach, M., Lahni, B., Miesfeld, R.L., Kunz, S. Raynes, D.A., Guerriero, V.. Dec 2006. Expression of the Cochaperone HspBP1 is not Coordinately Regulated with Hsp70 Expression. Internat. J. Cell Biol., 30:553-558