Vince Guerriero
Associate Professor
Office: Shantz 232
Primary Phone: (520) 621-7764
Secondary Phone: (520) 621-5995
Fax: (520) 621-9435
guerrier@email.arizona.edu
Degrees
- Ph.D. Syracuse University
- M.S. Biochemistry - State University of New York at Fredonia
- B.S. Biology - State University of New York at Fredonia
Classes Taught
- ANS 596A - Animal Sciences Graduate Seminar
Dr. Guerriero has an extensive background in Cell Biology. He served as a Postdoctoral Fellow and Research Instructor for the Baylor College of Medicine Department of Cell Biology before joining the University of Arizona in 1986. In his time in Tucson Dr. Guerriero has taught Animal Genetics and Biotechnology in Animal Science. He is currently instructing the Graduate Seminar course and is developing a new graduate course. Dr. Guerriero's research focuses on cellular stress due to such factors as heat stress.
Research Interests
All cells contain a set of proteins 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. These proteins are named according to their molecular weight. The most studied of these proteins have molecular weights of approximately 70kDa and are therefore called the Hsp70-related family of stress proteins. Hsp70 helps the cell survive stresses by binding to partially denatured proteins and assisting to refold these proteins into more stable native structures.
The importance of Hsp70 as a cellular regulator has dramatically increased over the years due to its association with a number of other cellular processes including protein refolding, apoptosis, cell proliferation and protein degradation. Misfolded proteins are a characteristic of some neuromuscular diseases and therefore studies are focused on understanding the regulation of Hsp70 activity on protein refolding. In addition, elevated Hsp70 levels have been reported in a number of different types of cancer and lowering these levels causes cancer cells to undergo apoptosis. Therefore, understanding the regulation of Hsp70 will provide information on the regulation of a diverse number of cellular activities and will have importance in both basic as well as applied medical research. The long term goal of this laboratory is to understand how other proteins can regulate Hsp70.
This laboratory has discovered a novel Hsp70 inhibitory protein called HspBP1. In vitro studies have revealed that HspBP1 binds to and inhibits Hsp70 by removal of bound nucleotide. Further studies have shown that HspBP1 is the most abundant Hsp70 cochaperone in tissues and cells and is elevated in a number of tumors. Recently, our laboratory has collaborated with a crystallography group to produce a model of HspBP1 binding to the ATPase domain of Hsp70.
This model has provided new insights on the mechanism of HspBP1 regulation of Hsp70 activity and information that will be used to design mutants for testing of the model. In addition, we have found that HspBP1 is presence in human sera and the levels of antibodies against HspBP1 are elevated in HIV infected patients. These new findings have provided support for the hypothesis that HspBP1 can function both inside and outside the cell.
Current Funding
- Muscular Dystrophy Association
- National Institutes of Health
Guerriero Lab
- Debbie Raynes - Research Specialist Senior
- Shamarie Black - Research Tech
Guerriero Lab
Shantz Building Room 234
Phone: 621-5995
Fax: 520-621-9435
Recent Articles
Selected Publications
- McLellan CA, Raynes DA, Guerriero V. 2003. HspBP1, an Hsp70 Cochaperone, Has Two Structural Domains and Is Capable of Altering the Conformation of the Hsp70 ATPase Domain. J. Biol. Chem. 278: 19017 - 19022.
- Raynes, D.A., Graner, M.A., Bagatell, R. McLellan, C. and Guerriero, V. 2003. Increased Expression of HspBP1 in Tumors. Tumor Biology 24:281-285. .
- Bernstein, H., Payne, C.M., Kunke, K., Guerriero, V., Raynes, D. A., Crowley-Weber, C.L., Waltmire, C.N., Dvorakova, K., Holubec., H., Bernstein, C., Vaillancourt, R.R. and Garewal, H. 2004. A proteomic study of deoxycholate induced apoptosis. Carcinogenesis 25: 681-692.
- Shomura, Y., Dragovic, Z., Chang, H-C., Tzvetkov, N., Young, J.C., Brodsky, J.L., Guerriero, V., Hartl, F.U. and Bracher, A. Regulation of Hsp70 function by HspBP1: Structural analysis reveals an alternate mechanism for Hsp70 nucleotide exchange. 2005. Molecular Cell 17:367-379.
- Papp, D., Prohászka, Z., Kocsis, J., Füst, G., Bánhegyi, D., Raynes, D.A. and Guerriero, V. 2005. Development of a sensitive assay for the measurement of antibodies against heat shock protein binding protein 1 (HspBP1): Increased levels of anti-HspBP1 IgG are prevalent in HIV infected subjects. J. Med. Vir. 76:464-469.
- Gottwald, E., Herschbach, M., Lahni, B., Miesfeld, R.L., Kunz, S. Raynes, D.A., Guerriero, V. Expression of the Cochaperone HspBP1 is not Coordinately Regulated with Hsp70 Expression. Cell Biology International 30: 553-558.
- Shen, L., Black, E. D., Witkowski, E.D., Lencer, W. I., Schneeberger, E. E., Guerriero, V. and Turner, J.R. Myosin light chain phosphorylation regulates barrierfunction by remodeling tight junction composition. J. Cell Sci. 119: 2095-2106.
- Raynes, D.A., Thomson , C.A., Stroster, J., Newton, T., Cuneo, P. and Guerriero, V. Human Sera Contains Detectable Levels of the Hsp70 Cochaperone HspBP1 and Antibodies Bound to HspBP1. J. Immunoassay and Immunochemistry 27:251-264.
