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Structure/Function
of Mammalian Stress Proteins and Implications for Medicine 
Understanding how cells respond to injury will help in diagnosing and
treating injury at the organ/tissue level. Consequently, our laboratory
examines how cells respond to metabolic injuries at the molecular level.
For example, in response to adverse changes in their environment (e.g.
heat, anoxia, metabolic poisons) cells increase their expression of a
group of proteins referred to as heat shock proteins. Many of the hsp's
function as "molecular chaperones", facilitating the synthesis and assembly
of cellular proteins. Exactly how these proteins participate in protein
maturation events is one research focus of our group.
Activation of the stress response occurs in vivo in response to clinically
relevant insults including ischemia/reperfusion, excitatory amino acid
overload, hypertrophy, and fever. Increased expression of the hsp's in
tissues/organs confers added protection, especially upon a subsequent
injury. Hence, we are exploring pharmacological ways by which to increase
the expression of these proteins in the animal and thereby harness their
protective effects. Such studies eventually may prove to be important
for enhancing the viability of organs used in transplantation, or for
reducing the extent of tissue/organ damage following infection and/or
traumatic injury.
Selected Publications:
Welch, WJ. How cells respond to stress. Scientific American 268 (1993):
56-64.
Minowada, G and Welch, WJ. Clinical implications of the stress response.
J. Clin. Invest. 95 (1995): 3-12.
Brown, R, Hong-Brown, L and Welch, WJ. Correcting temperature-sensitive
folding defects. J. Clin. Invest. 99 (1997): 1432- 1444.
Contact Information:
Email: welch@itsa.ucsf.edu
Phone: 415/ 206-5908
Address: Box 1302, SFGHMC 1 210
The University of California, San Francisco, CA 94143, (415) 476-9000
Copyright 2003, The Regents of the University of California.
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