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Small Stress Proteins (Paperback, Softcover reprint of the original 1st ed. 2002)
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Small Stress Proteins (Paperback, Softcover reprint of the original 1st ed. 2002)
Series: Progress in Molecular and Subcellular Biology, 28
Expected to ship within 10 - 15 working days
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Studies have identified important families of proteins (denoted:
heat shock or stress proteins, Hsps) which display an enhanced
expression in response to heat shock or other physiological
stresses. Besides the characterization of the genes encoding Hsp
and the mechanisms of their induction, recent studies have
concentrated on the function of these proteins. It was shown that
the expression of Hsp protects the cell against different types of
aggressions. In addition,Hsp can regulate essential biochemical
processes in unstressed cells. For example, members of the Hsp60
and Hsp70 families act as ATP-binding proteins allowing the folding
of nascent or denatured proteins as well as the assembly or
disassembly of protein complexes. These observations have led to
the discovery of the molecular chaperone concept (Ellis and
Hemmingsen 1989). Amongst the proteins whose expression is
up-regulated by heat shock or other types of stresses are the small
stress proteins also denoted (sHsps, sHsp or sHSP). Small stress
proteins encompass a large numbers of related proteins which are
represented in virtually all organisms, including prokary- otes.
These polypeptides share a structural domain, often referred to as
the a-crystallin domain, common to the lens protein
alpha-crystallin (Ingolia and Craig 1982;Wistow 1985). In addition
to being increased in response to several types of stresses, the
Hsp level is also upregulated during development and correlates
with the differentiation and oncogenic status of the cell. In spite
of the fact that sHsp can confer cellular protection against
stresses,their molecular function has remained enigmatic for years.
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