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Chemistry and Biology of Serpins (Paperback, Softcover reprint of the original 1st ed. 1997)
Loot Price: R1,593
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Chemistry and Biology of Serpins (Paperback, Softcover reprint of the original 1st ed. 1997)
Series: Advances in Experimental Medicine and Biology, 425
Expected to ship within 10 - 15 working days
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Serpins (serine protease inhibitors) are a superfamily of proteins
whose physiologi- cal action is primarily targeted to inhibiting
serine proteases. There are instances where serpins are not
inhibitors (and can carry steroid hormones for instance), yet key
structural and functional elements found in all serpins are
maintained in these 'non-inhibitor' ser- pins. Many serpins have
well-described biological properties which influence pathophysi-
ological events, including: antithrombin (historically called
antithrombin III), ai-protease inhibitor (historically called
ai-antitrypsin), and plasminogen activator inhibitor-I, just to
mention a few. A deficiency or defect in antithrombin leads to
venous thromboembolic disease, while a deficiency or defect in
ai-protease inhibitor is associated with chronic obstructive
pulmonary emphysema. In contrast, it has been suggested that
increased levels of plasminogen activator inhibitor-l may be a
predisposition to myocardial infarction. The list goes on for each
of our own "favorite" serpin. The biological roles found for
serpins are key participants in almost every physiological event.
In other words, serine proteases are needed for many events in
biology and the role of serpins to down regulate these pro- teases
is essential. Thus, just using these three examples above for
serpins and their patho- physiological roles reminds us that the
medical costs to control such events is significant worldwide.
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