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    Chemistry and Biology of Serpins (Advances in Experimental Medicine and Biology) (Paperback) Edited by Frank C. Church, Edited by Dennis D. Cunningham, Edited by David Ginsburg, Edited by Maureane R. Hoffman, Edited by Stuart R. Stone, Edited by Douglas M. Tollefsen

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    DescriptionSerpins (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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    Title
    Chemistry and Biology of Serpins
    Authors and contributors
    Edited by Frank C. Church, Edited by Dennis D. Cunningham, Edited by David Ginsburg, Edited by Maureane R. Hoffman, Edited by Stuart R. Stone, Edited by Douglas M. Tollefsen
    Physical properties
    Format: Paperback
    Number of pages: 382
    Width: 178 mm
    Height: 254 mm
    Thickness: 22 mm
    Weight: 721 g
    Language
    English
    ISBN
    ISBN 13: 9781461374619
    ISBN 10: 1461374618
    Classifications

    BIC E4L: HEA
    Nielsen BookScan Product Class 3: S6.0
    B&T Book Type: NF
    Ingram Subject Code: PI
    LC subject heading: ,
    BIC subject category V2: PSV
    B&T Merchandise Category: SCI
    B&T General Subject: 710
    BISAC V2.8: SCI070000
    LC subject heading:
    BIC subject category V2: MF, PSB
    Abridged Dewey: 572
    LC classification: QP
    BISAC V2.8: MED008000
    Warengruppen-Systematik des deutschen Buchhandels: 16760
    BISAC V2.8: MED107000
    LC subject heading:
    BISAC V2.8: SCI007000
    DC21: 612.01575
    DC22: 612.01575
    LC classification: QH431, QH345, QD415-436, QH301-705, RB155-155.8, QP82-82.2
    Thema V1.0: PSV, MF, PSB
    Edition statement
    Softcover Reprint of the Origi ed.
    Illustrations note
    biography
    Publisher
    Springer-Verlag New York Inc.
    Imprint name
    Springer-Verlag New York Inc.
    Publication date
    29 October 2012
    Publication City/Country
    New York, NY
    Review quote
    'The editors have succeeded in producing a volume of work which provides many answers to questions, asked and unasked, about a critically important field of biologic research. It should be in the library of any scientist with an interest in human physiology; it would be useful to many other researchers as well.' Chemtracts - Biochemistry and Molecular Biology, 12:10 (1999)
    Table of contents
    Introduction: Serpins: From the Way It Was to the Way It Is; J. Travis. Serpins: A Mechanistic Class of Their Own; S.R. Stone, et al. Coagulation: Antithrombin-A Bloody Important Serpin; I. Bjork, S.T. Olson. Heparin Cofactor II; D.M. Tollefsen. Neurobiology and Cancer: Regulation of Neurons and Astrocytes by Thrombin and Protease Nexin-l: Relationship to Brain Injury; D.D. Cunningham, F.M. Donovan. Maspin: A Tumor Suppressing Serpin; R. Sager, et al. Fibrinolysis: The Role of Reactive-Center Loop Mobility in the Serpin Inhibitory Mechanism; D.A. Lawrence. Substrate Specificity of Tissue Type Plasminogen Activator; E.L. Madison. Development and Reproduction: Biology of Progesterone-Induced Uterine Serpins; P.J. Hansen, W.-J. Liu. Serpins from an Insect, Manduca sexta; M.R. Kanost, H. Jiang. Inflammation: Serpins and Programmed Cell Death; G.S. Salvesen. Noninhibitor Serpins: Structure-Function Studies on PEDF: A Noninhibitory Serpin with Neurotropic Activity; S.P. Becerra. Abstracts: Coagulation, Neurobiology and Cancer. Fibrinolysis, Development and Reproduction. Inflammation and Noninhibitor Serpins. 10 Additional Articles. Index.