Cell Surface Proteases: Volume 54

Cell Surface Proteases: Volume 54

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Description

Cell Surface Proteases provides a comprehensive overview of these important enzymes that catalyze the hydrolysis of a protein as it degrades to a simpler substance. In the 1990s, an explosion of new discoveries shed light on the role of cell surface proteases and extended it beyond degradation of extracellular matrix components to include its influence on growth factors, cell signaling, and other cellular events. This volume unites the scientific literature from across disciplines and teases out unified themes of interactions between cell surface proteases and interconnecting cell surface-related systems -- including integrins and other adhesion molecules. Scientists and students involved in developmental biology, cell biology and disease processes will find this an indispensable resource.
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Product details

  • Hardback | 452 pages
  • 152.4 x 228.6 x 25.4mm | 816.48g
  • Academic Press Inc
  • San Diego, United States
  • English
  • Illustrations (some col.)
  • 0121531546
  • 9780121531546

Table of contents

Membrane Type - Matrix Metalloproteinases
Surface Association of Secreted Matrix Metalloproteinases
Biochemical Properties and Functions of Membrane-anchored Metalloprotease-Disintegrin Proteins (ADAMs)
Shedding of plasma membrane proteins
Expression of Meprins in Health and Disease
Type II Transmembrane Serine Proteases
DPPIV, Seprase and Related Serine Peptidases in Multiple Cellular Functions
The Secretases of Alzheimer's Disease
Plasminogen Activation at the Cell Surface
Cell Surface Cathepsin B: Understanding its Functional Significance
Protease activated receptors
EMMPRIN (CD147), a cell surface regulator of Matrix Metalloproteinase Production and Function
The evolving roles of Cell Surface Proteases in Health and Disease: Implications for Developmental, Adaptive, Inflammatory and Neoplastic Processes
Shed Membrane Vesicles and Clustering of Membrane-bound Proteolytic Enzymes
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About Stanley Zucker

Edited by Stanley Zucker
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