About the Book
Please note that the content of this book primarily consists of articles available from Wikipedia or other free sources online. Pages: 66. Chapters: ADAM10, ADAM11, ADAM12, ADAM15, ADAM17, ADAM18, ADAM19, ADAM2, ADAM22, ADAM23, ADAM28, ADAM7, ADAM8, ADAM9, ADAMTS2, Angiotensin-converting enzyme, A disintegrin and metalloproteinase, Calpain, Calpastatin, Caspase, Caspase 8, Cathepsin, Cathepsin A, Cathepsin B, Cathepsin C, Cathepsin D, Cathepsin E, Cathepsin F, Cathepsin G, Cathepsin H, Cathepsin K, Cathepsin L1, Cathepsin L2, Cathepsin O, Cathepsin S, Cathepsin W, Cathepsin Z, Cauxin, Chymotrypsin, CLPP, Dipeptidyl peptidase, Dipeptidyl peptidase-4, Elastase, Endoproteinase Lys-C, Gingipain, Glutamate carboxypeptidase II, Hementerin, HIV-1 protease, HtrA serine peptidase 2, IgA protease, KLK1, Lys-N, Matrix metallopeptidase 12, Matrix metallopeptidase 13, MEROPS, MMP1, MMP10, MMP11, MMP14, MMP15, MMP16, MMP17, MMP19, MMP2, MMP20, MMP21, MMP3, MMP7, MMP8, MMP9, Oligopeptidase, Papain, Pepsin, Procollagen peptidase, Proteases (medical and related uses), Proteases in angiogenesis, Protease accumulated by inhibitors, Retroviral aspartyl protease, Serratiopeptidase, Signal peptide peptidase, Subtilase, Thermolysin, Tripeptidyl peptidase, Tripeptidyl peptidase I, Tripeptidyl peptidase II. Excerpt: Angiogenesis is the process of forming new blood vessels from existing blood vessels. It is a highly complex process involving extensive interplay between cells, soluble factors, and the extracellular matrix (ECM). Angiogenesis is critical during normal physiological development, but it also occurs in adults during inflammation, wound healing, ischemia, and in pathological conditions such as rheumatoid arthritis, hemangioma, and tumor growth. Proteolysis has been indicated as one of the first and most sustained activities involved in the formation of new blood vessels. Numerous proteases including matrix metalloproteases (MMPs), a disintegrin and metalloprotease domain (ADAM), a disintegrin and metalloprotease domain with throbospondin motifs (ADAMTS), and cysteine and serine proteases are involved in angiogenesis. This article focuses on the important and diverse roles that these proteases play in the regulation of angiogenesis. MMPs are a large multigene family of zinc-dependent endopeptidases. The collective MMP family is capable of degrading all known ECM macromolecules. MMP activity is regulated at the level of transcription as well as by endogenous inhibitors known as tissue inhibitors of metalloproteases (TIMPs). The role of matrix metalloproteases and TIMPs in several pathological conditions including angiogenesis, tumor growth, and metastasis has been investigated and very well described. Matrix metalloproteases contain five conserved domain structures: There is also a subfamily of the matrix metalloproteases, the membrane-type MMPs (MT-MMPs) which contain an additional transmembrane domain and a short cytoplasmic domain. After activation of MMPs by removal of the propeptide domain, their activity is regulated by TIMPs. TIMPs specifically and reversibly inhibit the activity of MMPs. So far there have been identified four members of the family, TIMP1-4. All TIMPs contain twelve conserved cystein residues, which form six disulfide bonds. The C-terminal domain
