Download PDF by Michael W. Thompson, Louis B. Hersh (auth.), Nigel M.: Aminopeptidases in Biology and Disease

By Michael W. Thompson, Louis B. Hersh (auth.), Nigel M. Hooper, Uwe Lendeckel (eds.)

ISBN-10: 1441988696

ISBN-13: 9781441988690

ISBN-10: 1461346983

ISBN-13: 9781461346982

Aminopeptidases in Biology and Disease offers a finished evaluation of the rising position of aminopeptidases in a number of organic strategies and sickness occasions. methods as various as angiogenesis, antigen presentation, neuropeptide and hormone processing, being pregnant and copy, protein turnover, reminiscence, irritation, tumour development, melanoma and metastasis, blood strain and high blood pressure all significantly contain a number of aminopeptidases. the person chapters were written by way of specialists within the box who've supplied distinctive debts of the vital roles performed by way of quite a few aminopeptidases in biology and disease.

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Extra resources for Aminopeptidases in Biology and Disease

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1~:? L E-Cdk2 Rb-Pn *E2F Figure 4. Potential mechanism(s) ofVEC cytostatic growth arrest after TNP-470 treatment. Phosphorylation of p53 has been shown to decrease the association of p53 and Mdm2 (Agarwal et al. 1998). However, Mdm2 expression increases in primary murine pulmonary endothelial cells (MPEs) after TNP-470 36 VETRO, DUMMITT, AND CHANG Chapter 2 treatment (Yeh et al. 2000), and the phosphorylation of common sites on p53 (Ser-6, -9, -15, -20, -37, and -392) does not occur (Yeh et al.

Furthermore, treatment of VEC with cytostatic concentrations of TNP-470 (10 nM) that are similar to therapeutic serum concentrations in animal models does not induce apoptosis (Yeh et al. 2000) . Thus, it is unclear whether decreased eNOS N'--myristoylation is relevant to the pharmacological effect ofTNP-470 at therapeutic concentrations. An analysis of total protein eH]-myristic acid incorporation in BABCs after treatment with a lower cytostatic concentration of TNP-470 (50 oM) indicates that protein N'--myristoylation is largely unaffected (Turk et al.

Roderick, S. , Matthews, B. , 1994, Sequence and structure comparison suggest that methionine aminopeptidase, prolidase, aminopeptidase P, and creatinase share a common fold. , Chang, S. , 1987, Processing of the initiation methionine from proteins: properties of the Escherichia coli methionine aminopeptidase and its gene structure.

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Aminopeptidases in Biology and Disease by Michael W. Thompson, Louis B. Hersh (auth.), Nigel M. Hooper, Uwe Lendeckel (eds.)

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