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

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

Aminopeptidases in Biology and Disease offers a complete evaluation of the rising position of aminopeptidases in a variety of organic procedures and affliction events. tactics as different 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 particular money owed of the primary roles performed via numerous aminopeptidases in biology and disease.

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L. , 1999, The sizes of peptides generated from protein by mammalian 26 and 20 S proteasomes: implications for understanding the degradative mechanism and antigen presentation. J. Bioi. Chem. 274: 3363-3371. , 2001, Specific inhibitor of puromycin-sensitive aminopeptidase with a homophthalimide skeleton: identification of the target molecule and a structure-activity relationship study. Bioorg. Med. Chem. 9: 121-131. , 1996, Pain, anxiety and aggression in mice deficient in pre-proenkephalin, Nature 383: 535-538 .

Fumagillin R= ~~OH 4 Ovalicin Figure 3. The Fumagillin class of angiogenesis inhibitors. Carbon numbering was adopted from Liu et al. 2 Targeting of Mammalian MetAP2 by the Fumagillin Angioinhibins Evidence that fumagillin and ovalicin target and irreversibly inhibit mammalian MetAP2 catalytic activity in VECs was recently reported. Near 32 VETRO, DUMMITT, AND CHANG Chapter 2 western analyses of crude protein extracts from primary VECs using biotinlabeled fumagillin (Sin et al. 1997) or photoaffinity-labeled ovalicin (Griffith et al.

4 Possible downstream effects of MetAP2 inhibition that lead to p53 activation Given the specificity of TNP-470 for MetAP2, it has been proposed that differences in substrate processing efficiencies between MetAP1 and MetAP2 in vivo might lead to the retention of Metinit on proteins that rely primarily on MetAP2 for Metinit hydrolysis (Griffith et al. 1997; Sin et al. 1997; Turk et al. 1999). The retention of Metinit may then interfere with the function of one or more of these MetAP2-reliant proteins, thus resulting in the activation of the p53 pathway and subsequent cell cycle arrest (Figure 4).

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