Download e-book for iPad: Aminopeptidases in Biology and Disease by Michael W. Thompson, Louis B. Hersh (auth.), Nigel M.

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 accomplished assessment of the rising position of aminopeptidases in various organic strategies and disorder events. procedures as different as angiogenesis, antigen presentation, neuropeptide and hormone processing, being pregnant and replica, protein turnover, reminiscence, irritation, tumour development, melanoma and metastasis, blood strain and high blood pressure all severely contain a number of aminopeptidases. the person chapters were written by way of specialists within the box who've supplied unique bills of the critical roles performed by way of a variety of aminopeptidases in biology and disease.

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Genomics 56: 361-362. , 1999b, Increased anxiety and impaired pain response in puromycin-sensitive aminopeptidase gene-deficient mice obtained by a mouse gene-trap method. J. Neurosci. 19: 6068-6078 . , 2000, Aminopeptidase N is a receptor for tumor-homing peptides and a target for inhibiting angiogenesis . Cancer Res. 60: 722-727. , 1999, Neonatal handling in rats induces long-term effects on dynorphin peptides. Neuropeptides 33: 468-474 . , 200 I, Frequency of tau gene mutations in familial and sporadic cases of non-alzheimer dementia.

1997). 3 Regulation of mammalian MetAP2 Mammalian MetAP2 expression is regulated both transcriptionally and post-translationally. Transcription of rat MetAP2 (p67) is induced by phorbol 13-myristate 12-acetate (PMA) (Chatterjee et al. 1997). Additionally, p67 is absent from serum-starved rat KRC-7 cells, and treatment with p67 antisense DNA prevents PMA induction of p67 and subsequent protein synthesis (Gupta et al. 1997), which demonstrates the importance of p'" in growth and protein synthesis .

Crystal structure studies of human MetAP2 complexed with fumagillin revealed that the imidazole nitrogen (NE2) of the conserved catalytic residue His 231 covalently attaches to the C3 ring epoxide group of fumagillin (Liu et al. 1998). These studies are further supported by the findings that the substitution of His231 with Asn in hMetAP2 precludes the covalent attachment of fumagillin to hMetAP2 and that the C3 ring epoxide group is required for EC growth inhibition by the fumagillin class of angiogenesis inhibitors (Griffith et al.

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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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