By Michael W. Thompson, Louis B. Hersh (auth.), Nigel M. Hooper, Uwe Lendeckel (eds.)
Aminopeptidases in Biology and Disease offers a accomplished evaluation of the rising function of aminopeptidases in a variety of organic techniques and ailment occasions. approaches as varied as angiogenesis, antigen presentation, neuropeptide and hormone processing, being pregnant and copy, protein turnover, reminiscence, irritation, tumour progress, 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 exact money owed of the crucial roles performed via numerous aminopeptidases in biology and disease.
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1997; Sin et al. 1997; Turk et al. 001) between the inhibition of MetAP2 activity and the inhibition of EC growth in vitro (Griffith et al. 1997). Furthermore, the concentration of TNP-470 sufficient to modify half of MetAP2 in intact EC (100 ± 13 pM) is comparable to the ICso of TNP-470 that is cytostatic under the same conditions (161 ± 69 pM) (Turk et al. 1999). Rationally designed drugs based on the crystal structure of hMetAP2 also show much greater potency against EC growth (Han et al. 2000; Wang et al.
This proposal is further supported by the finding that high concentrations of ovalicin (structurally similar to TNP-470) covalently modify Escherichia coli MetAP (a type 1 MetAP) and yeast MetAPI in the same manner as hMetAP2 (Lowther et al. 1998). 1 TNP-470 inhibition ofVEC growth through inhibition of MetAP2 catalytic activity There is much evidence indicating that the selective, cytostatic inhibition of VEe growth is responsible for the anti-angiogenic activity of TNP-470 (Kusaka et al. 1994).
It is proposed that the abnormal hydrolysis of methionine decreases the hydrophobic surface area of the N-terminal region, which is required for transport by the mitochondrial import machinery (Hammen et al. 1999). 2 The Role of MetAP in Protein Turnover The N-end rule states that the intracellular half-life of a protein is governed by its N-terminal residue (for review see Varshavsky 1997). , Met, Ser) have considerably longer half-lives in vivo (Varshavsky 1997). Methionine is considered a stabilizing N-terminal residue and proteins that retain Metinil generally have long half-lives in vivo (Varshavsky 1997).