Methionine aminopeptidase 2 inhibition: antiangiogenesis and tumour therapy

Bibliography

• BRADSHAW RA, HOPE CJ, YI E, WALKER KW: Co- and post-translational processing: the removal of methionine. In The Enzymes: Co- and Post-translational Proteoksis of Proteins. Dalbey RE et al. (Eds) Academic press, San Diego, USA (2001):389–420.
   Google Scholar
• •Gives a detailed summary of MetAPs.
   Google Scholar
• ARFIN SM, KENDALL RL, HALL L et al.: Eukaryotic methionyl aminopeptidases: two classes of cobalt-dependent enzymes. Proc. Natl Acad. ScL USA (1995) 92:7714–7718.
   PubMed Web of Science ®Google Scholar
• •First description of the two types of MetAPs.
   Google Scholar
• BRADSHAW RA, BRICKEY WW, WALKER KW: N-terminal processing: the methionine aminopeptidase and N-a-acetyl transferase families. Trends Biochem. Sci. (1998) 23:263–267.
   PubMed Web of Science ®Google Scholar
• TOWLER DA, EUBANKS SR, TOWERY DS, ADAMS SP, GLASER L: Amino-terminal processing of proteins by N-myristoylation. Substrate specificity of N-myristoyl transferase. Biol. Chem. (1987) 262:1030–1036.
   Google Scholar
• GIGLIONE C, SERERO A, PIERRE M, BOISSON B, MEINNEL T: Identification of eukaryotic peptide deformylases reveals universality of N-terminal protein processing mechanisms. EMBO (2000) 21:5916–5929.
   Google Scholar
• LIU S, WIDOM J, KEMP CW, CREWS CM, CLARDY J: Structure of human methionine aminopeptidase-2 complexed with fumagillin. Science (1998) 282:1324–1327.
   PubMed Web of Science ®Google Scholar
• •Describes three-dimensional structure of human MetAP2 complex with fumagillin.
   Google Scholar
• RODERICK SL, MATTHEWS BW: Structure of the cobalt-dependent methionine aminopeptidase from Escherichia colt. a new type of proteolytic enzyme. Biochemistry (1993) 32:3907–3912.
   Google Scholar
• MILLER CG, STRAUCH KL, KUKRAL AM et aL: N-terminal methionine-specific peptidase in Salmonella hphimurium. Proc. Natl Acad. ScL USA (1987) 84:2718–2722.
   PubMedGoogle Scholar
• BEN-BASSAT A, BAUER K, CHANG SY et al.: Processing of the initiation methionine from proteins: properties of the Escherichia colimethionine aminopeptidase and its gene structure. Bacteria (1987) 169:751–757.
   PubMed Web of Science ®Google Scholar
• D'SOUZA VM, HOLZ RC: The methionyl aminopeptidase from Escherichia coil can function as an iron(II) enzyme. Biochemistry (1999) 38:11079–11085.
   PubMedGoogle Scholar
• D'SOUZA VM, BENNETT B, COPIK AJ, HOLZ RC: Divalent metal binding properties of the methionyl aminopeptidase from Escherichia colt. Biochemistry (2000) 39:3817–3826.
   PubMedGoogle Scholar
• D'SOUZA VM, SWIERCZEK SI, COSPER NJ et al.: Kinetic and structural characterization of manganese(II)-loaded methionyl aminopeptidases. Biochemistry (2002) 41:13096–13105.
   Google Scholar
• MENG L, RUEBUSH S, D'SOUZA VM et al.: Overexpression and divalent metal binding properties of the methionyl aminopeptidase from Pyrococcus furiarus. Biochemistry (2002) 41:7199–7208.
   Google Scholar
• WANG J, SHEPPARD GS, LOU P et al:Physiologically relevant metal cofactor for methionine aminopeptidase-2 is manganese. Biochemistry (2003) 42:5035–5042.
   PubMedGoogle Scholar
• WALKER KW, BRADSHAW RA: Yeast methionine aminopeptidase I can utilize either Zn2+ or Co2+ as a cofactor: a case of mistaken identity? Protein Sci. (1998) 7:2684–2687.
   Google Scholar
• LI X, CHANG YH: Amino-terminal protein processing in Saccharomyces cerevisiaeis an essential function that requires two distinct methionine aminopeptidases. Proc. Natl Acad. Sci USA (1995) 92:12357–12361.
   PubMed Web of Science ®Google Scholar
• CHANG SY, MCGARY EC, CHANG S: Methionine aminopeptidase gene of Escherichia coil is essential for cell growth. J. Bacteria (1989) 171:4071–4072.
   PubMed Web of Science ®Google Scholar
• TURK BE, GRIFFITH EC, WOLF S et al.: Selective inhibition of amino-terminal methionine processing by TNP-470 and ovalicin in endothelial cells. Chem. Biol. (1999) 6:823–833.
   PubMed Web of Science ®Google Scholar
• •Best description of differences in catalytic properties of the two MetAP isoforms.
   Google Scholar
• SIN N, MENG L, WANG MQ et al.: The antiangiogenic agent fumagillin covalently binds and inhibits the methionine aminopeptidase, MetAP-2. Proc. Natl Acad. Sci. USA (1997) 94:2362–2367.
   PubMedGoogle Scholar
• •See Griffith, 1997 [20].
   Google Scholar
• GRIFFITH EC, SU Z, TURK BE et al: Methionine aminopeptidase (Type 2) is the common target for angiogenesis inhibitors AGM-1470 and ovalicin. Chem. Biol . (1997) 4:461–471.
   PubMed Web of Science ®Google Scholar
• •Initial identification of MetAP2 as the target of fumagillin and related substances.
   Google Scholar
• MCCOWEN M, CALLENDER M, LAWLIS J: Fumagillin (H-3), a new antibiotic with amebicidal properties. Science (1951) 113:202–203.
   PubMed Web of Science ®Google Scholar
• SIGG HP, WEBER HP: Isolation and structure elucidation of ovalicin. Hely. Chim. Acta. (1968) 51:1395–1408.
   PubMedGoogle Scholar
• HARTMANN GR, RICHTER H, WEINER EM, ZIMMERMANN W: On the mechanism of action of the cytostatic drug anguidine and of the immunosuppressive agent ovalicin, two sesquiterpenes from fungi. Planta Med. (1978) 34:231–252.
   PubMedGoogle Scholar
• GRIFFITH EC, SU Z, NIWAYAMA S et al.: Molecular recognition of angiogenesis inhibitors fumagillin and ovalicin by methionine aminopeptidase 2. Proc. Natl Acad. Sci. USA (1998) 95:15183–15188.
   PubMedGoogle Scholar
• LOWTHER WT, MCMILLEN DA, ORVILLE AM, MATTHEWS BW: The antiangiogenic agent fumagillin covalently modifies a conserved active-site histidine in the Escherichia coil methionine aminopeptidase. Proc. Nati Acad. Sci. USA (1998) 95:12153–12157.
   PubMed Web of Science ®Google Scholar
• HAN C, AHN S, CHOI N et al.: Design and synthesis of highly potent fumagillin analogues from homology modeling for a human MetAP-2. Bioorg. Med. Chem. Lett. (2000) 10:39–43.
   PubMed Web of Science ®Google Scholar
• LUO QL, LI JY, LIU ZY et al.: Discovery and structural modification of inhibitors of methionine aminopeptidases from Escherichia coil and Saccharomyces cerevisiae. J. Med. Chem. (2003) 46:2631–2640.
   PubMedGoogle Scholar
• KEDING S, DALES N, LIM S, BEAULIEU D, RICH D: Synthesis of (3/0 -amino-(2.5)-hydroxy amino acids for the inhibition of methionine aminopeptidase-1. Synthesis Commun. (1998) 28:4463–4470.
   Google Scholar
• INGBER D, FUJITA T, KISHIMOTO S et al.: Synthetic analogues of fumagillin that inhibit angiogenesis and suppress tumour growth. Nature (1990) 348:555–557.
   PubMed Web of Science ®Google Scholar
• •First identification of fumagillin as an antiangiogenic substance.
   Google Scholar
• CASTRONOVO V, BELOTTI D: TNP-470 (AGM-1470): mechanisms of action and early clinical development. Ear: J. Cancer (1996) 32A:2520–2527.
   Google Scholar
• KUSAKA M, SUDO K, MATSUTANI E et al.: Cytostatic inhibition of endothelial cell growth by the angiogenesis inhibitor TNP-470 (AGM-1470). Br: J. Cancer (1994) 69:212–216.
   Google Scholar
• ABE J, ZHOU W, TAKUWA N et al: A fumagillin derivative angiogenesis inhibitor, AGM-1470, inhibits activation of cyclin-dependent kinases and phosphorylation of retinoblastoma gene product but not protein tyrosyl phosphorylation or protooncogene expression in vascular endothelial cells. Cancer Res. (1994) 54:3407–3412.
   PubMed Web of Science ®Google Scholar
• HORI A, IKEYAMA S, SUDO K: Suppression of cyclin D1 mRNA expression by the angiogenesis inhibitor TNP-470 (AGM-1470) in vascular endothelial cells. Biochem. Biophys. Res. Commun. (1994) 204:1067–1073.
   PubMed Web of Science ®Google Scholar
• YEH J, MOHAN R, CREWS C: The antiangiogenic agent TNP-470 requires p53 and p21 CIP/WAF for endothelial cell growth arrest. Proc. Nati Acad. Sci. USA (2000) 23:12782–12787.
   Google Scholar
• ZHANG Y, GRIFFITH EC, SAGE J, JACKS T, LIU JO: Cell cycle inhibition by the antiangiogenic agent TNP-470 is mediated by p53 and p21WAF1/CIP1. Proc. Nati Acad. Sci. USA (2000) 97:6427–6432.
   PubMed Web of Science ®Google Scholar
• MASIERO L, FIGG WD, KOHN EC: New antiangiogenesis agents: review of the clinical experience with carboxyamido-triazole (CAI), thalidomide, TNP-470 and interleukin-12. Angiogenesis (1997) 1:23–35.
   PubMedGoogle Scholar
• KRUGER EA, FIGG WD: TNP-470: an angiogenesis inhibitor in clinical development for cancer. Expert Opin. Investig. Drugs (2000) 9:1383–1396.
   PubMed Web of Science ®Google Scholar
• •Most complete description of the clinical trials with TNP-470.
   Google Scholar
• GIMBRONE M, LEAPMANS S, COTRANS R, FOLKMAN J: Tumor dormancy M vitro by prevention of neovascularization. J. Exp. Med. (1972) 136:261–276.
   PubMed Web of Science ®Google Scholar
• KENDALL RL, BRADSHAW RA: Isolationand characterization of the methionine aminopeptidase from porcine liver responsible for the co-translational processing of proteins. J. Biol. Chem. (1992) 267:20667–20673.
   PubMedGoogle Scholar