Angiogenin 3512034 224265374 2008-07-08T01:52:16Z ProteinBoxBot 3991663 Replaced protein Box Template with PBB Template for easy viewing. <!-- The PBB_Controls template provides controls for Protein Box Bot, please see Template:PBB_Controls for details. --> {{PBB|geneid=283}} '''Angiogenin''' (Ang) is a small [[polypeptide]] that is implicated in [[angiogenesis]] (formation of new blood vessels) in tumor growth . However, angiogenin is unique among the many proteins that are involved in angiogenesis in that it is also an [[enzyme]] with an [[amino acid]] sequence 33% identical to that of [[bovine]] [[pancreatic]] [[ribonuclease]] (RNase) A). Moreover, although Ang has the same general [[catalytic]] properties as RNase A - it cleaves preferentially on the 3' side of [[pyrimidines]] and follows a transphosphorylation/[[hydrolysis]] mechanism - its activity differs markedly both in magnitude and in specificity. Although angiogenin contains counterparts for the key catalytic residues of bovine pancreatic RNase A, it cleaves standard RNase substrates 10<sup>5</sup> - 10<sup>6</sup> times less efficiently than does RNase A. Despite this apparent weakness, the enzymatic activity of Ang appears to be essential for biological activity: replacements of important active site residues invariably diminish [[ribonuclease]] and [[angiogenesis]] activities in parallel, and a substitution that increases [[enzymatic]] activity also enhances [[angiogenic]] potency. Angiogenin may function as a [[tRNA]]-specific [[ribonuclease]] that binds to [[actin]] on the surface of [[endothelial]] cells; once bound, angiogenin is endocytosed and translocated to the [[Cell nucleus|nucleus]], thereby promoting the [[endothelial]] invasiveness necessary for [[blood vessel]] formation. Angiogenin induces [[vascularization]] of normal and [[malignant]] tissues, and abolishes protein synthesis by specifically hydrolyzing cellular tRNAs. [[Alternative splicing]] results in two transcript variants encoding the same protein. This gene and the gene that encodes ribonuclease, RNase A family, 4 share [[promoter]]s and 5' [[exon]]s. Each gene splices to a unique downstream exon that contains its complete coding region.<ref>{{cite web | title = Entrez Gene: ANG angiogenin, ribonuclease, RNase A family, 5| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=283| accessdate = }}</ref> ==References== {{reflist}} ==Further reading== {{refbegin | 2}} {{PBB_Further_reading | citations = *{{cite journal | author=Saxena SK, Rybak SM, Davey RT, ''et al.'' |title=Angiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily. |journal=J. Biol. Chem. |volume=267 |issue= 30 |pages= 21982–6 |year= 1992 |pmid= 1400510 |doi= }} *{{cite journal | author=Weremowicz S, Fox EA, Morton CC, Vallee BL |title=Localization of the human angiogenin gene to chromosome band 14q11, proximal to the T cell receptor alpha/delta locus. |journal=Am. J. Hum. Genet. |volume=47 |issue= 6 |pages= 973–81 |year= 1990 |pmid= 1978563 |doi= }} *{{cite journal | author=Weremowicz S, Fox EA, Morton CC, Vallee BL |title=The placental ribonuclease inhibitor (RNH) gene is located on chromosome subband 11p15.5. |journal=Genomics |volume=8 |issue= 4 |pages= 717–21 |year= 1991 |pmid= 2276743 |doi= }} *{{cite journal | author=Shapiro R, Riordan JF, Vallee BL |title=Characteristic ribonucleolytic activity of human angiogenin. |journal=Biochemistry |volume=25 |issue= 12 |pages= 3527–32 |year= 1986 |pmid= 2424496 |doi= }} *{{cite journal | author=Weiner HL, Weiner LH, Swain JL |title=Tissue distribution and developmental expression of the messenger RNA encoding angiogenin. |journal=Science |volume=237 |issue= 4812 |pages= 280–2 |year= 1987 |pmid= 2440105 |doi= }} *{{cite journal | author=Bicknell R, Vallee BL |title=Angiogenin activates endothelial cell phospholipase C. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=85 |issue= 16 |pages= 5961–5 |year= 1988 |pmid= 2457905 |doi= }} *{{cite journal | author=Shapiro R, Vallee BL |title=Site-directed mutagenesis of histidine-13 and histidine-114 of human angiogenin. Alanine derivatives inhibit angiogenin-induced angiogenesis. |journal=Biochemistry |volume=28 |issue= 18 |pages= 7401–8 |year= 1990 |pmid= 2479414 |doi= }} *{{cite journal | author=Bicknell R, Vallee BL |title=Angiogenin stimulates endothelial cell prostacyclin secretion by activation of phospholipase A2. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=86 |issue= 5 |pages= 1573–7 |year= 1989 |pmid= 2646638 |doi= }} *{{cite journal | author=Lee FS, Vallee BL |title=Characterization of ribonucleolytic activity of angiogenin towards tRNA. |journal=Biochem. Biophys. Res. Commun. |volume=161 |issue= 1 |pages= 121–6 |year= 1989 |pmid= 2730651 |doi= }} *{{cite journal | author=Lee FS, Vallee BL |title=Binding of placental ribonuclease inhibitor to the active site of angiogenin. |journal=Biochemistry |volume=28 |issue= 8 |pages= 3556–61 |year= 1989 |pmid= 2742853 |doi= }} *{{cite journal | author=Strydom DJ, Fett JW, Lobb RR, ''et al.'' |title=Amino acid sequence of human tumor derived angiogenin. |journal=Biochemistry |volume=24 |issue= 20 |pages= 5486–94 |year= 1986 |pmid= 2866794 |doi= }} *{{cite journal | author=Kurachi K, Davie EW, Strydom DJ, ''et al.'' |title=Sequence of the cDNA and gene for angiogenin, a human angiogenesis factor. |journal=Biochemistry |volume=24 |issue= 20 |pages= 5494–9 |year= 1986 |pmid= 2866795 |doi= }} *{{cite journal | author=Shapiro R, Vallee BL |title=Human placental ribonuclease inhibitor abolishes both angiogenic and ribonucleolytic activities of angiogenin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=84 |issue= 8 |pages= 2238–41 |year= 1987 |pmid= 3470787 |doi= }} *{{cite journal | author=Rybak SM, Fett JW, Yao QZ, Vallee BL |title=Angiogenin mRNA in human tumor and normal cells. |journal=Biochem. Biophys. Res. Commun. |volume=146 |issue= 3 |pages= 1240–8 |year= 1987 |pmid= 3619929 |doi= }} *{{cite journal | author=Shapiro R, Strydom DJ, Olson KA, Vallee BL |title=Isolation of angiogenin from normal human plasma. |journal=Biochemistry |volume=26 |issue= 16 |pages= 5141–6 |year= 1987 |pmid= 3663649 |doi= }} *{{cite journal | author=Hu GF, Strydom DJ, Fett JW, ''et al.'' |title=Actin is a binding protein for angiogenin. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=90 |issue= 4 |pages= 1217–21 |year= 1993 |pmid= 7679494 |doi= }} *{{cite journal | author=Moroianu J, Riordan JF |title=Identification of the nucleolar targeting signal of human angiogenin. |journal=Biochem. Biophys. Res. Commun. |volume=203 |issue= 3 |pages= 1765–72 |year= 1994 |pmid= 7945327 |doi= 10.1006/bbrc.1994.2391 }} *{{cite journal | author=Moroianu J, Riordan JF |title=Nuclear translocation of angiogenin in proliferating endothelial cells is essential to its angiogenic activity. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 5 |pages= 1677–81 |year= 1994 |pmid= 8127865 |doi= }} *{{cite journal | author=Acharya KR, Shapiro R, Allen SC, ''et al.'' |title=Crystal structure of human angiogenin reveals the structural basis for its functional divergence from ribonuclease. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=91 |issue= 8 |pages= 2915–9 |year= 1994 |pmid= 8159679 |doi= }} *{{cite journal | author=Hu GF, Riordan JF, Vallee BL |title=A putative angiogenin receptor in angiogenin-responsive human endothelial cells. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=94 |issue= 6 |pages= 2204–9 |year= 1997 |pmid= 9122172 |doi= }} }} {{refend}} [[Category:Biomolecules]] [[Category:enzymes]] {{enzyme-stub}} {{Nucleases}} [[uk:Ангіогенін]] {{PBB_Controls | update_page = yes | require_manual_inspection = no | update_protein_box = yes | update_summary = yes | update_citations = yes }}