ANG ( angiogenin , ribonuclease , RNase A family , 5 )
نویسنده
چکیده
The amino acid sequence is available at NCBI protein locus AAA51678. It consists of a signal peptide from amino acid 1 to 24 and a mature peptide from amino acid 25 to 147. ANG is a basic, single chain potent blood-vessel inducing protein with a molecular weight of 14 kDa which was originally discovered in conditioned media of a human colon carcinoma cell line HT-29. ANG belongs to the RNAse superfamily, being 35% identical and 68% homologous to the pancreatic RNAse A sequence. The overall crystal structure of ANG shows a similarity to, but the biological actions of ANG differ distinctly from those of RNAse A. ANG possesses two distinct regions: a ribonucleolytic and a noncatalytic site, both being critical for angiogenic activity. Besides the ribonucleolytic activity, ANG differs from RNAse A in noncatalytic activities such as interactions with endothelial and smooth muscle cells and subsequent cellular responses in the events of neovascularization, including basement membrane degradation, signal transduction, and nuclear translocation.
منابع مشابه
Replacing a surface loop endows ribonuclease A with angiogenic activity.
Angiogenin (ANG) promotes the formation of blood vessels in animals. This hormone is a small, monomeric protein that is homologous to bovine pancreatic ribonuclease A (RNase). ANG is a poor ribonuclease but its ribonucleolytic activity is essential for its angiogenic activity. RNase is not angiogenic. A hybrid protein was produced in which 13 residues of a divergent surface loop of ANG were sub...
متن کاملMolecular recognition of human angiogenin by placental ribonuclease inhibitor--an X-ray crystallographic study at 2.0 A resolution.
Human placental RNase inhibitor (hRI), a leucine-rich repeat protein, binds the blood vessel-inducing protein human angiogenin (Ang) with extraordinary affinity (Ki <1 fM). Here we report a 2.0 A resolution crystal structure for the hRI-Ang complex that, together with extensive mutagenesis data from earlier studies, reveals the molecular features of this tight interaction. The hRI-Ang binding i...
متن کاملRibonuclease inhibitor regulates neovascularization by human angiogenin.
Human angiogenin (ANG) is a homologue of bovine pancreatic ribonuclease (RNase A) that induces neovascularization. ANG is the only human angiogenic factor that possesses ribonucleolytic activity. To stimulate blood vessel growth, ANG must be transported to the nucleus and must retain its catalytic activity. Like other mammalian homologues of RNase A, ANG forms a femtomolar complex with the cyto...
متن کاملThe ribonucleolytic activity of angiogenin.
Angiogenin (ANG), a homologue of bovine pancreatic ribonuclease A (RNase A), promotes the growth of new blood vessels. The biological activity of ANG is dependent on its ribonucleolytic activity, which is far lower than that of RNase A. Here, the efficient heterologous production of human ANG in Escherichia coli was achieved by replacing two sequences of rare codons with codons favored by E. co...
متن کاملAngiogenin is a cytotoxic, tRNA-specific ribonuclease in the RNase A superfamily.
Angiogenin is a 14.4-kDa human plasma protein with 65% homology to RNase A that retains the key active site residues and three of the four RNase A disulfide bonds. We demonstrate that recombinant angiogenin functions as a cytotoxic tRNA-specific RNase in cell-free lysates and when injected into Xenopus oocytes. Inhibition of protein synthesis by angiogenin correlates with degradation of endogen...
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