Characteristic ribonucleolytic activity of human angiogenin

Shapiro, Robert; Riordan, James; Vallée, Bert L.

doi:10.1021/bi00360a008

Cited by 344 publications

(325 citation statements)

References 27 publications

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“…In both angiogenins, the six cysteine residues involved in disulfide bridges are found in the same positions reflecting the highly conserved tertiary structure of these molecules. As shown previously, one of the most surprising features of the human angiogenin sequence was its homology with the sequence of human pancreatic RNase A [4]. Here we demonstrate ( fig.2) that the sequence of bovine angiogenin shares a similar homology (34% identity) with the sequence of bovine RNase A [8].…”

Section: Characteristics Of the Sequencesupporting

confidence: 81%

“…Identities between bovine angiogenin and either of the other proteins are boxed, xxx, residues known to be involved in catalysis by bovine RNase. As these strong local homologies probably reflect similar unusual ribonucleolytic activities as those found with human angiogenin [4], we have determined the catalytic properties of bovine angiogenin. When the protein isolated from bovine milk was tested against polyribonucleotides, dinucleotides and wheat germ RNA no ribonucleolytic activity could be detected.…”

Section: Characteristics Of the Sequencementioning

confidence: 86%

“…This homology was shown to be biologically functional as human angiogenin displays specific ribonucleolytic activities, catalyzing the cleavage of 28 and 18 S rRNA [4]. Both angiogenic and RNase activities are selectively inhibited by placenta ribonuclease inhibitor [5].…”

Section: Introductionmentioning

confidence: 96%

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The complete amino acid sequence of bovine milk angiogenin

et al. 1988

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The amino acid sequence of angiogenin isolated from bovine milk was deduced by gas-phase sequencing of the protein and its fragments. The protein contains 125 residues and has a calculated molecular mass of 14577 Da. The sequence is highly homologous (65% identity) to the sequence of human angiogenin, most of the differences being the result of conservative replacements. Like human angiogenin, the bovine protein is also homologous to bovine pancreatic RNase A (34% identity) and the three major active site residues known to be involved in the catalytic process, His-14, Lys-41 and His-115, are conserved. When tested against conventional substrates for RNase A activity, bovine angiogenin displays the same selective ribonucleolytic activity as human angiogenin. The sequence of bovine angiogenin contains the cell recognition tripeptide Arg-Gly-Asp which is not present in the human protein.

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Section: Characteristics Of the Sequencesupporting

confidence: 81%

Section: Characteristics Of the Sequencementioning

confidence: 86%

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The complete amino acid sequence of bovine milk angiogenin

et al. 1988

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“…Its primary sequence is 35% identical to that of human pancreatic ribonuclease , and, indeed, it exhibits ribonucleolytic activity, albeit markedly different from that of the pancreatic enzyme (Shapiro et al, 1986).…”

mentioning

confidence: 96%

Human angiogenin, an organogenic protein

Riordan

Vallee²

1988

Br J Cancer

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Angiogenin is a 14 kD protein, initially isolated as a tumour-cell secreted product but subsequently found to be a normal constituent of human plasma. It is a potent inducer of blood vessel formation on the chorioallantoic membrane of the chick embryo. Chemical characterization of the protein reveals a remarkable homology to the pancreatic ribonuclease family and has led to the identification of a unique ribonucleolytic activity for angiogenin. It is a particularly potent inhibitor of in vitro protein synthesis. Treatment with placental ribonuclease inhibitor abolishes the biological and enzymatic activities of angiogenin, an effect with important mechanistic, physiological and pharmacologic implications.

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“…The protein is a 123-amino acid polypeptide with a molecular mass of 14.1 kDa and known to be an angiogenic factor [9]. Angiogenin expression is upregulated in a variety of tumor cells and its concentration in plasma is elevated in many types of cancer patients [10ϳ13].…”

Section: Introductionmentioning

confidence: 99%

A New Terrein Glucoside, a Novel Inhibitor of Angiogenin Secretion in Tumor Angiogenesis

et al. 2008

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Angiogenesis is a critical step for the tumor therapy. Many angiogenic factors are involved in the tumor angiogenesis. In the course of our screening for inhibitors of angiogenin secretion, one of angiogenic factors, we have isolated a new terrein glucoside (1) and terrein (2) from the fermentation broth of fungal strain Aspergillus sp. PF1381. The structure and absolute stereochemistry of 1 was determined to be (4S,5R)-5-[(a -D-glucopyranosyl)oxy]-4-hydroxy-3-(E-1-propenyl)-2-cyclopenten-1-one on the basis of spectral and enzymatic analyses. Compounds 1 and 2 equally inhibited angiogenin secretion from androgendependent prostate cancer cells, LNCaP-CR, with IC 50 values of 13 mM. However, both compounds did not affect VEGF secretion, another angiogenic factor. Furthermore, both compounds inhibited tube formation of human umbilical vein endothelial cells (HUVEC). These results suggested that 1 and 2 act as angiogenesis inhibitors through the inhibition of angiogenin secretion.

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Characteristic ribonucleolytic activity of human angiogenin

Cited by 344 publications

References 27 publications

The complete amino acid sequence of bovine milk angiogenin

The complete amino acid sequence of bovine milk angiogenin

Human angiogenin, an organogenic protein

A New Terrein Glucoside, a Novel Inhibitor of Angiogenin Secretion in Tumor Angiogenesis

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