ANG ELISA Kit, Human |
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BACKGROUND Angiogenin (ANG)/ degranulation inhibitory protein (DIP) is a basic heparin binding protein of 14.4 kDa and belongs to a protein family, designated RNAse superfamily, which also includes eosinophil cationic protein, eosinophil-derived neurotoxin, sialic-acid binding lectin and anti-tumor protein p30. Angiogenin is homologous with pancreatic ribonuclease (RNASE1) and yeast RNASE1. It was also called ribonuclease A family 5a (Rnase5a). Angiogenin was originally isolated from the conditioned medium of HT-29 human colon adenocarcinoma cells. It has been shown to play a role in tumor angiogenesis. Its expression increases in a variety of cancer cells, which results in an elevation of plasma angiogenin in cancer patients. Angiogenin antagonists have been shown to inhibit the establishment, progression, and metastasis of xenografic human tumors in athymic mice. Angiogenin mRNA is also expressed in a wide spectrum of normal cells. Angiogenin is a liver-derived component of normal serum the concentration of which can increase in various disease states and its expression is regulated in vivo in a manner that is characteristic of acute phase proteins. IL6, a major inducer of acute phase proteins, stimulates the synthesis and secretion of angiogenin protein in human HepG2 cells.1
Angiogenin is now recognized as a pleiotropic molecule capable of inducing several intra- and extracellular activities. It induces most of the individual events in the process of angiogenesis including binding to endothelial cells, stimulating second messengers, mediating cell adhesion, activating cell-associated proteinases, inducing cell invasion, stimulating DNA synthesis and cell proliferation, and organizing the formation of tubular structures from cultured endothelial cells. It was shown that angiogenin binds to the endothelial cell surface, interacts with a 170 kDa putative receptor or a 42 kDa binding protein on the cell surface. Angiogenin undergoes nuclear translocation in endothelial cells, which is essential for its biologic activity. When nuclear translocation is inhibited, its angiogenic activity is abolished. It was shown that angiogenin is able to bind to the ribosomal DNA (rDNA) and to stimulate rRNA transcription. Since rRNA transcription regulates ribosome production and, consequently, the translation potential of a cell, angiogenin-induced rRNA transcription is required for endothelial cell proliferation induced by other angiogenic factors. In addition, Angiogenin displays limited ribonuclease activity. The activity of angiogenin can be blocked by ribonuclease inhibitors, including a specific inhibitor of mammalians, designated RAI (ribonuclease/angiogenin inhibitor). Highly basic proteins (poly-arginine, poly-lysine, poly-ornithine, core histones, spermatid-specific S1 protein, and the protamines HP3 and Z3) strongly inhibit angiogenin binding to the inhibitor and may be potential regulators of angiogenin-triggered angiogenesis and/or intracellular inhibitor functions. Blocking of the ribonuclease activity concomitantly also blocks the angiogenic activity of angiogenin. Mutations that enhance ribonuclease activity also enhance the angiogenic activity. Very likely, the biological activity of angiogenin is due to the cell activation of accessory cells, which then secrete cytokines causing cell activation of endothelial cells. The activity of angiogenin as an angiogenesis factor is blocked by Angiostatin.2 In addition to its well-known role in mediating angiogenesis, human angiogenin also directly stimulates prostate cancer cell proliferation.3 Furthermore, it was shown that the serum angiogenin level increases in patients with nasopharyngeal carcinoma, and is correlate with primary tumor progression. In addition, angiogenin has also been reported to suppress significantly the proliferation of human lymphocytes stimulated by a mixed-lymphocyte culture or by phytohemagglutinin or concanavalin A. It also inhibits both spontaneous and peptide-stimulated degranulation of polymorphonuclear leukocytes.4
Angiogenin is now recognized as a pleiotropic molecule capable of inducing several intra- and extracellular activities. It induces most of the individual events in the process of angiogenesis including binding to endothelial cells, stimulating second messengers, mediating cell adhesion, activating cell-associated proteinases, inducing cell invasion, stimulating DNA synthesis and cell proliferation, and organizing the formation of tubular structures from cultured endothelial cells. It was shown that angiogenin binds to the endothelial cell surface, interacts with a 170 kDa putative receptor or a 42 kDa binding protein on the cell surface. Angiogenin undergoes nuclear translocation in endothelial cells, which is essential for its biologic activity. When nuclear translocation is inhibited, its angiogenic activity is abolished. It was shown that angiogenin is able to bind to the ribosomal DNA (rDNA) and to stimulate rRNA transcription. Since rRNA transcription regulates ribosome production and, consequently, the translation potential of a cell, angiogenin-induced rRNA transcription is required for endothelial cell proliferation induced by other angiogenic factors. In addition, Angiogenin displays limited ribonuclease activity. The activity of angiogenin can be blocked by ribonuclease inhibitors, including a specific inhibitor of mammalians, designated RAI (ribonuclease/angiogenin inhibitor). Highly basic proteins (poly-arginine, poly-lysine, poly-ornithine, core histones, spermatid-specific S1 protein, and the protamines HP3 and Z3) strongly inhibit angiogenin binding to the inhibitor and may be potential regulators of angiogenin-triggered angiogenesis and/or intracellular inhibitor functions. Blocking of the ribonuclease activity concomitantly also blocks the angiogenic activity of angiogenin. Mutations that enhance ribonuclease activity also enhance the angiogenic activity. Very likely, the biological activity of angiogenin is due to the cell activation of accessory cells, which then secrete cytokines causing cell activation of endothelial cells. The activity of angiogenin as an angiogenesis factor is blocked by Angiostatin.2 In addition to its well-known role in mediating angiogenesis, human angiogenin also directly stimulates prostate cancer cell proliferation.3 Furthermore, it was shown that the serum angiogenin level increases in patients with nasopharyngeal carcinoma, and is correlate with primary tumor progression. In addition, angiogenin has also been reported to suppress significantly the proliferation of human lymphocytes stimulated by a mixed-lymphocyte culture or by phytohemagglutinin or concanavalin A. It also inhibits both spontaneous and peptide-stimulated degranulation of polymorphonuclear leukocytes.4
REFERENCES
1. Shapiro, R. et al: Biochem. 25:3527–32, 1986
2. Kong, H.L. & Crystal, R.G.: J. NCI 90:274-86, 1998
3. Yoshioka, N. et al: Proc. Natl. Acad. Sci. USA 103:14519-24, 2006
4. Tschesche, H. et al: J. Biol. Chem. 269:30274-80, 1994
2. Kong, H.L. & Crystal, R.G.: J. NCI 90:274-86, 1998
3. Yoshioka, N. et al: Proc. Natl. Acad. Sci. USA 103:14519-24, 2006
4. Tschesche, H. et al: J. Biol. Chem. 269:30274-80, 1994
Products are for research use only. They are not intended for human, animal, or diagnostic applications.
Параметры
Cat.No.: | CL0305 |
Target Protein Species: | Human |
Range: | 62.5pg/ml-4000pg/ml |
Specificity: | No detectable cross-reactivity with any other cytokine. |
Storage: | Store at 4°C. Use within 6 months. |
ELISA Kits are based on standard sandwich enzyme-linked immunosorbent assay technology. Freshly prepared standards, samples, and solutions are recommended for best results.
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