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Human angiogenin, an organogenic protein.

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 reveal...

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Detalles Bibliográficos
Autores principales: Riordan, J. F., Vallee, B. L.
Formato: Texto
Lenguaje:English
Publicado: Nature Publishing Group 1988
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246469/
https://www.ncbi.nlm.nih.gov/pubmed/2457389
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author Riordan, J. F.
Vallee, B. L.
author_facet Riordan, J. F.
Vallee, B. L.
author_sort Riordan, J. F.
collection PubMed
description 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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spelling pubmed-22464692009-09-10 Human angiogenin, an organogenic protein. Riordan, J. F. Vallee, B. L. Br J Cancer Research Article 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. Nature Publishing Group 1988-06 /pmc/articles/PMC2246469/ /pubmed/2457389 Text en https://creativecommons.org/licenses/by/4.0/This article is licensed under a Creative Commons Attribution 4.0 International License, which permits use, sharing, adaptation, distribution and reproduction in any medium or format, as long as you give appropriate credit to the original author(s) and the source, provide a link to the Creative Commons license, and indicate if changes were made. The images or other third party material in this article are included in the article’s Creative Commons license, unless indicated otherwise in a credit line to the material. If material is not included in the article’s Creative Commons license and your intended use is not permitted by statutory regulation or exceeds the permitted use, you will need to obtain permission directly from the copyright holder. To view a copy of this license, visit https://creativecommons.org/licenses/by/4.0/.
spellingShingle Research Article
Riordan, J. F.
Vallee, B. L.
Human angiogenin, an organogenic protein.
title Human angiogenin, an organogenic protein.
title_full Human angiogenin, an organogenic protein.
title_fullStr Human angiogenin, an organogenic protein.
title_full_unstemmed Human angiogenin, an organogenic protein.
title_short Human angiogenin, an organogenic protein.
title_sort human angiogenin, an organogenic protein.
topic Research Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2246469/
https://www.ncbi.nlm.nih.gov/pubmed/2457389
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