C-terminal angiogenin peptides inhibit the biological and enzymatic activities of angiogenin

Susanna M. Rybak, David S. Auld, Daret K.St Clair, Qi Zhi Yao, James W. Fett

Research output: Contribution to journalArticlepeer-review

9 Scopus citations

Abstract

Synthetic peptides corresponding to the C-terminal region of angiogenin (Ang) inhibit the enzymatic and biological activities of the molecule while peptides from the N-terminal region do not affect either activity. The peptide Ang(108-121) transiently abolishes the inhibition of cell-free protein synthesis caused by angiogenin coincidentally with its cleavage of reticulocyte RNA. Several C-terminal peptides also inhibit nuclease activity of angiogenin when tRNA is the substrate. Furthermore, peptide Ang(108-123) significantly decreases neovascularization elicited by angiogenin in the chick chorioallantoic membrane assay.

Original languageEnglish
Pages (from-to)535-543
Number of pages9
JournalBiochemical and Biophysical Research Communications
Volume162
Issue number1
DOIs
StatePublished - Jul 14 1989

Bibliographical note

Funding Information:
We thank Dr. B.L. Vallee for continued advice and support, Dr. J.L. Bethune for statistical analysis of the CAM results, and Mr. Douglas S. Auld for assistance in preparing synthetic peptides. This work was supported by the Endowment for Research in Human Biology, Inc. and in part by funds from Hoechst, A.G. under agreements with Harvard University.

ASJC Scopus subject areas

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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