Basic homopolyamino acids, histones and protamines are potent antagonists of angiogenin binding to ribonuclease inhibitor

FEBS Letters

Moenner, Michel³  Chevaillier, Philippe¹  Badet, Josette³  Chauvière, Muriel² 

[1] Laboratoire de Biologie Cellulaire, avenue du Général de Gaulle, Université Paris XII-Val de Marne, 94010 Créteil Cedex, France;Institut de Recherche sur le Cancer, UPR 9044, Groupe G3M, 7 rue G. Moquet, 94801 Villejuif, France;INSERM U 427, Université René Descartes-Paris V, 4 avenue de l'Observatoire, 75270 Paris Cedex 6, France

关键词: Angiogenin;    Ribonuclease inhibitor;    Poly-arginine;    Poly-lysine;    Histone;    Protamine;    BS-RNase;    bovine seminal ribonuclease;    ECP;    eosinophil cationic protein;    EDN;    eosinophil-derived neurotoxin;    RI;    ribonuclease inhibitor;    RNase A;    bovine ribonuclease A;    poly(Lys);    poly-lysine;    poly(Arg);    poly-arginine;    poly(Orn);    poly-ornithine;   

DOI  :  10.1016/S0014-5793(98)01721-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

A radio-ribonuclease inhibitor assay based on the interaction of ¹²⁵I-angiogenin with ribonuclease inhibitor (RI) was used to detect pancreatic-type ribonucleases and potential modulators of their action. We show that highly basic proteins including the homopolypeptides poly-arginine, poly-lysine and poly-ornithine, core histones, spermatid-specific S1 protein and the protamines HP3 and Z3 were strong inhibitors of angiogenin binding to RI. A minimum size of poly-arginine and poly-lysine was required for efficient inhibition. The inhibition likely resulted from direct association of the basic proteins with the acidic inhibitor, as RI bound to poly-lysine and protamines while ¹²⁵I-angiogenin did not. Antagonists of the angiogenin-RI interaction are potential regulators of either angiogenin-triggered angiogenesis and/or intracellular RI function, depending on their preferential target.

【 授权许可】

Unknown