Proteolytic degradation of hemoglobin by endogenous lysosomal proteases gives rise to bioactive peptides: hemorphins

FEBS Letters

Garreau, Isabelle²  Cupo, Anny¹  Lacroix, André³  Fruitier, Ingrid²  Piot, Jean Marie² 

[1] Institut de Pharmacologie Moléculaire et Cellulaire CNRS-UPR 411, 660 Route des Lucioles, Sophia Antipolis, 06560 Valbonne, France;Laboratoire de Génie Protéique et Cellulaire, UPRES 2001, UFR Sciences, Université La Rochelle, Avenue Marillac, 17042 La Rochelle, France;Centre d'Etudes Biologiques de Chizé CNRS-UPR 4701, 79360 Beauvoir-Sur-Niort, France

关键词: Lysosome;    Hemoglobin;    Proteolysis;    Hemorphin;    Radioimmunoassay;    HPLC;   

DOI  :  10.1016/S0014-5793(99)00271-9

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

Hemorphin generation by mice peritoneal macrophages has been recently reported, nevertheless no conclusive data exist to localize clearly the macrophage proteolytic activity implicated in their generation. Because lysosomes are believed to be the main site of degradation in the endocytic pathway, we have studied their potential implication in the generation of hemorphins from hemoglobin. When this protein is submitted to purified rat liver lysosomes, an early generation of hemorphin-7-related peptides, detected by a radioimmunoassay, was observed. These peptides seemed to be relatively stable during the first hours of hydrolysis.

【 授权许可】

Unknown