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

被引:33
作者
Fruitier, I
Garreau, I
Lacroix, A
Cupo, A
Piot, JM
机构
[1] Univ La Rochelle, UFR Sci, UPRES 2001, Lab Genie Prot & Cellulaire, F-17042 La Rochelle, France
[2] Ctr Etud Biol Chize, CNRS UPR 4701, F-79360 Beauvoir Sur Niort, France
[3] CNRS, Inst Pharmacol Mol & Cellulaire, UPR 411, F-06560 Valbonne, France
关键词
lysosome; hemoglobin; proteolysis; hemorphin; radioimmunoassay; HPLC;
D O I
10.1016/S0014-5793(99)00271-9
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
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. (C) 1999 Federation of European Biochemical Societies.
引用
收藏
页码:81 / 86
页数:6
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