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

Citation
I. Fruitier et al., Proteolytic degradation of hemoglobin by endogenous lysosomal proteases gives rise to bioactive peptides: hemorphins, FEBS LETTER, 447(1), 1999, pp. 81-86
Citations number
30
Categorie Soggetti
Biochemistry & Biophysics
Journal title
FEBS LETTERS
ISSN journal
00145793 → ACNP
Volume
447
Issue
1
Year of publication
1999
Pages
81 - 86
Database
ISI
SICI code
0014-5793(19990319)447:1<81:PDOHBE>2.0.ZU;2-8
Abstract
Hemorphin generation by mice peritoneal macrophages has been recently repor ted, nevertheless no conclusive data exist to localize clearly the macropha ge proteolytic activity implicated in their generation. Because lysosomes a re believed to be the main site of degradation in the endocytic pathway, we have studied their potential implication in the generation of hemorphins f rom hemoglobin. When this protein is submitted to purified rat liver lysoso mes, an early generation of hemorphin-7-related peptides, detected by a rad ioimmunoassay, was observed. These peptides seemed to be relatively stable during the first hours of hydrolysis. (C) 1999 Federation of European Bioch emical Societies.