Proteolytic degradation of hemoglobin by endogenous lysosomal proteases gives rise to bioactive peptides: hemorphins.
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.
Fruitier
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I
Laboratoire de Génie Protéique et Cellulaire, UPRES 2001, UFR Sciences, Université La Rochelle, France.
Garreau
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Lacroix
A
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Cupo
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Piot
J M
JM
D000818:Animals; D010450:Endopeptidases / Q000378:metabolism*; D006454:Hemoglobins / Q000096:biosynthesis* / Q000302:isolation & purification / Q000378:metabolism*; D008099:Liver / Q000166:cytology / Q000201:enzymology*; D008247:Lysosomes / Q000201:enzymology*; D008264:Macrophages / Q000166:cytology / Q000201:enzymology; D008297:Male; D018847:Opioid Peptides / Q000096:biosynthesis* / Q000302:isolation & purification; D010446:Peptide Fragments / Q000096:biosynthesis* / Q000302:isolation & purification; D051381:Rats; D017208:Rats, Wistar; D019032:Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization
D006454:Hemoglobins; D018847:Opioid Peptides; D010446:Peptide Fragments; C085122:hemorphin 7; D010450:Endopeptidases