Generation of VV-hemorphin-7 from globin by peritoneal macrophages

Bovine globin has been incubated with mice peritoneal macrophages in order to study its hydrolysis by lysosomal enzymes, among which chiefly cathepsin D. Analysis of resulting peptides, by reversed-phase high-performance liquid chromatography (RP-HPLC), shown the release of a bioactive peptide, VV-h...

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Veröffentlicht in:	FEBS letters 1996-03, Vol.382 (1), p.37-42
Hauptverfasser:	Dagouassat, Nathalie, Garreau, Isabelle, Sannier, Frederic, Zhao, Qiuyu, Pio, Jean Marie
Format:	Artikel
Sprache:	eng
Schlagworte:	Amino Acid Sequence Amino Acids - analysis Animals Cathepsin D Cathepsin D - metabolism Cattle Cells, Cultured Female Globins - metabolism Hemoglobin Hemoglobins - chemistry Hemoglobins - metabolism Hemorphin High-performance liquid chromatography Hydrolysis Leupeptins - pharmacology Lysosomal enzymes Lysosomes - enzymology Macrophages Macrophages, Peritoneal - metabolism Mice Molecular Sequence Data Pepstatins - pharmacology Peptide Fragments - chemistry Peptide Fragments - metabolism Protease Inhibitors - pharmacology Specific Pathogen-Free Organisms
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Zusammenfassung:	Bovine globin has been incubated with mice peritoneal macrophages in order to study its hydrolysis by lysosomal enzymes, among which chiefly cathepsin D. Analysis of resulting peptides, by reversed-phase high-performance liquid chromatography (RP-HPLC), shown the release of a bioactive peptide, VV-hemorphin-7. When a carboxyl proteinase inhibitor such as pepstatin A was added, no hemorphin was generated. Our results clearly demonstrated that VV-hemorphin-7 generation was principally due to cathepsin D. This study allowed us to hypothetize a possible pathway for in vivo hemorphins appearance from globin catabolism by macrophages.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(96)00144-5