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Generation of VV‐hemorphin‐7 from globin by peritoneal macrophages
Author(s) -
Dagouassat Nathalie,
Garreau Isabelle,
Sannier Frederic,
Zhao Qiuyu,
Pio Jean Marie
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(96)00144-5
Subject(s) - pepstatin , globin , chemistry , cathepsin , in vivo , biochemistry , high performance liquid chromatography , cathepsin d , microbiology and biotechnology , enzyme , biology , chromatography , hemoglobin , protease
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.