Histamine release induced by proteolytic digests of human serum albumin: isolation and structure of an active peptide from pepsin treatment.
Treatment of human serum albumin with a proteolytic enzyme such as pepsin, alpha-chymotrypsin, cathepsin D or trypsin generated histamine releasing peptides. A low-molecular weight peptide (P-1) responsible for releasing histamine was isolated from peptic digests of human serum albumin by affinity chromatography on heparin-Ultrogel and reversed-phase high performance liquid chromatography. The amino acid sequence of the P-1 was estimated to be V-R-Y-T-K-K-V-P-Q-V-S-T-P-T-L by Edman degradation. The sequence determined appears to correspond to residues 409-423 of human serum albumin. Peptide P-1 produced dose-related histamine release from isolated rat mast cells in the concentration range of 1-50 microM. The intradermal injection of the P-1 (0.5 micrograms) increased capillary permeability in rats. This response was blocked by the antihistamine diphenhydramine.
Sugiyama
K
K
Department of Pharmacology, Okayama University Dental School, Japan.
Ogino
T
T
Ogata
K
K
D000818:Animals; D002199:Capillary Permeability / Q000187:drug effects; D006636:Histamine Release / Q000187:drug effects*; D006801:Humans; D008407:Mast Cells / Q000378:metabolism*; D010434:Pepsin A / Q000378:metabolism*; D010446:Peptide Fragments / Q000032:analysis* / Q000494:pharmacology; D010447:Peptide Hydrolases / Q000378:metabolism; D051381:Rats; D011919:Rats, Inbred Strains; D012709:Serum Albumin / Q000378:metabolism / Q000494:pharmacology*
D010446:Peptide Fragments; D012709:Serum Albumin; D010447:Peptide Hydrolases; D010434:Pepsin A