Hemopressin: a novel bioactive peptide derived from the alpha1-chain of hemoglobin
AUTOR(ES)
Dale, Camila Squarzoni, Pagano, Rosana de Lima, Rioli, Vanessa
FONTE
Memórias do Instituto Oswaldo Cruz
DATA DE PUBLICAÇÃO
2005-03
RESUMO
Hemopressin (PVNFKFLSH), a novel bioactive peptide derived from the alpha1-chain of hemoglobin, was originally isolated from rat brain homogenates. Hemopressin causes hypotension in anesthetized rats and is metabolized in vivo and in vitro by endopeptidase 24.15 (EP24.15), neurolysin (EP24.16), and angiotensin-converting enzyme (ACE). Hemopressin also exerts an antinociceptive action in experimental inflammatory hyperalgesia induced by carrageenin or bradykinin via a mechanism that is independent of opioids. These findings suggest that this peptide may have important regulatory physiological actions in vivo.
Documentos Relacionados
- FORMATION OF THE PEPTIDE CHAIN OF HEMOGLOBIN
- Proenkephalin system in human polymorphonuclear cells. Production and release of a novel 1.0-kD peptide derived from synenkephalin.
- Resolution of products of the duplicated hemoglobin alpha-chain loci by isoelectric focusing.
- Chromostatin, a chromogranin A-derived bioactive peptide, is present in human pancreatic insulin (beta) cells.
- Biochemical and physiological correlates of deer mouse alpha-chain hemoglobin polymorphisms.