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Titolo:
EFFECTS OF RECOMBINANT HUMAN HEMOGLOBIN ON OPOSSUM SPHINCTER OF ODDI MOTOR FUNCTION IN-VIVO AND IN-VITRO
Autore:
CULLEN JJ; CONKLIN JL; MURRAY J; LEDLOW A; ROSENTHAL G;
Indirizzi:
UNIV IOWA HOSP & CLIN,DEPT SURG IOWA CITY IA 52242 UNIV IOWA,COLL MED,DEPT SURG IOWA CITY IA 52242 UNIV IOWA,COLL MED,DEPT INTERNAL MED IOWA CITY IA 52242 VET ADM MED CTR IOWA CITY IA 00000 SOMATOGEN INC BOULDER CO 00000
Titolo Testata:
Digestive diseases and sciences
fascicolo: 2, volume: 41, anno: 1996,
pagine: 289 - 294
SICI:
0163-2116(1996)41:2<289:EORHHO>2.0.ZU;2-6
Fonte:
ISI
Lingua:
ENG
Soggetto:
NITRIC-OXIDE; MEDIATOR; MUSCLE;
Keywords:
HEMOGLOBIN; SPHINCTER OF ODDI MOTILITY;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
21
Recensione:
Indirizzi per estratti:
Citazione:
J.J. Cullen et al., "EFFECTS OF RECOMBINANT HUMAN HEMOGLOBIN ON OPOSSUM SPHINCTER OF ODDI MOTOR FUNCTION IN-VIVO AND IN-VITRO", Digestive diseases and sciences, 41(2), 1996, pp. 289-294

Abstract

Nitric oxide (NO) acts as a nonadrenergic, noncholinergic inhibitor neurotransmitter that regulates sphincter of Oddi (SO) motor function, Hemoglobin blocks NO activity by binding it after it is synthesized. We hypothesized that recombinant human hemoglobin (rHb1.1) affects SO motor function by scavenging NO. Under anesthesia, 12 opossums underwent biliary tract manometry, Following a stabilization period, six animals were given rHb1.1 (0.28 g/kg over 30 min), while six received bovine albumin (0.28 g/kg over 30 min), Recordings were made during the infusion and for 3 hr after the infusion. In an in vitro preparation, force transducers were used to record spontaneous contractions at two sites along the sphincter segment. After a control period, rHb1.1 (0.1 mM) or cyanomethemoglobin (0.1 mM) was added to the tissue bath and recordings continued for another 2 hr, Recombinant human hemoglobin decreased the frequency of contractions, increased resting tone, and blockedthe relaxation phase of contraction in vivo. It increased the baseline amplitude, the frequency, and the peak amplitudes of contractions invitro. Albumin or cyanomethoglobin, which are unable to bind NO, had little effect on SO motor activity, We conclude that rHb1.1 may alter SO motor function by binding endogenous NO.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 29/09/20 alle ore 16:39:04