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Titolo:
PURIFICATION AND CHARACTERIZATION OF A LUMINAL CHOLECYSTOKININ-RELEASING FACTOR FROM RAT INTESTINAL SECRETION
Autore:
SPANNAGEL AW; GREEN GM; GUAN DF; LIDDLE RA; FAULL K; REEVE JR;
Indirizzi:
UNIV TEXAS,HLTH SCI CTR,DEPT PHYSIOL SAN ANTONIO TX 78284 UNIV TEXAS,HLTH SCI CTR,DEPT PHYSIOL SAN ANTONIO TX 78284 DUKE UNIV,MED CTR,DEPT MED DURHAM NC 27710 UNIV CALIF LOS ANGELES,DEPT MED LOS ANGELES CA 90024 UNIV CALIF LOS ANGELES,CTR DIGEST DIS,CTR ULCER RES & EDUC LOS ANGELES CA 90024
Titolo Testata:
Proceedings of the National Academy of Sciences of the United Statesof America
fascicolo: 9, volume: 93, anno: 1996,
pagine: 4415 - 4420
SICI:
0027-8424(1996)93:9<4415:PACOAL>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
PANCREATIC-ENZYME-SECRETION; MEDIATES FEEDBACK-REGULATION; TRYPSIN-INHIBITOR; CONSCIOUS RATS; ANTAGONIST LOXIGLUMIDE; EXOCRINE SECRETION; PEPTIDE; JUICE; SUPPRESSION; MECHANISM;
Keywords:
FEEDBACK REGULATION; PANCREATIC SECRETION;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Science Citation Index Expanded
Citazioni:
38
Recensione:
Indirizzi per estratti:
Citazione:
A.W. Spannagel et al., "PURIFICATION AND CHARACTERIZATION OF A LUMINAL CHOLECYSTOKININ-RELEASING FACTOR FROM RAT INTESTINAL SECRETION", Proceedings of the National Academy of Sciences of the United Statesof America, 93(9), 1996, pp. 4415-4420

Abstract

Cholecystokinin (CCK) secretion in rats and humans is inhibited by pancreatic proteases and bile acids in the intestine. It has been hypothesized that the inhibition of CCK release caused by pancreatic proteases is due to proteolytic inactivation of a CCK-releasing peptide present in intestinal secretion. To purify the putative luminal CCK-releasing factor (LCRF), intestinal secretions were collected by perfusing a modified Thiry-Vella fistula of jejunum in conscious rats. From these secretions, the peptide was concentrated by ultrafiltration followed by low-pressure reverse-phase chromatography and purified by reverse-phase high-pressure liquid chromatography. Purity was confirmed by high-performance capillary electrophoresis. Fractions were assayed for CCK-releasing activity by their ability to stimulate pancreatic protein secretion when infused into the proximal small intestine of conscious rats. Partially purified fractions strongly stimulated both pancreatic secretion and CCK release while CCK receptor blockade abolished the pancreatic response. Amino acid analysis and mass spectral analysis showed that the purified peptide is composed of 70-75 amino acid residues and has a mass of 8136 Da. Microsequence analysis of LCRF yielded an amino acid sequence for 41 residues as follows: STFWAYQPDGDNDPTDYQKYEHTSSPSQLLAPGDYPCVIEV. When infused intraduodenally,the purified peptide stimulated pancreatic protein and fluid secretion in a dose-related manner in conscious rats and significantly elevated plasma CCK levels. Immunoaffinity chromatography using antisera raised to synthetic LCRF(1-6) abolished the CCK releasing activity of intestinal secretions. These studies demonstrate, to our knowledge, the first chemical characterization of a luminally secreted enteric peptide functioning as an intraluminal regulator of intestinal hormone release.

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Documento generato il 03/12/20 alle ore 06:06:16