Interaction of a newly isolated intestinal polypeptide (PHI) with glucose and arginine to effect the secretion of insulin and glucagon

Szecówka, J; Tatemoto, Keigo; Mutt, Viktor; Efendić, Suad

doi:10.1016/0024-3205(80)90162-9

Cited by 60 publications

(17 citation statements)

References 3 publications

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“…An aliquot ofeach lyophilized fraction was assayed for PHI. The PHI-containing fractions (6)(7)(8)42 mg) were pooled and subjected to chromatography on a DEAE-cellulose column equilibrated with 0.01 M NH4HCO3, pH 8, as shown in Fig. 3.…”

Section: Methodsmentioning

confidence: 99%

“…Fractions 4-8 were found to contain PHI and were combined and lyophilized. The preparation (8.3 mg) was dissolved in 0.01 M HOAc to make a solution of 4 mg/ml, and the pH of the solution was slowly adjusted to 7 by addition of 0.2 M NH4HCO3. In this step, PHI was precipitated and separated by centrifugation.…”

Section: Methodsmentioning

confidence: 99%

“…This view was strengthened Table 1 Gly-GIn-Lou-Sor-Ala-Lys-Lys-Tyr-Lou-Glu-Sor-Lou-I I *-NH2 inhibited the binding ofVIP to its receptor and stimulated cyclic AMP production in rat liver and intestinal membranes. Szec6wka et ad (7) have reported that PHI is capable ofreleasing insulin and glucagon from the isolated rat pancreas. PHI stimulates amylase secretion and also the production ofcyclic AMP from dispersed acini ofguinea pig pancreas (8).…”

Section: Methodsmentioning

confidence: 99%

“…This paper describes the isolation and complete amino acid sequence of a peptide amide that contains isoleucine amide at its COOH terminus. The peptide amide, PHI (PHI-27; for derivation ofthe name, see Discussion), has been found to be biologically active (6)(7)(8)(9). This suggests that a chemical screening approach involving systematic isolation ofpeptide amides from natural sources may lead to the discovery of new peptides of biological interest.…”

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confidence: 99%

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Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family.

Tatemoto¹,

Mutt²

1981

Proc. Natl. Acad. Sci. U.S.A.

334

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A new peptide, designated PHI (PHI-27), has been discovered and isolated from porcine upper intestinal tissue by using a chemical method for finding peptide hormones and other active peptides. The method is based on chemical detection ofpeptides having the COOH-terminal a-amide structure, which is an unusual chemical feature of some peptide hormones and active peptides. Porcine PHI was found in the intestinal extract by the presence ofits COOH-terminal isoleucine amide structure. It consists of27 amino acid residues and has the following amino acid sequence: His-Ala-Asp-Gly-Val.Phe-Thr-Ser-Asp-Phe-Ser-Arg-LeuLou-Gly-Gln-Leu-Ser-Ala-Lys-Lys-Tyr-Leu-Glu-Ser-Lou-lle-NH2. Me2CO, CHC13, and EtOH for high-performance liquid chromatography (HPLC) were of spectroscopic grade; all other reagents were ofanalytical grade and were used without fiurther purification. The enzyme preparations used were subtilisin BPN' (EC 3.4.21.14; Sigma), trypsin (EC 3.4.21.4; N-tosylphenylalanine chloromethyl ketone-treated, Worthington), chymotrypsin (EC 3.4.21.1; Merk), and carboxypeptidase Y (EC 3.4.12. 1; Boehringer Mannheim).Chemical Assay ofPHI. PHI was determined by the amount ofisoleucine amide released after treatment ofthe sample with subtilisin BPN' by using .the following procedure, which was derived from a slight modification of the amide determination method previously described (3). Samples (<1 mg) in siliconized glass tubes (5 x 50 mm) were dissolved in 20 Adl-of Hepes, pH 7.5, containing 40 ,g ofsubtilisin BPN', and the tubes were sealed with parfilm and incubated at room temperature for 48 hr. At the end ofthe incubation, 1 nmol of y-aminobutyric acid amide was added to each tube as an internal standard. The reaction mixtures were evaporated to dryness under reduced pressure, and the residues were dissolved in 20-100 p1 of 0.1 M sodium bicarbonate/carbonate, pH 9.5, and treated with equal volumes of DnsCl (2-5 mg/ml) in Me2CO; the mixtures were incubated at 37C for 1 hr. The amount of DnsCl added should not greatly exceed the estimated content of DanCl-reactive groups in the sample to avoid side reactions due to modAbbreviations: PHI, PHI-27, the peptide (P) having NH2-terminal histidine (H) and COOH-terminal isoleucine (I) amide and 27 amino acid residues; VIP, vasoactive intestinal peptide; HPLC, high-performance liquid chromatography; TLC, thin-layer chromatography; Dns, dansyl. * A preliminary communication on this study has been published: Ta The publication costs ofthis article were defr-ayed in part by page charge payment. This article must -therefore be hereby marked "advertisement" in accordance with 18 U. S. C. §1734 solely to indicate this fact.

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Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

mentioning

confidence: 99%

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Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family.

Tatemoto¹,

Mutt²

1981

Proc. Natl. Acad. Sci. U.S.A.

334

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“…Further, the peptide has been shown to exhibit a number of biological activities similar to VIP. For example, it stimulates insulin secretion [4,5] and pancreatic exocrine secretion [2,6]. PHI causes vasodilation [7], increases intestinal fluid transport [8,9] and relaxes tracheal [7,10] and gallbladder [l l] smooth muscle.…”

Section: Introductionmentioning

confidence: 99%

Isolation and primary structure of human PHI (peptide HI)

et al. 1984

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The isolation of the human form of PHI (peptide HI) is described. The peptide was purified from human colonic extracts by using a chemical method for the detection of its C-terminal amidated structure. Human PHI consists of 27 amino acid residues and the complete amino acid sequence is: His-Ala-Asp-Gly-Val-PheThr-Ser-Asp-Phe-Ser-Lys-Leu-Leu-Gly-Gln-Leu-Ser-Ala-Lys-Lys-Tyr-Leu-Glu-Ser-Leu-Met-NH*.The differences between the structures of porcine and human PHI are at position 12 (Arg/Lys replacement) and at position 27 (Ile/Met).

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Vasoactive Intestinal Peptide

Fahrenkrug

1989

Comprehensive Physiology

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Interaction of a newly isolated intestinal polypeptide (PHI) with glucose and arginine to effect the secretion of insulin and glucagon

Cited by 60 publications

References 3 publications

Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family.

Isolation and characterization of the intestinal peptide porcine PHI (PHI-27), a new member of the glucagon--secretin family.

Isolation and primary structure of human PHI (peptide HI)

Vasoactive Intestinal Peptide

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