Hormonal polypeptides of the upper intestine

Mutt, Viktor; Jorpes, Erik

doi:10.1042/bj1250057p

Cited by 272 publications

(60 citation statements)

References 17 publications

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“…It is also evident that if the amino acid sequence of (porcine) cholecystokinin-pancreozymin [30] is aligned in parallel with the sequences of the octacosapeptide and glucagon in such a fashion that the Cterminal phenylalanine amide of cholecystokinin- Table 2. Amino-acid sequences of substance P , glucagon, the vasoactive intestinal octacosapeptide, secretin, cholecystokinin-pancreo-…”

Section: Hs D G T F T S E L S R Lmentioning

confidence: 99%

Structure of the Porcine Vasoactive Intestinal Octacosapeptide

Mutt

Said

1974

European Journal of Biochemistry

386

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The amino acid sequence of the porcine vasoactive intestinal octacosapeptide is His-Ser-AspAla-Val-Phe-Thr-Asp-Asn-Tyr-Thr-Arg-Leu-Arg-Lys-~ln-Met -Ala -Val -Lys -Lys -Tyr -Leu -AsnSer-Ile-Leu-Asn-NH,. Its amino acid residues 1, 2, 6 and 7, counted from the N-terminus, are identical to those in the corresponding positions in both porcine glucagon and secretin. The residues in positions 3, 12, 13, 14 and 23 are identical to those in secretin, but not in glucagon, and position 10 is occupied by a tyrosyl and position 28 by an asparaginyl residue, like in glucagon but not in secretin. If in addition to identical amino acid residues also chemically similar residues, such as isoleucine in position 26 of the octacosapeptide, as compared to leucine in secretin and glucagon, are taken into consideration then the similarity between these three polypeptides is still more evident.At a more remote level there is some structural resemblance also between these peptides and the other four peptides from the intestinal wall, cholecystokinin-pancreozymin, motilin, the gastric inhibitory peptide and substance P, the structures of which are known.The elucidation of the structure of the octacosapeptide was facilitated by the finding that pancreatic kallikrein preferentially cleaved only one of the three bonds in its N-terminal cyanogen bromide heptadecapeptide that are susceptible to cleavage with trypsin.In a previous paper [l] we reported that the porcine vasoactive intestinal octacosapeptide, like secretin and like glucagon, has an N-terminal histidylseryl structure. The complete amino acid sequence of the polypeptide has now been elucidated. Partial sequences have already been reported in publications on its synthesis [2,3] and the complete sequence too has recently been disclosed in a preliminary communication by Bodanszky et al. on the completion of the synthesis [4]. The present paper gives the evidence for the proposed sequence. MATERIALS AND METHODSPorcine vasoactive intestinal octacosapeptide was prepared as described earlier [l].Pancreatic kallikrein (sialidase -treated pig pancreatic kallikrein R, batch H 376) was a gift from Professor E. Werle, Munich. Tosyl-lysyl-chloromethyl ketone-treated chymotrypsin, proteinase K and L -(1 -tosylamido -2 -pheny1)ethyl chloromethylketone-treated trypsin, and carboxypeptidase A treated with diisopropyl phosphofluoridate from Worthington.L-Aspartic acid diamide -HCl, hemihydrate, was obtained from Cyclo Chemical, isoleucylleucine and leucylisoleucine from Fox Chemical Company and cyanogen bromide from Eastman Kodak.L-Asparagine-tert-butyl ester-HC1, L-aspartic aciddi-tert-butyl ester-HC1, tert-butyloxycarbonyl-L-asparagine p-nitrophenyl ester, and tert-butyloxycarbonyl-L-aspartic acid-p-tert-butyl-a-p-nitrophenyl ester were obtained from either Fox Chemical Company or from Bachem (Liestal, Switzerland).The sources and qualities of the other materials used have been described previously, as have the methods for paper chromatography and paper electrophoresis of peptides and for their h...

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Section: Hs D G T F T S E L S R Lmentioning

confidence: 99%

Structure of the Porcine Vasoactive Intestinal Octacosapeptide

Mutt

Said

1974

European Journal of Biochemistry

386

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“…This experiment does not reveal subtle differences in base sequence nor does it rule out the possibility that other CCK mRNAs exist that are not sufficiently homologous to be detected by these probes. DISCUSSION CCK was originally isolated from the small intestine (36) and later shown to occur in the brain (37). In the gut, release of CCK causes contraction of the gallbladder and release of pancreatic enzymes (25).…”

Section: Design and Synthesis Of The Icosadeoxynucleotides D(t-c-c-mentioning

confidence: 99%

Cloning and sequence analysis of a cDNA encoding rat preprocholecystokinin.

Deschenes

Lorenz

Haun

et al. 1984

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

286

110

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Poly(A) RNA was isolated from a rat medullary thyroid carcinoma that exhibited high levels of immunoreactive cholecystokinin (CCK). Double-stranded cDNA was synthesized from the poly(A) RNA and inserted into the Pst I site of pBR322. Bacterial colonies containing CCK cDNA were identified using the hybridization probe d(T-C-C-A-T-C-C-A-N-C-C-C-A-T-G-T-A-G-T-C). The sequence of the probe was deduced from the known amino acid sequence of porcine CCK-8, Asp-Tyr-Met-Gly-Trp-Met-Asp-Phe-NH2. The nucleotide sequence of the cDNA complementary to the mRNA of rat preprocholecystokinin was determined. The cDNA contains 33 nucleotides in the 5'-noncoding region, 199 nucleotides in the 3'-noncoding region, and 345 nucleotides coding for a precursor to CCK, which is 115 amino acids (Mr, 12,826). Examination of the rat CCK gene revealed a suggested transcriptional control sequence analogous to the "TATA" sequence located 33 nucleotides upstream from a proposed transcriptional start site. The amino acid sequence of CCK-39 is flanked by both amino-terminal and carboxyl-terminal extensions. Analysis of CCK mRNA showed that it is approximately equal to 750 nucleotides long. CCK mRNA of the rat brain and intestine appeared to be identical in size to the CCK mRNA of the carcinoma.

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“…Other molecular forms of CCK have been identified in intestinal extracts, brain, and plasma of various species (4-1 1). CCK-39 was characterized from hog intestine as a hexapeptide extension on the amino terminus of CCK-33 (4,5). A larger molecular form, CCK-58, has been extracted from dog intestine and partially characterized (6).…”

Section: Introductionmentioning

confidence: 99%