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- Article] Sequence and characterization of cDNA encoding the motilin precursor from chicken, dog, cow and horse. Evidence of mosaic evolution in prepromotilin
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DocNo of ILP: 6901
Doc. Type: Article
Title: Sequence and characterization of cDNA encoding the motilin precursor from chicken, dog, cow and horse. Evidence of mosaic evolution in prepromotilin
Authors: Huang, Z; Depoortere, I; De Clercq, P; Peeters, T
Full Name of Authors: Huang, Z; Depoortere, I; De Clercq, P; Peeters, T
Keywords by Author: homology; motilin associated peptide; PEST; prepromotilin
Keywords Plus: PREPROPANCREATIC POLYPEPTIDE; AMINO-ACID; INTESTINAL MOTILIN; PORCINE MOTILIN; GENE; PURIFICATION; LOCALIZATION; exPRESSION; BRAIN; RAT
Abstract: Motilin is involved in the regulation of the fasting motility pattern in man and in dog, but may have a different role in other species. Immunoreactive motilin has been demonstrated in several species, but the sequence is mostly unknown. The aim of this study was to isolate and sequence the cDNA encoding the motilin precursor from several mammalian species and from chicken. Total RNA was isolated from the duodenal mucosa of the chicken, dog, cow and horse. In each case single stranded cDNA was synthesized. Motilin cDNA fragments were amplified by PCR, ligated into a plasmid and cloned. Clones which were positive after screening with an appropriate P-32-labeled probe were sequenced. The 5'- and 3'-ends were determined by the rapid amplification of cDNA ends (RACE) method. Analysis of the cDNAs revealed an open reading frame coding for 115 (chicken and cow), or 117 (dog and horse) amino acids. It consists of a 25 amino acid signal peptide, motilin itself, and a 68 (chicken and cow) or 70 (dog and horse) amino acid motilin associated peptide (MAP). As in all motilin precursors already sequenced (man, monkey, pig and rabbit), an endoproteinase cleavage site is present at Lys(23)-Lys(24). Comparison of all known sequences shows considerable identity in amino acid and nucleotide sequence of the signal peptide and motilin. However, the MAPs differ not only in length but also, more strongly, in amino acid and nucleotide sequence. Our study demonstrates that the N- and C-terminal regions of the motilin precursor have evolved at different rates, which is evidence for 'mosaic evolution'. (C) 1999 Elsevier Science B.V. All rights reserved.
Cate of OECD: Biological sciences
Year of Publication: 1999
Business Area: other
Detail Business: medicine & science
Country: Netherlands
Study Area:
Name of Journal: GENE
Language: English
Country of Authors: Catholic Univ Louvain, Dept Pathophysiol, Gut Hormone Lab, Gasthuisberg O&N, B-3000 Louvain, Belgium
Press Adress: Peeters, T (reprint author), Catholic Univ Louvain, Dept Pathophysiol, Gut Hormone Lab, Gasthuisberg O&N, Herestr 29, B-3000 Louvain, Belgium.
Email Address:
Citaion: Depoortere, Inge/0000-0002-0289-2175
Funding:
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Number of Citaion: 31
Publication: ELSEVIER SCIENCE BV
City of Publication: AMSTERDAM
Address of Publication: PO BOX 211, 1000 AE AMSTERDAM, NETHERLANDS
ISSN: 0378-1119
29-Character Source Abbreviation: GENE
ISO Source Abbreviation: Gene
Volume: 240
Version: 1
Start of File: 217
End of File: 226
DOI: 10.1016/S0378-1119(99)00397-2
Number of Pages: 10
Web of Science Category: Genetics & Heredity
Subject Category: Genetics & Heredity
Document Delivery Number: 258RR
Unique Article Identifier: WOS:000083853400023
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