Characterization of two molecular forms of vasoactive intestinal polypeptide (VIP) from the pallid sturgeon, Scaphirhynchus albus (Acipenseriformes)

J. B. Kim; B. A. Barton; J. M. Conlon

doi:10.1023/A:1022243304391

Characterization of two molecular forms of vasoactive intestinal polypeptide (VIP) from the pallid sturgeon, Scaphirhynchus albus (Acipenseriformes)

J. B. Kim, B. A. Barton, J. M. Conlon

School of Biomedical Sciences

Research output: Contribution to journal › Article › peer-review

3 Citations (Scopus)

Abstract

Vasoactive intestinal polypeptide (VIP) was isolated in two molecular forms from an extract of the gastroenteropancreatic system of the pallid sturgeon Scaphirhynchus albus (Acipenseriformes). VIP-1 was identical to the peptide previously isolated from the rainbow trout Oncorhynchus mykiss and the bowfin, Amia calva, consistent with the proposed sister group relationship of the Acipenseriformes and the Neopterygii. Sturgeon VIP-2 contained the amino acid substitution (Ala⁴ → Ser) at a site previously regarded as invariant. The isolation of two distinct VIP gene products provides some support for the hypothesis that S. albus, with approximately 120 chromosomes, is functionally tetraploid but the alternative view that the species is functionally diploid and the two peptides arose from a local duplication of the VIP gene within the Scaphirhynchus lineage cannot be rejected.

Original language	English
Pages (from-to)	231-238
Number of pages	8
Journal	Fish Physiology and Biochemistry
Volume	25
Issue number	3
DOIs	https://doi.org/10.1023/A:1022243304391
Publication status	Published (in print/issue) - Dec 2001

Keywords

Acipenseridae
Phylogeny
Polyploidy
Scaphirhynchinae
Structure-activity
T etraploidization

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title = "Characterization of two molecular forms of vasoactive intestinal polypeptide (VIP) from the pallid sturgeon, Scaphirhynchus albus (Acipenseriformes)",

abstract = "Vasoactive intestinal polypeptide (VIP) was isolated in two molecular forms from an extract of the gastroenteropancreatic system of the pallid sturgeon Scaphirhynchus albus (Acipenseriformes). VIP-1 was identical to the peptide previously isolated from the rainbow trout Oncorhynchus mykiss and the bowfin, Amia calva, consistent with the proposed sister group relationship of the Acipenseriformes and the Neopterygii. Sturgeon VIP-2 contained the amino acid substitution (Ala4 → Ser) at a site previously regarded as invariant. The isolation of two distinct VIP gene products provides some support for the hypothesis that S. albus, with approximately 120 chromosomes, is functionally tetraploid but the alternative view that the species is functionally diploid and the two peptides arose from a local duplication of the VIP gene within the Scaphirhynchus lineage cannot be rejected.",

keywords = "Acipenseridae, Phylogeny, Polyploidy, Scaphirhynchinae, Structure-activity, T etraploidization",

author = "Kim, {J. B.} and Barton, {B. A.} and Conlon, {J. M.}",

year = "2001",

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AU - Kim, J. B.

AU - Barton, B. A.

AU - Conlon, J. M.

PY - 2001/12

Y1 - 2001/12

N2 - Vasoactive intestinal polypeptide (VIP) was isolated in two molecular forms from an extract of the gastroenteropancreatic system of the pallid sturgeon Scaphirhynchus albus (Acipenseriformes). VIP-1 was identical to the peptide previously isolated from the rainbow trout Oncorhynchus mykiss and the bowfin, Amia calva, consistent with the proposed sister group relationship of the Acipenseriformes and the Neopterygii. Sturgeon VIP-2 contained the amino acid substitution (Ala4 → Ser) at a site previously regarded as invariant. The isolation of two distinct VIP gene products provides some support for the hypothesis that S. albus, with approximately 120 chromosomes, is functionally tetraploid but the alternative view that the species is functionally diploid and the two peptides arose from a local duplication of the VIP gene within the Scaphirhynchus lineage cannot be rejected.

AB - Vasoactive intestinal polypeptide (VIP) was isolated in two molecular forms from an extract of the gastroenteropancreatic system of the pallid sturgeon Scaphirhynchus albus (Acipenseriformes). VIP-1 was identical to the peptide previously isolated from the rainbow trout Oncorhynchus mykiss and the bowfin, Amia calva, consistent with the proposed sister group relationship of the Acipenseriformes and the Neopterygii. Sturgeon VIP-2 contained the amino acid substitution (Ala4 → Ser) at a site previously regarded as invariant. The isolation of two distinct VIP gene products provides some support for the hypothesis that S. albus, with approximately 120 chromosomes, is functionally tetraploid but the alternative view that the species is functionally diploid and the two peptides arose from a local duplication of the VIP gene within the Scaphirhynchus lineage cannot be rejected.

KW - Acipenseridae

KW - Phylogeny

KW - Polyploidy

KW - Scaphirhynchinae

KW - Structure-activity

KW - T etraploidization

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DO - 10.1023/A:1022243304391

M3 - Article

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SN - 0920-1742

VL - 25

SP - 231

EP - 238

JO - Fish Physiology and Biochemistry

JF - Fish Physiology and Biochemistry

IS - 3

ER -

Characterization of two molecular forms of vasoactive intestinal polypeptide (VIP) from the pallid sturgeon, Scaphirhynchus albus (Acipenseriformes)

Abstract

Keywords

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