Switch to
| Predicate | Object |
|---|---|
| rdf:type | |
| lifeskim:mentions | |
| pubmed:issue |
16
|
| pubmed:dateCreated |
1998-5-21
|
| pubmed:abstractText |
Helodermin and exendin-4, two peptides isolated from the salivary gland of the Gila monster, Heloderma suspectum, are approximately 50% homologous to vasoactive intestinal peptide (VIP) and glucagon-like peptide-1 (GLP-1), respectively, and interact with the mammalian receptors for VIP and GLP-1 with equal or higher affinity and efficacy. Immunohistochemical studies suggested the presence of helodermin-like peptides in mammals. To determine whether helodermin and exendin-4 are present in mammals and their evolutionary relationship to VIP and GLP-1, their cDNAs were first cloned from Gila monster salivary gland. Northern blots and reverse transcription-polymerase chain reaction of multiple Gila monster tissues identified approximately 500-base pair transcripts only from salivary gland. Both helodermin and exendin-4 full-length cDNAs were approximately 500 base pairs long, and they encoded precursor proteins containing the entire amino acid sequence of helodermin and exendin-4, as well as a 44- or 45-amino acid N-terminal extension peptide, respectively, having approximately 60% homology. The size and structural organization of these cDNAs indicated that they were closely related to one another but markedly different from known cDNAs for the VIP/GLP-1 peptide family previously identified in both lower and higher evolved species. Cloning of the Gila monster VIP/peptide histidine isoleucine, pituitary adenylate cyclase activating polypeptide, and glucagon/GLP-1 cDNAs and Southern blotting of Gila monster DNA demonstrate the coexistence of separate genes for these peptides and suggests, along with the restricted salivary gland expression, that helodermin and exendin-4 coevolved to serve a separate specialized function. Probing of a variety of rat and human tissues on Northern blots, human and rat Southern blots, and genomic and cDNA libraries with either helodermin- or exendin-4-specific cDNAs failed to identify evidence for mammalian homologues. These data indicate that helodermin and exendin-4 are not the precursors to VIP and GLP-1 and that they belong to a separate peptide family encoded by separate genes. Furthermore, the existence of as yet undiscovered mammalian homologues to helodermin and exendin-4 seems unlikely.
|
| pubmed:language |
eng
|
| pubmed:journal | |
| pubmed:citationSubset |
IM
|
| pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/ADCYAP1 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Adcyap1 protein, rat,
http://linkedlifedata.com/resource/pubmed/chemical/DNA, Complementary,
http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers,
http://linkedlifedata.com/resource/pubmed/chemical/Glucagon,
http://linkedlifedata.com/resource/pubmed/chemical/Glucagon-Like Peptide 1,
http://linkedlifedata.com/resource/pubmed/chemical/Glucagon-Like Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Neuropeptides,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peptides,
http://linkedlifedata.com/resource/pubmed/chemical/Pituitary Adenylate...,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Precursors,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Vasoactive Intestinal Peptide,
http://linkedlifedata.com/resource/pubmed/chemical/Venoms,
http://linkedlifedata.com/resource/pubmed/chemical/exenatide,
http://linkedlifedata.com/resource/pubmed/chemical/glucagon-like peptide 1 (7-36),
http://linkedlifedata.com/resource/pubmed/chemical/heliodermin
|
| pubmed:status |
MEDLINE
|
| pubmed:month |
Apr
|
| pubmed:issn |
0021-9258
|
| pubmed:author | |
| pubmed:issnType |
Print
|
| pubmed:day |
17
|
| pubmed:volume |
273
|
| pubmed:owner |
NLM
|
| pubmed:authorsComplete |
Y
|
| pubmed:pagination |
9778-84
|
| pubmed:dateRevised |
2006-11-15
|
| pubmed:meshHeading |
pubmed-meshheading:9545315-Amino Acid Sequence,
pubmed-meshheading:9545315-Animals,
pubmed-meshheading:9545315-Base Sequence,
pubmed-meshheading:9545315-Chickens,
pubmed-meshheading:9545315-Cloning, Molecular,
pubmed-meshheading:9545315-DNA, Complementary,
pubmed-meshheading:9545315-DNA Primers,
pubmed-meshheading:9545315-Glucagon,
pubmed-meshheading:9545315-Glucagon-Like Peptide 1,
pubmed-meshheading:9545315-Glucagon-Like Peptides,
pubmed-meshheading:9545315-Humans,
pubmed-meshheading:9545315-Lizards,
pubmed-meshheading:9545315-Mammals,
pubmed-meshheading:9545315-Molecular Sequence Data,
pubmed-meshheading:9545315-Neuropeptides,
pubmed-meshheading:9545315-Peptide Fragments,
pubmed-meshheading:9545315-Peptides,
pubmed-meshheading:9545315-Pituitary Adenylate Cyclase-Activating Polypeptide,
pubmed-meshheading:9545315-Polymerase Chain Reaction,
pubmed-meshheading:9545315-Protein Precursors,
pubmed-meshheading:9545315-Rats,
pubmed-meshheading:9545315-Recombinant Proteins,
pubmed-meshheading:9545315-Sequence Alignment,
pubmed-meshheading:9545315-Sequence Homology, Amino Acid,
pubmed-meshheading:9545315-Trout,
pubmed-meshheading:9545315-Vasoactive Intestinal Peptide,
pubmed-meshheading:9545315-Venoms
|
| pubmed:year |
1998
|
| pubmed:articleTitle |
Molecular cloning of the helodermin and exendin-4 cDNAs in the lizard. Relationship to vasoactive intestinal polypeptide/pituitary adenylate cyclase activating polypeptide and glucagon-like peptide 1 and evidence against the existence of mammalian homologues.
|
| pubmed:affiliation |
Digestive Diseases Branch, NIDDK, National Institutes of Health, Bethesda, Maryland 20892, USA.
|
| pubmed:publicationType |
Journal Article
|