Linked Life Data

11587188

Source:http://linkedlifedata.com/resource/pubmed/id/11587188

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
9
pubmed:dateCreated
2001-10-5
pubmed:abstractText
The recently identified protein, insulin 3 (INSL3), has structural features that make it a bona fide member of the insulin superfamily. Its predicted amino acid sequence contains the classic two-peptide chain (A- and B-) structure with conserved cysteine residues that results in a disulphide bond disposition identical to that of insulin. Recently, the generation of insl3 knockout mice has demonstrated that testicular descent is blocked due to the failure of a specific ligament, the gubernaculum, to develop. The mechanism by which INSL3 exerts its action on the gubernaculum is currently unknown. The purpose of this study was to, for the first time, synthesize rat INSL3 and test its action on organ cultures of foetal rat gubernaculum. INSL3 also contains a cassette of residues Arg-X-X-X-Arg within the B-chain, a motif that is essential for characteristic activity of another related member of the superfamily, relaxin. Hence, the relaxin activity of rat INSL3 was also tested in two different relaxin bioassays. The primary structure of rat INSL3 was determined by deduction from its cDNA sequence and successfully prepared by solid phase peptide synthesis of the two constituent chains followed by their combination in solution. Following confirmation of its chemical integrity by a variety of analytical techniques, circular dichroism spectroscopy confirmed the presence of high beta-turn and alpha-helical content, with a remarkable spectral similarity to the synthetic ovine INSL3 peptide and to synthetic rat relaxin. The synthetic rat INSL3 bound with very low affinity to rat relaxin receptors and had no activity in a relaxin bioassay. Furthermore, it did not augment or antagonize relaxin activity. The rat INSL3 did however induce growth of foetal rat gubernaculum in whole organ cultures demonstrating that INSL3 has a direct action on this structure.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Sep
pubmed:issn
1075-2617
pubmed:author
pubmed:issnType
Print
pubmed:volume
7
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
495-501
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11587188-Amino Acid Sequence, pubmed-meshheading:11587188-Animals, pubmed-meshheading:11587188-Biological Assay, pubmed-meshheading:11587188-Circular Dichroism, pubmed-meshheading:11587188-Conserved Sequence, pubmed-meshheading:11587188-Cyclic AMP, pubmed-meshheading:11587188-Cysteine, pubmed-meshheading:11587188-DNA, Complementary, pubmed-meshheading:11587188-Dose-Response Relationship, Drug, pubmed-meshheading:11587188-Insulin, pubmed-meshheading:11587188-Ligands, pubmed-meshheading:11587188-Male, pubmed-meshheading:11587188-Molecular Sequence Data, pubmed-meshheading:11587188-Peptides, pubmed-meshheading:11587188-Protein Binding, pubmed-meshheading:11587188-Protein Structure, Tertiary, pubmed-meshheading:11587188-Proteins, pubmed-meshheading:11587188-Rats, pubmed-meshheading:11587188-Spectrometry, Mass, Matrix-Assisted Laser..., pubmed-meshheading:11587188-Testis, pubmed-meshheading:11587188-Time Factors
pubmed:year
2001
pubmed:articleTitle
Chemical synthesis and biological activity of rat INSL3.
pubmed:affiliation
The Howard Florey Institute, University of Melbourne, Victoria, Australia.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't