Linked Life Data

15252030

Source:http://linkedlifedata.com/resource/pubmed/id/15252030

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
40
pubmed:dateCreated
2004-9-27
pubmed:databankReference
pubmed:abstractText
Dual specificity phosphatases (DSPs) are members of the protein-tyrosine phosphatase superfamily that dephosphorylate both phosphotyrosine and phosphoserine/threonine residues in vitro. Many DSPs have been found to play important roles in various aspects of cellular function and to be involved in human disease. We have identified a gene located on human chromosome 10q22.2, which utilizes alternative open reading frames (ORFs) to encode the following two distinct DSPs: the previously described testis and skeletal muscle-specific dual specificity phosphatase (TMDP) and a novel DSP, muscle-restricted dual specificity phosphatase (MDSP). Use of alternative ORFs encoding distinct proteins from a single gene is extremely rare in eukaryotes, and in all previously reported cases the two proteins produced from one gene are unrelated. To our knowledge this is the first example of a gene from which two distinct proteins of the same family are expressed using alternative ORFs. Here we provide evidence that both MDSP and TMDP proteins are expressed in vivo and are restricted to specific tissues, skeletal muscle and testis, respectively. Most interestingly, the protein expression profiles of both MDSP and TMDP during mouse postnatal development are strikingly similar. MDSP is expressed at very low levels in myotubes and early postnatal muscle. TMDP is not detectable in testis lysate in the first 3 weeks of life. The expression of both MDSP and TMDP proteins was markedly increased at approximately the 3rd week after birth and continued to increase gradually into adulthood, implying that the physiological functions of both DSPs are specific to the mature/late-developing organs. The conserved gene structure and the similarity in postnatal expression profile of these two proteins suggest biological significance of the unusual gene arrangement.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Oct
pubmed:issn
0021-9258
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
279
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
41404-13
pubmed:dateRevised
2010-12-3
pubmed:meshHeading
pubmed-meshheading:15252030-Animals, pubmed-meshheading:15252030-Base Sequence, pubmed-meshheading:15252030-Chromosomes, Human, Pair 10, pubmed-meshheading:15252030-Dual-Specificity Phosphatases, pubmed-meshheading:15252030-Gene Expression Profiling, pubmed-meshheading:15252030-Gene Expression Regulation, Developmental, pubmed-meshheading:15252030-Genes, pubmed-meshheading:15252030-Humans, pubmed-meshheading:15252030-Male, pubmed-meshheading:15252030-Mice, pubmed-meshheading:15252030-Molecular Sequence Data, pubmed-meshheading:15252030-Muscle, Skeletal, pubmed-meshheading:15252030-Open Reading Frames, pubmed-meshheading:15252030-Organ Specificity, pubmed-meshheading:15252030-Phosphoprotein Phosphatases, pubmed-meshheading:15252030-Protein Tyrosine Phosphatases, pubmed-meshheading:15252030-Testis, pubmed-meshheading:15252030-Tissue Distribution
pubmed:year
2004
pubmed:articleTitle
Characterization of two distinct dual specificity phosphatases encoded in alternative open reading frames of a single gene located on human chromosome 10q22.2.
pubmed:affiliation
Cold Spring Harbor Laboratory, Cold Spring Harbor, New York 11724, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S.