Identification of skeletal muscle protein-tyrosine phosphatases by amplification of conserved cDNA sequences.
Identifieur interne : 004876 ( Main/Curation ); précédent : 004875; suivant : 004877Identification of skeletal muscle protein-tyrosine phosphatases by amplification of conserved cDNA sequences.
Auteurs : W R Zhang [États-Unis] ; B J GoldsteinSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1991.
Descripteurs français
- KwdFr :
- ADN (génétique), ADN (isolement et purification), ARN messager (génétique), ARN messager (isolement et purification), Animaux, Banque de gènes, Clonage moléculaire, Données de séquences moléculaires, Lignées consanguines de rats, Muscles (enzymologie), Mâle, Phosphoprotein Phosphatases (génétique), Protein Tyrosine Phosphatases, Rats, Similitude de séquences d'acides nucléiques, Sondes oligonucléotidiques, Souris, Spécificité d'organe, Séquence d'acides aminés, Séquence nucléotidique, Techniques d'amplification d'acides nucléiques, Évolution biologique.
- MESH :
- enzymologie : Muscles.
- génétique : ADN, ARN messager, Phosphoprotein Phosphatases.
- isolement et purification : ADN, ARN messager.
- Animaux, Banque de gènes, Clonage moléculaire, Données de séquences moléculaires, Lignées consanguines de rats, Mâle, Protein Tyrosine Phosphatases, Rats, Similitude de séquences d'acides nucléiques, Sondes oligonucléotidiques, Souris, Spécificité d'organe, Séquence d'acides aminés, Séquence nucléotidique, Techniques d'amplification d'acides nucléiques, Évolution biologique.
English descriptors
- KwdEn :
- Amino Acid Sequence, Animals, Base Sequence, Biological Evolution, Cloning, Molecular, DNA (genetics), DNA (isolation & purification), Gene Library, Male, Mice, Molecular Sequence Data, Muscles (enzymology), Nucleic Acid Amplification Techniques, Oligonucleotide Probes, Organ Specificity, Phosphoprotein Phosphatases (genetics), Protein Tyrosine Phosphatases, RNA, Messenger (genetics), RNA, Messenger (isolation & purification), Rats, Rats, Inbred Strains, Sequence Homology, Nucleic Acid.
- MESH :
- chemical , genetics : DNA, Phosphoprotein Phosphatases, RNA, Messenger.
- chemical , isolation & purification : DNA, RNA, Messenger.
- enzymology : Muscles.
- Amino Acid Sequence, Animals, Base Sequence, Biological Evolution, Cloning, Molecular, Gene Library, Male, Mice, Molecular Sequence Data, Nucleic Acid Amplification Techniques, Oligonucleotide Probes, Organ Specificity, Protein Tyrosine Phosphatases, Rats, Rats, Inbred Strains, Sequence Homology, Nucleic Acid.
Abstract
Specific protein-tyrosine phosphatase (PTPase) enzymes that regulate signal transduction by the insulin receptor in target tissues have not been identified. We evaluated the expression of PTPase homologs in skeletal muscle since this tissue is the major site of insulin-mediated glucose disposal in vivo. A rat skeletal muscle cDNA pool was prepared with a set of degenerate oligonucleotide primers and PTPase cDNA sequences were amplified using pairs of "guess-mers" that were deduced from highly conserved residues within the known catalytic domains of these enzymes. Sequences encoding three "receptor-like" transmembrane PTPases were identified and two of these (known as LAR and LRP) were confirmed to be expressed in muscle by subsequent cDNA library screening and Northern blot analysis. The expression of the LAR and LRP PTPases in skeletal muscle suggests that these enzymes might have a role in the regulation of insulin action in muscle and other insulin-sensitive tissues.
DOI: 10.1016/0006-291x(91)91034-a
PubMed: 1651716
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pubmed:1651716Le document en format XML
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amplification of conserved cDNA sequences.</title><author><name sortKey="Zhang, W R" sort="Zhang, W R" uniqKey="Zhang W" first="W R" last="Zhang">W R Zhang</name><affiliation wicri:level="2"><nlm:affiliation>Research Division, Joslin Diabetes Center, Brigham and Women's Hospital, Boston, MA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><placeName><region type="state">Massachusetts</region></placeName><wicri:cityArea>Research Division, Joslin Diabetes Center, Brigham and Women's Hospital, Boston</wicri:cityArea></affiliation></author><author><name sortKey="Goldstein, B J" sort="Goldstein, B J" uniqKey="Goldstein B" first="B J" last="Goldstein">B J Goldstein</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" 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gènes</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Lignées consanguines de rats</term><term>Muscles (enzymologie)</term><term>Mâle</term><term>Phosphoprotein Phosphatases (génétique)</term><term>Protein Tyrosine Phosphatases</term><term>Rats</term><term>Similitude de séquences d'acides nucléiques</term><term>Sondes oligonucléotidiques</term><term>Souris</term><term>Spécificité d'organe</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Techniques d'amplification d'acides nucléiques</term><term>Évolution biologique</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>DNA</term><term>Phosphoprotein Phosphatases</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>DNA</term><term>RNA, Messenger</term></keywords><keywords scheme="MESH" qualifier="enzymologie" 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xml:lang="fr"><term>Animaux</term><term>Banque de gènes</term><term>Clonage moléculaire</term><term>Données de séquences moléculaires</term><term>Lignées consanguines de rats</term><term>Mâle</term><term>Protein Tyrosine Phosphatases</term><term>Rats</term><term>Similitude de séquences d'acides nucléiques</term><term>Sondes oligonucléotidiques</term><term>Souris</term><term>Spécificité d'organe</term><term>Séquence d'acides aminés</term><term>Séquence nucléotidique</term><term>Techniques d'amplification d'acides nucléiques</term><term>Évolution biologique</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Specific protein-tyrosine phosphatase (PTPase) enzymes that regulate signal transduction by the insulin receptor in target tissues have not been identified. We evaluated the expression of PTPase homologs in skeletal muscle since this tissue is the major site of insulin-mediated glucose disposal in vivo. A rat skeletal muscle cDNA pool was prepared with a set of degenerate oligonucleotide primers and PTPase cDNA sequences were amplified using pairs of "guess-mers" that were deduced from highly conserved residues within the known catalytic domains of these enzymes. Sequences encoding three "receptor-like" transmembrane PTPases were identified and two of these (known as LAR and LRP) were confirmed to be expressed in muscle by subsequent cDNA library screening and Northern blot analysis. The expression of the LAR and LRP PTPases in skeletal muscle suggests that these enzymes might have a role in the regulation of insulin action in muscle and other insulin-sensitive tissues.</div></front></TEI></record>Pour manipuler ce document sous Unix (Dilib)
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