12447687

Source:http://linkedlifedata.com/resource/pubmed/id/12447687

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Predicate	Object
rdf:type	pubmed:Citation
lifeskim:mentions	umls-concept:C0007634, umls-concept:C0021665, umls-concept:C0021666, umls-concept:C0023269, umls-concept:C0034818, umls-concept:C0162638, umls-concept:C0205263, umls-concept:C0596138, umls-concept:C0597298, umls-concept:C1545588, umls-concept:C2699153
pubmed:dateCreated	2002-11-26
pubmed:abstractText	One of the two isoforms of the human insulin receptor (isoform A or IR-A) binds IGF-II with high affinity and is predominantly expressed in fetal tissues and malignant cells. We evaluated the biological relevance of IR-A in human myosarcoma cells. Six myosarcoma cell lines were studied. All produced high amounts of IGF-II and five of them predominantly expressed IR-A. SKUT-1 leiomyosarcoma cells, that do not express the IGF-IR, were identified as a suitable model to study the effects of IR-A in the absence of the interference of IGF-IR. In these cells, which express high levels of IR with an IR-A relative abundance of approximately 95%, IGF-II elicits biological effects exclusively via IR-A activation and IGF-I is almost ineffective. Blockade of autocrine IGF-II reduced unstimulated cell viability and migration. Although both insulin and IGF-II activate IR-A, these two ligands showed a different ability to activate different intracellular signaling pathways and to elicit different biological effects. Insulin was more potent than IGF-II in activating the PI3-K/Akt pathway and in protecting cells from apoptosis. In contrast, IGF-II was more potent than insulin in activating the Shc/ERK pathway and in stimulating cell migration. These data indicate that IGF-II sensitive IR-A is the predominant IR isoform in a variety of myosarcoma cells. In SKUT-1 leiomyoma cells this fetal IR isoform may vicariate the IGF-IR for cell response to both insulin and IGF-II. Acting on the same IR-A receptor IGF-II is more potent than insulin in stimulating cancer cell migration.
pubmed:language	eng
pubmed:citationSubset	IM
pubmed:chemical	http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD, http://linkedlifedata.com/resource/pubmed/chemical/DNA Primers, http://linkedlifedata.com/resource/pubmed/chemical/INSR protein, human, http://linkedlifedata.com/resource/pubmed/chemical/Insulin-Like Growth Factor II, http://linkedlifedata.com/resource/pubmed/chemical/Protein-Serine-Threonine Kinases, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins, http://linkedlifedata.com/resource/pubmed/chemical/Proto-Oncogene Proteins c-akt, http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, IGF Type 1, http://linkedlifedata.com/resource/pubmed/chemical/Receptor, Insulin, http://linkedlifedata.com/resource/pubmed/chemical/TRS1 protein, Human herpesvirus 5, http://linkedlifedata.com/resource/pubmed/chemical/Viral Proteins
pubmed:status	MEDLINE
pubmed:author	pubmed-author:BelfioreAntoninoA, pubmed-author:MineoRossanaR, pubmed-author:MurabitoAntonellaA, pubmed-author:PandiniGiuseppeG, pubmed-author:SciaccaLauraL, pubmed-author:VigneriRiccardoR
pubmed:owner	NLM
pubmed:authorsComplete	Y
pubmed:pagination	8240-50
pubmed:dateRevised	2009-11-19
pubmed:articleTitle	In IGF-I receptor-deficient leiomyosarcoma cells autocrine IGF-II induces cell invasion and protection from apoptosis via the insulin receptor isoform A.
pubmed:affiliation	Dipartimento di Medicina Interna e Medicina Specialistica, University of Catania, Ospedale Garibaldi, 95123 Catania, Italy.