Targeting of PED/PEA-15 molecular interaction with phospholipase D1 enhances insulin sensitivity in skeletal muscle cells (454 views)
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Sep 1; 283(31): 21769-21778.
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Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.52, 5-year impact factor: 5.575
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-52049085539&partnerID=40&md5=4f06778aafb5b4992d87f55c051a0032
Keywords: Glucose, Pea15 Protein, Mouse, Peptide, Phospholipase D, Phosphoprotein, Protein Kinase C Alpha, Phosphoprotein Enriched In Diabetes Phosphoprotein Enriched In Astrocytes 15, Unclassified Drug, Animal, Article, Biological Model, Chemistry, Cytology, Gene Deletion, Gene Vector, Genetics, Metabolism, Skeletal Muscle, Transgenic Mouse, Transport At The Cellular Level, Animal Cell, Binding Affinity, Carboxy Terminal Sequence, Controlled Study, Enzyme Activity, Enzyme Binding, Enzyme Linked Immunosorbent Assay, Gene Disruption, Gene Overexpression, Gene Targeting, Glucose Transport, In Vitro Study, Insulin Sensitivity, Molecular Interaction, Molecular Recognition, Muscle Cell, Non Insulin Dependent Diabetes Mellitus, Nonhuman, Priority Journal, Protein Binding, Protein Domain, Protein Protein Interaction, Protein Transport, Surface Plasmon Resonance, Transgenic Animal, Biological Transport, Genetic Vectors, Protein Kinase C-Alpha, Do-Mains, Glucose Uptakes, High Affinities, Insulin Regulations, Insulin Sensitivities, Intact Cells, Myocytes, Skeletal Muscle Cells, Type 2 Diabetes, Active Networks, Amines, Animal Cell Culture, Hormones, Molecular Structure, Plants (botany), Flow Interactions, Mus Musculus,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini and Istituto di Endocrinologia e Oncologia Sperimentale Gaetano Salvatore, Consiglio Nazionale delle Ricerche, Naples, Italy.
Dipartimento di Scienze Biologiche, Università di Napoli Federico II, Naples 80131, Italy
Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università di Napoli Federico II, Naples 80131, Italy
Tecnogen SpA, Località la Fagianeria, 81015 Piana di Monte Verna, Caserta, Italy
References:
Not available.
Jbc Papers (ISSN: 0021-9258, 1083-351x, 0021-9258linking), 2008 Sep 1; 283(31): 21769-21778.
Export to BibTeX Export to EndNote
Paper type: Journal Article, Research Support, Non-U. S. Gov'T,
Impact factor: 5.52, 5-year impact factor: 5.575
Url: http://www.scopus.com/inward/record.url?eid=2-s2.0-52049085539&partnerID=40&md5=4f06778aafb5b4992d87f55c051a0032
Keywords: Glucose, Pea15 Protein, Mouse, Peptide, Phospholipase D, Phosphoprotein, Protein Kinase C Alpha, Phosphoprotein Enriched In Diabetes Phosphoprotein Enriched In Astrocytes 15, Unclassified Drug, Animal, Article, Biological Model, Chemistry, Cytology, Gene Deletion, Gene Vector, Genetics, Metabolism, Skeletal Muscle, Transgenic Mouse, Transport At The Cellular Level, Animal Cell, Binding Affinity, Carboxy Terminal Sequence, Controlled Study, Enzyme Activity, Enzyme Binding, Enzyme Linked Immunosorbent Assay, Gene Disruption, Gene Overexpression, Gene Targeting, Glucose Transport, In Vitro Study, Insulin Sensitivity, Molecular Interaction, Molecular Recognition, Muscle Cell, Non Insulin Dependent Diabetes Mellitus, Nonhuman, Priority Journal, Protein Binding, Protein Domain, Protein Protein Interaction, Protein Transport, Surface Plasmon Resonance, Transgenic Animal, Biological Transport, Genetic Vectors, Protein Kinase C-Alpha, Do-Mains, Glucose Uptakes, High Affinities, Insulin Regulations, Insulin Sensitivities, Intact Cells, Myocytes, Skeletal Muscle Cells, Type 2 Diabetes, Active Networks, Amines, Animal Cell Culture, Hormones, Molecular Structure, Plants (botany), Flow Interactions, Mus Musculus,
Affiliations:
*** IBB - CNR ***
Istituto di Biostrutture e Bioimmagini and Istituto di Endocrinologia e Oncologia Sperimentale Gaetano Salvatore, Consiglio Nazionale delle Ricerche, Naples, Italy.
Dipartimento di Scienze Biologiche, Università di Napoli Federico II, Naples 80131, Italy
Dipartimento di Biologia e Patologia Cellulare e Molecolare, Università di Napoli Federico II, Naples 80131, Italy
Tecnogen SpA, Località la Fagianeria, 81015 Piana di Monte Verna, Caserta, Italy
References:
Not available.
Targeting of PED/PEA-15 molecular interaction with phospholipase D1 enhances insulin sensitivity in skeletal muscle cells
Phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes (PED/PEA-15) is overexpressed in several tissues of individuals affected by type 2 diabetes. In intact cells and in transgenic animal models, PED/PEA-15 overexpression impairs insulin regulation of glucose transport, and this is mediated by its interaction with the C-terminal D4 domain of phospholipase D1 (PLD1) and the consequent increase of protein kinase C-alpha activity. Here we show that interfering with the interaction of PED/PEA-15 with PLD1 in L6 skeletal muscle cells overexpressing PED/PEA-15 (L6(PED/PEA-15)) restores insulin sensitivity. Surface plasmon resonance and ELISA-like assays show that PED/PEA-15 binds in vitro the D4 domain with high affinity (K(D) = 0.37 +/- 0.13 mum), and a PED/PEA-15 peptide, spanning residues 1-24, PED-(1-24), is able to compete with the PED/PEA-15-D4 recognition. When loaded into L6(PED/PEA-15) cells and in myocytes derived from PED/PEA-15-overexpressing transgenic mice, PED-(1-24) abrogates the PED/PEA-15-PLD1 interaction and reduces protein kinase C-alpha activity to levels similar to controls. Importantly, the peptide restores insulin-stimulated glucose uptake by approximately 70%. Similar results are obtained by expression of D4 in L6(PED/PEA-15). All these findings suggest that disruption of the PED/PEA-15-PLD1 molecular interaction enhances insulin sensitivity in skeletal muscle cells and indicate that PED/PEA-15 as an important target for type 2 diabetes.
Phosphoprotein enriched in diabetes/phosphoprotein enriched in astrocytes (PED/PEA-15) is overexpressed in several tissues of individuals affected by type 2 diabetes. In intact cells and in transgenic animal models, PED/PEA-15 overexpression impairs insulin regulation of glucose transport, and this is mediated by its interaction with the C-terminal D4 domain of phospholipase D1 (PLD1) and the consequent increase of protein kinase C-alpha activity. Here we show that interfering with the interaction of PED/PEA-15 with PLD1 in L6 skeletal muscle cells overexpressing PED/PEA-15 (L6(PED/PEA-15)) restores insulin sensitivity. Surface plasmon resonance and ELISA-like assays show that PED/PEA-15 binds in vitro the D4 domain with high affinity (K(D) = 0.37 +/- 0.13 mum), and a PED/PEA-15 peptide, spanning residues 1-24, PED-(1-24), is able to compete with the PED/PEA-15-D4 recognition. When loaded into L6(PED/PEA-15) cells and in myocytes derived from PED/PEA-15-overexpressing transgenic mice, PED-(1-24) abrogates the PED/PEA-15-PLD1 interaction and reduces protein kinase C-alpha activity to levels similar to controls. Importantly, the peptide restores insulin-stimulated glucose uptake by approximately 70%. Similar results are obtained by expression of D4 in L6(PED/PEA-15). All these findings suggest that disruption of the PED/PEA-15-PLD1 molecular interaction enhances insulin sensitivity in skeletal muscle cells and indicate that PED/PEA-15 as an important target for type 2 diabetes.
Targeting of PED/PEA-15 molecular interaction with phospholipase D1 enhances insulin sensitivity in skeletal muscle cells
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Targeting of PED/PEA-15 molecular interaction with phospholipase D1 enhances insulin sensitivity in skeletal muscle cells
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13 Records (11 excluding Abstracts).
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Total 5 year impact factor: 55.271 (42.38 excluding Abstracts).
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