Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription. (Articolo in rivista)

Type

• Prodotto della ricerca (Classe)
• Articolo in rivista (Classe)

Label

• Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription. (Articolo in rivista) (literal)

Anno

• 2003-01-01T00:00:00+01:00 (literal)

Alternative label

• Capanni C.1, Cenni V.1, Mattioli E.1, Sabatelli P.1, Ognibene A.1, Columbaro M.3, Parnaik VK.4, Wehnert M.5, Maraldi NM.1-2, Squarzoni S.2, Lattanzi G.2 (2003)
  Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription.
  in Experimental brain research
  (literal)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori

• Capanni C.1, Cenni V.1, Mattioli E.1, Sabatelli P.1, Ognibene A.1, Columbaro M.3, Parnaik VK.4, Wehnert M.5, Maraldi NM.1-2, Squarzoni S.2, Lattanzi G.2 (literal)

Pagina inizio

• 122 (literal)

Pagina fine

• 134 (literal)

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• Collaborazione internazionale. Lavoro multidisciplinare a carattere clinico. Lavoro finanziato dal progetto europeo MYOCLUSTER I.F. 4,712 (literal)

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• 291 (literal)

Rivista

• Experimental brain research (Rivista)

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• I.F. 4,712 (literal)

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• Familial partial lipodystrophy is an autosomal dominant disease caused by mutations of the LMNA gene encoding alternatively spliced lamins A and C. Abnormal distribution of body fat and insulin resistance characterize the clinical phenotype. In this study, we analyzed primary fibroblast cultures from a patient carrying an R482L lamin A/C mutation by a morphological and biochemical approach. Abnormalities were observed consisting of nuclear lamin A/C aggregates mostly localized close to the nuclear lamina. These aggregates were not bound to either DNA-containing structures or RNA splicing intranuclear compartments. In addition, emerin did not colocalize with nuclear lamin A/C aggregates. Interestingly, emerin failed to interact with lamin A in R482L mutated fibroblasts in vivo, while the interaction with lamin C was preserved in vitro, as determined by coimmunoprecipitation experiments. The presence of lamin A/C nuclear aggregates was restricted to actively transcribing cells, and it was increased in insulin-treated fibroblasts. In fibroblasts carrying lamin A/C nuclear aggregates, a reduced incorporation of bromouridine was observed, demonstrating that mutated lamin A/C in FPLD cells interferes with RNA transcription (literal)

Note

• ISI Web of Science (WOS) (literal)

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• 1Laboratory of Cell Biology, Istituti Ortopedici Rizzoli, Bologna 2ITOI, CNR, Unit of Bologna – CNR 3Neuromuscular Unit, Istituti Ortopedici Rizzoli, Bologna 4Centre for Cellular and Molecular Biology, Hyderabad 500 007, India 5Institute of Human Genetics, University of Greifswald, Germany (literal)

Titolo

• Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription. (literal)

Abstract

• Familial partial lipodystrophy is an autosomal dominant disease caused by mutations of the LMNA gene encoding alternatively spliced lamins A and C. Abnormal distribution of body fat and insulin resistance characterize the clinical phenotype. In this study, we analyzed primary fibroblast cultures from a patient carrying an R482L lamin A/C mutation by a morphological and biochemical approach. Abnormalities were observed consisting of nuclear lamin A/C aggregates mostly localized close to the nuclear lamina. These aggregates were not bound to either DNA-containing structures or RNA splicing intranuclear compartments. In addition, emerin did not colocalize with nuclear lamin A/C aggregates. Interestingly, emerin failed to interact with lamin A in R482L mutated fibroblasts in vivo, while the interaction with lamin C was preserved in vitro, as determined by coimmunoprecipitation experiments. The presence of lamin A/C nuclear aggregates was restricted to actively transcribing cells, and it was increased in insulin-treated fibroblasts. In fibroblasts carrying lamin A/C nuclear aggregates, a reduced incorporation of bromouridine was observed, demonstrating that mutated lamin A/C in FPLD cells interferes with RNA transcription. (literal)

Autore CNR

• PATRIZIA SABATELLI (Unità di personale interno)
• STEFANO SQUARZONI (Persona)
• CRISTINA CAPANNI (Persona)
• VITTORIA CENNI (Unità di personale interno)
• NADIR MARIO MARALDI (Unità di personale esterno)
• GIOVANNA LATTANZI (Persona)

Insieme di parole chiave

• Keywords of "Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription." (Insieme di parole chiave)

Incoming links:

Autore CNR di

• PATRIZIA SABATELLI (Unità di personale interno)
• GIOVANNA LATTANZI (Persona)
• STEFANO SQUARZONI (Persona)
• NADIR MARIO MARALDI (Unità di personale esterno)
• CRISTINA CAPANNI (Persona)
• VITTORIA CENNI (Unità di personale interno)

Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#rivistaDi

• Experimental brain research (Rivista)

Insieme di parole chiave di

• Keywords of "Failure of lamin A/C to functionally assemble in R482L mutated familial partial lipodystrophy fibroblasts: altered intermolecular interaction with emerin and implications for gene transcription." (Insieme di parole chiave)