http://www.cnr.it/ontology/cnr/individuo/prodotto/ID5253
Altered pre-lamin A processing is a common mechanism leading to lipodystrophy, (Articolo in rivista)
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- Label
- Altered pre-lamin A processing is a common mechanism leading to lipodystrophy, (Articolo in rivista) (literal)
- Anno
- 2005-01-01T00:00:00+01:00 (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#doi
- 10.1093/hmg/ddi158 (literal)
- Alternative label
C. CAPANNI, E. MATTIOLI, M. COLUMBARO, E. LUCARELLI, V.K. PARNAIK, G. NOVELLI, M. WEHNERT, V. CENNI, N.M. MARALDI, S. SQUARZONI, G. LATTANZI, (2005)
Altered pre-lamin A processing is a common mechanism leading to lipodystrophy,
in Human molecular genetics (Print)
(literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#autori
- C. CAPANNI, E. MATTIOLI, M. COLUMBARO, E. LUCARELLI, V.K. PARNAIK, G. NOVELLI, M. WEHNERT, V. CENNI, N.M. MARALDI, S. SQUARZONI, G. LATTANZI, (literal)
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- ISI Web of Science (WOS) (literal)
- Http://www.cnr.it/ontology/cnr/pubblicazioni.owl#affiliazioni
- Titolo
- Altered pre-lamin A processing is a common mechanism leading to lipodystrophy, (literal)
- Abstract
- Lipodystrophies are a heterogeneous group of human disorders characterized by the anomalous distribution
of body fat associated with insulin resistance and altered lipid metabolism. The pathogenetic mechanism of
inherited lipodystrophies is not yet clear; at the molecular level they have been linked to mutations of lamin
A/C, peroxisome proliferator-activated receptor (PPARg) and other seemingly unrelated proteins. In this
study, we examined lamin A/C processing in three laminopathies characterized by lipodystrophic phenotypes:
Dunnigan type familial partial lipodystrophy, mandibuloacral dysplasia and atypical Werner's
syndrome. We found that the lamin A precursor was specifically accumulated in lipodystrophy cells. Prelamin
A was located at the nuclear envelope and co-localized with the adipocyte transcription factor sterol
regulatory element binding protein 1 (SREBP1). Using co-immunoprecipitation experiments, we obtained
the first demonstration of an in vivo interaction between SREBP1 and pre-lamin A. Binding of SREBP1 to
the lamin A precursor was detected in patient fibroblasts as well as in control fibroblasts forced to accumulate
pre-lamin A by farnesylation inhibitors. In contrast, SREBP1 did not interact in vivo with mature lamin A
or C in cultured fibroblasts. To gain insights into the effect of pre-lamin A accumulation in adipose tissue, we
inhibited lamin A precursor processing in 3T3-L1 pre-adipocytes. Our results show that pre-lamin A sequesters
SREBP1 at the nuclear rim, thus decreasing the pool of active SREBP1 that normally activates PPARg
and causing impairment of pre-adipocyte differentiation. This defect can be rescued by treatment with troglitazone,
a known PPARg ligand activating the adipogenic program. (literal)
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