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1.
Rev Neurol (Paris) ; 172(10): 607-613, 2016 Oct.
Article in English | MEDLINE | ID: mdl-27569989

ABSTRACT

Characteristics of the intermediate filament proteins (IFPs) expressed during the development and cell differentiation of peripheral neurons are here reviewed. Neurofilament triplet proteins (NFPs), peripherin, α-internexin, synemin, syncoilin, nestin, vimentin and glial fibrillary acidic protein (GFAP) are each produced by different genes. NFPs, the most extensively studied, are thought to maintain axonal caliber, thus ensuring normal axonal transport, but this network is highly disrupted in several diseases, particularly motor neuron diseases. α-internexin has been proposed as the fourth NFP subunit. The relative plasticity of the peripherin network may account for its possible role during development, when axons have to find their targets, and when axons regenerate. In addition to their expression in muscle, other IFPs, such as syncoilin and synemin, are also expressed in neuronal tissues. Syncoilin modulates peripherin filament networks. Synemin M, associated with peripherin, is present in small unmyelinated fibers, whereas synemin L is produced in large neurons with myelinated fibers positive for the light-chain neurofilament (NF-L) subunit. Nestin is an IFP expressed in dividing cells during early stages of development in the central and peripheral nervous systems, and in muscles and other tissues. After differentiation, nestin is downregulated and replaced by tissue-specific IFPs. IFPs in glial cells are primarily composed of GFAP, although vimentin is also expressed; vimentin is also widely distributed in mesenchymal derivatives and established cell lines. In the peripheral nervous system, NFPs appear early in its development and progressively replace vimentin, which is expressed before NFPs in most, if not all, dividing neuroepithelial cells. In addition, in tissues undergoing an injury response, the unique and complex cell and tissue distribution of IFPs can be markedly modified.


Subject(s)
Intermediate Filaments/pathology , Peripheral Nervous System Diseases/pathology , Peripheral Nervous System/pathology , Peripheral Nervous System/physiology , Humans , Intermediate Filaments/metabolism
2.
Peptides ; 26(9): 1567-72, 2005 Sep.
Article in English | MEDLINE | ID: mdl-16112394

ABSTRACT

The media of the rat hepatic portal vein is composed of an internal circular muscular layer (CL) and an external longitudinal muscular layer (LL). These two perpendicular layers differentiate progressively from mesenchymal cells within the first month after birth. In this paper, we studied the development of calcitonin gene-related peptide (CGRP) innervation during post-natal differentiation of the vessel. We show that CGRP innervation is already present around the vessel at birth in the future adventitia but far from the lumen of the vessel. Progressively, CGRP immunoreactive fibers reached first LL then CL. CL by itself become only innervated at day 14 after birth. This corresponds to the time at which thick filaments (myosin) are visible in electron microscopy and desmin visualisable by immunocytochemistry. Furthermore, we provide evidence by autoradiography, that binding sites for CGRP are transiently expressed on the portal vein media at day 1 and 14 after birth. Vascular smooth muscle cells were transfected with constructs containing promoters for desmin or smooth muscle myosin heavy chain (smMHC). CGRP treatment of the cells significantly increased the expression of smMHC. Overall these results suggest that CGRP can potentially influence the differentiation of smooth muscle cells from the vessel wall.


Subject(s)
Calcitonin Gene-Related Peptide/physiology , Cell Differentiation/physiology , Muscle, Smooth, Vascular/growth & development , Myocytes, Smooth Muscle/physiology , Portal Vein/growth & development , Age Factors , Animals , Binding Sites , Calcitonin Gene-Related Peptide/analysis , Calcitonin Gene-Related Peptide/pharmacology , Cell Line , Connective Tissue/innervation , Gene Expression/drug effects , Humans , Immunohistochemistry , Liver/blood supply , Luciferases/genetics , Luciferases/metabolism , Mice , Muscle, Smooth, Vascular/innervation , Myocytes, Smooth Muscle/drug effects , Myosin Heavy Chains/genetics , Neuropeptides/pharmacology , Neuropeptides/physiology , Portal Vein/chemistry , Portal Vein/innervation , Promoter Regions, Genetic/genetics , Rabbits , Rats , Rats, Wistar , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Transfection
3.
Arch Mal Coeur Vaiss ; 98(6): 655-60, 2005 Jun.
Article in French | MEDLINE | ID: mdl-16007820

ABSTRACT

Serum response factor (SRF) is a widely expressed transcription factor involved in the transcription of various genes linked to muscle differentiation and cellular growth. Recent studies show the pivotal role of SRF in orchestrating genetic programs essential for cardiac development and function. Dominant negative isoforms of SRF resulting from caspase cleavage or alternative splicing have been identified in different forms of cardiomyopathies. This review summarizes the role of SRF, its structure, function and its role in human cardiopathies. Finally, we discuss the results of recently developed murine models which address the role of SRF in the adult heart in vivo. The existing biological data suggest that SRF could be a target of neurohumoral activation which is involved in myocardial hypertrophy. Conversely, inhibition of SRF activity in different murine models leads to dilated cardiomyopathy.


Subject(s)
Cardiomyopathy, Dilated/physiopathology , Heart/growth & development , Hypertrophy, Left Ventricular/physiopathology , Hypertrophy, Right Ventricular/physiopathology , Serum Response Factor/physiology , Animals , Cardiomyopathy, Dilated/veterinary , Disease Models, Animal , Humans , Hypertrophy, Left Ventricular/veterinary , Hypertrophy, Right Ventricular/veterinary , Mice
4.
Circ Res ; 88(5): 468-75, 2001 Mar 16.
Article in English | MEDLINE | ID: mdl-11249869

ABSTRACT

Gene transfer with adenoviral vectors is an attractive approach for the treatment of atherosclerosis and restenosis. However, because expression of a therapeutic gene in nontarget tissues may have deleterious effects, artery-specific expression is desirable. Although expression vectors containing transcriptional regulatory elements of genes expressed solely in smooth muscle cells (SMCs) have proved efficient to restrict expression of the transgene, their use in the clinical setting can be limited by their reduced strength. In the present study, we show that low levels of transgene expression are obtained with the smooth muscle (SM)-specific SM22alpha promoter compared with the viral cytomegalovirus (CMV) enhancer/promoter. We have generated chimeric transcriptional cassettes containing either a SM (SM-myosin heavy chain) or a skeletal muscle (creatine kinase) enhancer combined with the SM22alpha promoter. With both constructs we observed significantly stronger expression that remains SM-specific. In vivo, reporter gene expression was restricted to arterial SMCs with no detectable signal at remote sites. Moreover, when interferon-gamma expression was driven by one of these two chimeras, SMC growth was inhibited as efficiently as with the CMV promoter. Finally, we demonstrate that neointima formation in the rat carotid balloon injury model was reduced to the same extent by adenoviral gene transfer of interferon-gamma driven either by the SM-myosin heavy chain enhancer/SM22alpha promoter or the CMV promoter. These results indicate that such vectors can be useful for the treatment of hyperproliferative vascular disorders.


Subject(s)
Enhancer Elements, Genetic/genetics , Muscle Proteins/genetics , Muscle, Smooth, Vascular/metabolism , Promoter Regions, Genetic/genetics , Adenoviridae/genetics , Animals , Cardiovascular Diseases/genetics , Cardiovascular Diseases/therapy , Carotid Arteries/metabolism , Cell Differentiation , Cell Division , Cell Line , Cells, Cultured , Cytomegalovirus/genetics , Gene Expression , Gene Transfer Techniques , Genetic Therapy , Genetic Vectors/genetics , Green Fluorescent Proteins , Humans , Interferon-gamma/genetics , Interferon-gamma/metabolism , Luminescent Proteins/genetics , Luminescent Proteins/metabolism , Mice , Mice, Inbred C57BL , Microfilament Proteins/genetics , Muscle, Smooth, Vascular/cytology , Myosin Heavy Chains/genetics , Rats , Recombinant Fusion Proteins/genetics , Recombinant Fusion Proteins/metabolism , Sensitivity and Specificity , Tumor Cells, Cultured , Tunica Intima/metabolism
5.
Dev Biol ; 226(2): 192-208, 2000 Oct 15.
Article in English | MEDLINE | ID: mdl-11023680

ABSTRACT

The desmin gene encodes an intermediate filament protein that is present in skeletal, cardiac, and smooth muscle cells. This study shows that the 4-kb upstream region of the murine desmin promoter directs expression of a lacZ reporter gene throughout the heart from E7.5 and in skeletal muscle and vascular smooth muscle cells from E9. 5. The distal fragment (-4005/-2495) is active in arterial smooth muscle cells but not in venous smooth muscle cells or in the heart in vivo. It contains a CArG/octamer overlapping element (designated CArG4) that can bind the serum response factor (SRF) and an Oct-like factor. The desmin distal fragment can replace a SM22alpha regulatory region (-445/-126) that contains two CArG boxes, to cis-activate a minimal (-125/+65) SM22alpha promoter fragment in arterial smooth muscle cells of transgenic embryos. lacZ expression was abolished when mutations were introduced into the desmin CArG4 element that abolished the binding of SRF and/or Oct-like factor. These data suggest that a new type of combined CArG/octamer element plays a prominent role in the regulation of the desmin gene in arterial smooth muscle cells, and SRF and Oct-like factor could cooperate to drive specific expression in these cells.


Subject(s)
Desmin/genetics , Gene Expression Regulation, Developmental/genetics , Muscle Proteins/genetics , Muscle, Smooth, Vascular/metabolism , Promoter Regions, Genetic , Regulatory Sequences, Nucleic Acid , Transcription, Genetic/genetics , 3T3 Cells , Amino Acid Motifs , Animals , Base Sequence , Cardiovascular System/embryology , Cardiovascular System/growth & development , Cardiovascular System/metabolism , Cells, Cultured , Consensus Sequence , DNA-Binding Proteins/metabolism , DNA-Binding Proteins/pharmacology , Fetal Heart/metabolism , Gene Expression Regulation, Developmental/drug effects , Genes , Genes, Reporter , Lac Operon , Mice , Mice, Transgenic , Microfilament Proteins/deficiency , Microfilament Proteins/genetics , Microfilament Proteins/physiology , Molecular Sequence Data , Muscle Development , Muscle Proteins/deficiency , Muscle Proteins/physiology , Muscle, Skeletal/embryology , Muscle, Skeletal/growth & development , Muscle, Skeletal/metabolism , Muscle, Smooth, Vascular/cytology , Mutagenesis, Site-Directed , Nuclear Proteins/metabolism , Nuclear Proteins/pharmacology , Serum Response Factor , Transcription Factors/metabolism , Transcription Factors/pharmacology , Transcription, Genetic/drug effects , Transfection , beta-Galactosidase/analysis , beta-Galactosidase/genetics
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