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Article ; Online: Targeting WIP1 phosphatase promotes partial remission in experimental collapsing glomerulopathy.

Duret, Lou C / Hamidouche, Tynhinane / Steers, Nicholas J / Pons, Catherine / Soubeiran, Nicolas / Buret, Delphine / Gilson, Eric / Gharavi, Ali G / D'Agati, Vivette D / Shkreli, Marina

Kidney international

2024 Volume 105, Issue 5, Page(s) 980–996

Abstract: Collapsing focal segmental glomerulosclerosis (FSGS), also known as collapsing glomerulopathy (CG), is the most aggressive variant of FSGS and is characterized by a rapid progression to kidney failure. Understanding CG pathogenesis represents a key step ... ...

Abstract	Collapsing focal segmental glomerulosclerosis (FSGS), also known as collapsing glomerulopathy (CG), is the most aggressive variant of FSGS and is characterized by a rapid progression to kidney failure. Understanding CG pathogenesis represents a key step for the development of targeted therapies. Previous work implicated the telomerase protein component TERT in CG pathogenesis, as transgenic TERT expression in adult mice resulted in a CG resembling that seen in human primary CG and HIV-associated nephropathy (HIVAN). Here, we used the telomerase-induced mouse model of CG (i-TERTci mice) to identify mechanisms to inhibit CG pathogenesis. Inactivation of WIP1 phosphatase, a p53 target acting in a negative feedback loop, blocked disease initiation in i-TERTci mice. Repression of disease initiation upon WIP1 deficiency was associated with senescence enhancement and required transforming growth factor-β functions. The efficacy of a pharmacologic treatment to reduce disease severity in both i-TERTci mice and in a mouse model of HIVAN (Tg26 mice) was then assessed. Pharmacologic inhibition of WIP1 enzymatic activity in either the telomerase mice with CG or in the Tg26 mice promoted partial remission of proteinuria and ameliorated kidney histopathologic features. Histological as well as high-throughput sequencing methods further showed that selective inhibition of WIP1 does not promote kidney fibrosis or inflammation. Thus, our findings suggest that targeting WIP1 may be an effective therapeutic strategy for patients with CG.
MeSH term(s)	Adult ; Humans ; Mice ; Animals ; Glomerulosclerosis, Focal Segmental/pathology ; Telomerase/therapeutic use ; AIDS-Associated Nephropathy/pathology ; Proteinuria ; Renal Insufficiency/complications ; Disease Models, Animal
Chemical Substances	Telomerase (EC 2.7.7.49)
Language	English
Publishing date	2024-02-27
Publishing country	United States
Document type	Journal Article
ZDB-ID	120573-0
ISSN	1523-1755 ; 0085-2538
ISSN (online)	1523-1755
ISSN	0085-2538
DOI	10.1016/j.kint.2024.02.009
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Zs.A 797: Show issues

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Article ; Online: L’anémone de mer Nematostella vectensis - Un modèle émergent pour la recherche biomédicale : mécano-sensibilité, régénération et longévité.

Amiel, Aldine R / Michel, Vincent / Carvalho, João E / Shkreli, Marina / Petit, Christine / Röttinger, Eric

Medecine sciences : M/S

2021 Volume 37, Issue 2, Page(s) 167–177

Abstract: Nematostella has fascinating features such as whole-body regeneration, the absence of signs of aging and importantly, the absence of age-related diseases. Easy to culture and spawn, this little sea anemone in spite of its "simple" aspect, displays ... ...

Title translation	The sea anemone Nematostella vectensis, an emerging model for biomedical research: Mechano-sensitivity, extreme regeneration and longevity.
Abstract	Nematostella has fascinating features such as whole-body regeneration, the absence of signs of aging and importantly, the absence of age-related diseases. Easy to culture and spawn, this little sea anemone in spite of its "simple" aspect, displays interesting morphological characteristics similar to vertebrates and an unexpected similarity in gene content/genome organization. Importantly, the scientific community working on Nematostella is developing a variety of functional genomics tools that enable scientists to use this anemone in the field of regenerative medicine, longevity and mecano-sensory diseases. As a complementary research model to vertebrates, this marine invertebrate is emerging and promising to dig deeper into those fields of research in an integrative manner (entire organism) and provides new opportunities for scientists to lift specific barriers that can be encountered with other commonly used animal models.
MeSH term(s)	Animals ; Biomedical Research/methods ; Biomedical Research/trends ; Genomics/methods ; Genomics/trends ; Longevity/physiology ; Mechanotransduction, Cellular/physiology ; Models, Animal ; Regeneration/physiology ; Regenerative Medicine/methods ; Regenerative Medicine/trends ; Sea Anemones/physiology
Language	French
Publishing date	2021-02-16
Publishing country	France
Document type	Journal Article ; Review
ZDB-ID	632733-3
ISSN	1958-5381 ; 0767-0974
ISSN (online)	1958-5381
ISSN	0767-0974
DOI	10.1051/medsci/2020282
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Article ; Online: Telomerase is required for glomerular renewal in kidneys of adult mice.

Montandon, Margo / Hamidouche, Tynhinane / Yart, Lucile / Duret, Lou C / Pons, Catherine / Soubeiran, Nicolas / Pousse, Mélanie / Cervera, Ludovic / Vial, Valérie / Fassy, Julien / Croce, Olivier / Gilson, Eric / Shkreli, Marina

NPJ Regenerative medicine

2022 Volume 7, Issue 1, Page(s) 15

Abstract: Homeostatic renal filtration relies on the integrity of podocytes, which function in glomerular filtration. These highly specialized cells are damaged in 90% of chronic kidney disease, representing the leading cause of end-stage renal failure. Although ... ...

Abstract	Homeostatic renal filtration relies on the integrity of podocytes, which function in glomerular filtration. These highly specialized cells are damaged in 90% of chronic kidney disease, representing the leading cause of end-stage renal failure. Although modest podocyte renewal has been documented in adult mice, the mechanisms regulating this process remain largely unknown and controversial. Using a mouse model of Adriamycin-induced nephropathy, we find that the recovery of filtration function requires up-regulation of the endogenous telomerase component TERT. Previous work has shown that transient overexpression of catalytically inactive TERT (i-TERT
Language	English
Publishing date	2022-02-11
Publishing country	United States
Document type	Journal Article
ISSN	2057-3995
ISSN (online)	2057-3995
DOI	10.1038/s41536-022-00212-z
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Article ; Online: Inhibition of eIF5A hypusination reprogrammes metabolism and glucose handling in mouse kidney.

Cougnon, Marc / Carcy, Romain / Melis, Nicolas / Rubera, Isabelle / Duranton, Christophe / Dumas, Karine / Tanti, Jean-François / Pons, Catherine / Soubeiran, Nicolas / Shkreli, Marina / Hauet, Thierry / Pellerin, Luc / Giraud, Sébastien / Blondeau, Nicolas / Tauc, Michel / Pisani, Didier F

Cell death & disease

2021 Volume 12, Issue 4, Page(s) 283

Abstract: Inhibition of the eukaryotic initiation factor 5A activation by the spermidine analogue GC7 has been shown to protect proximal cells and whole kidneys against an acute episode of ischaemia. The highlighted mechanism involves a metabolic switch from ... ...

Abstract	Inhibition of the eukaryotic initiation factor 5A activation by the spermidine analogue GC7 has been shown to protect proximal cells and whole kidneys against an acute episode of ischaemia. The highlighted mechanism involves a metabolic switch from oxidative phosphorylation toward glycolysis allowing cells to be transiently independent of oxygen supply. Here we show that GC7 decreases protein expression of the renal GLUT1 glucose transporter leading to a decrease in transcellular glucose flux. At the same time, GC7 modifies the native energy source of the proximal cells from glutamine toward glucose use. Thus, GC7 acutely and reversibly reprogrammes function and metabolism of kidney cells to make glucose its single substrate, and thus allowing cells to be oxygen independent through anaerobic glycolysis. The physiological consequences are an increase in the renal excretion of glucose and lactate reflecting a decrease in glucose reabsorption and an increased glycolysis. Such a reversible reprogramming of glucose handling and oxygen dependence of kidney cells by GC7 represents a pharmacological opportunity in ischaemic as well as hyperglycaemia-associated pathologies from renal origin.
MeSH term(s)	Animals ; Glucose/metabolism ; Kidney/metabolism ; Male ; Mice ; Peptide Initiation Factors/metabolism ; RNA-Binding Proteins/metabolism ; Eukaryotic Translation Initiation Factor 5A
Chemical Substances	Peptide Initiation Factors ; RNA-Binding Proteins ; Glucose (IY9XDZ35W2)
Language	English
Publishing date	2021-03-17
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2541626-1
ISSN	2041-4889 ; 2041-4889
ISSN (online)	2041-4889
ISSN	2041-4889
DOI	10.1038/s41419-021-03577-z
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Article ; Online: Cancer cells induce immune escape via glycocalyx changes controlled by the telomeric protein TRF2.

Cherfils-Vicini, Julien / Iltis, Charlene / Cervera, Ludovic / Pisano, Sabrina / Croce, Olivier / Sadouni, Nori / Győrffy, Balázs / Collet, Romy / Renault, Valérie M / Rey-Millet, Martin / Leonetti, Carlo / Zizza, Pasquale / Allain, Fabrice / Ghiringhelli, Francois / Soubeiran, Nicolas / Shkreli, Marina / Vivier, Eric / Biroccio, Annamaria / Gilson, Eric

The EMBO journal

2019 Volume 38, Issue 11

Abstract: Myeloid-derived suppressor cells (MDSCs) are immature myeloid cells with strong immunosuppressive activity that promote tumor growth. In this study, we describe a mechanism by which cancer cells control MDSCs in human cancers by upregulating TRF2, a ... ...

Abstract	Myeloid-derived suppressor cells (MDSCs) are immature myeloid cells with strong immunosuppressive activity that promote tumor growth. In this study, we describe a mechanism by which cancer cells control MDSCs in human cancers by upregulating TRF2, a protein required for telomere stability. Specifically, we showed that the TRF2 upregulation in cancer cells has extratelomeric roles in activating the expression of a network of genes involved in the biosynthesis of heparan sulfate proteoglycan, leading to profound changes in glycocalyx length and stiffness, as revealed by atomic force microscopy. This TRF2-dependent regulation facilitated the recruitment of MDSCs, their activation via the TLR2/MyD88/IL-6/STAT3 pathway leading to the inhibition of natural killer recruitment and cytotoxicity, and ultimately tumor progression and metastasis. The clinical relevance of these findings is supported by our analysis of cancer cohorts, which showed a correlation between high TRF2 expression and MDSC infiltration, which was inversely correlated with overall patient survival.
MeSH term(s)	Animals ; Cells, Cultured ; Female ; Gene Expression Regulation, Neoplastic ; Glycocalyx/genetics ; Glycocalyx/metabolism ; HEK293 Cells ; Humans ; Male ; Mice ; Mice, Inbred C57BL ; Mice, Nude ; Myeloid-Derived Suppressor Cells/metabolism ; Myeloid-Derived Suppressor Cells/physiology ; NIH 3T3 Cells ; Neoplasms/genetics ; Neoplasms/immunology ; Neoplasms/mortality ; Neoplasms/pathology ; Telomere/metabolism ; Telomeric Repeat Binding Protein 2/genetics ; Telomeric Repeat Binding Protein 2/physiology ; Tumor Escape/genetics ; Tumor Escape/physiology
Chemical Substances	TERF2 protein, human ; Telomeric Repeat Binding Protein 2
Language	English
Publishing date	2019-04-18
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	586044-1
ISSN	1460-2075 ; 0261-4189
ISSN (online)	1460-2075
ISSN	0261-4189
DOI	10.15252/embj.2018100012
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Zs.A 1808: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (1.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Involvement of the oncoprotein c-Myc in viral telomerase RNA gene regulation during Marek's disease virus-induced lymphomagenesis.

Shkreli, Marina / Dambrine, Ginette / Soubieux, Denis / Kut, Emmanuel / Rasschaert, Denis

Journal of virology

2007 Volume 81, Issue 9, Page(s) 4848–4857

Abstract: Marek's disease virus (MDV) is an alphaherpesvirus that induces a highly malignant T-lymphoma in chickens. The viral genome encodes two identical copies of a viral telomerase RNA subunit (vTR) that exhibits 88% sequence identity to its chicken ortholog ... ...

Abstract	Marek's disease virus (MDV) is an alphaherpesvirus that induces a highly malignant T-lymphoma in chickens. The viral genome encodes two identical copies of a viral telomerase RNA subunit (vTR) that exhibits 88% sequence identity to its chicken ortholog chTR. The minimal telomerase ribonucleoprotein complex consists of a protein subunit with reverse transcriptase activity (TERT) and an RNA subunit (TR). The active complex compensates for the progressive telomere shortening that occurs during mitosis and is involved in the cell immortalization process. We show here that the upregulation of telomerase activity is associated with an increase in vTR gene expression in chickens infected with the highly oncogenic MDV strain RB-1B. A comparative functional analysis of the viral and chicken TR promoters, based on luciferase reporter assays, revealed that the vTR promoter was up to threefold more efficient than the chTR promoter in avian cells. We demonstrated, by directed mutagenesis of the vTR promoter region, that the stronger transcriptional activity of the vTR promoter resulted largely from an E-box located two nucleotides downstream from the transcriptional start site of the vTR gene. Furthermore, transactivation assays and chromatin immunoprecipitation assays demonstrated the involvement of the c-Myc oncoprotein in the transcriptional regulation of vTR. Finally, an Ets binding site was specifically implicated in the transcriptional regulation of vTR in the MDV-transformed lymphoblastoid cell line MSB-1.
MeSH term(s)	Animals ; Blotting, Western ; Cell Line ; Chickens ; Chromatin Immunoprecipitation ; DNA Primers ; Gene Expression Regulation, Viral/physiology ; Herpesvirus 2, Gallid/genetics ; Herpesvirus 2, Gallid/physiology ; Luciferases ; Lymphoma, T-Cell/physiopathology ; Lymphoma, T-Cell/virology ; Mutagenesis ; Promoter Regions, Genetic/genetics ; Proto-Oncogene Proteins c-myc/metabolism ; RNA/genetics ; RNA/metabolism ; Reverse Transcriptase Polymerase Chain Reaction ; Telomerase/genetics ; Telomerase/metabolism
Chemical Substances	DNA Primers ; Proto-Oncogene Proteins c-myc ; telomerase RNA ; RNA (63231-63-0) ; Luciferases (EC 1.13.12.-) ; Telomerase (EC 2.7.7.49)
Language	English
Publishing date	2007-05
Publishing country	United States
Document type	Comparative Study ; Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	80174-4
ISSN	1098-5514 ; 0022-538X
ISSN (online)	1098-5514
ISSN	0022-538X
DOI	10.1128/JVI.02530-06
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Zs.A 609: Show issues

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Article ; Online: Disruption of telomerase trafficking by TCAB1 mutation causes dyskeratosis congenita.

Zhong, Franklin / Savage, Sharon A / Shkreli, Marina / Giri, Neelam / Jessop, Lea / Myers, Timothy / Chen, Renee / Alter, Blanche P / Artandi, Steven E

Genes & development

2011 Volume 25, Issue 1, Page(s) 11–16

Abstract: Dyskeratosis congenita (DC) is a genetic disorder of defective tissue maintenance and cancer predisposition caused by short telomeres and impaired stem cell function. Telomerase mutations are thought to precipitate DC by reducing either the catalytic ... ...

Abstract	Dyskeratosis congenita (DC) is a genetic disorder of defective tissue maintenance and cancer predisposition caused by short telomeres and impaired stem cell function. Telomerase mutations are thought to precipitate DC by reducing either the catalytic activity or the overall levels of the telomerase complex. However, the underlying genetic mutations and the mechanisms of telomere shortening remain unknown for as many as 50% of DC patients, who lack mutations in genes controlling telomere homeostasis. Here, we show that disruption of telomerase trafficking accounts for unknown cases of DC. We identify DC patients with missense mutations in TCAB1, a telomerase holoenzyme protein that facilitates trafficking of telomerase to Cajal bodies. Compound heterozygous mutations in TCAB1 disrupt telomerase localization to Cajal bodies, resulting in misdirection of telomerase RNA to nucleoli, which prevents telomerase from elongating telomeres. Our findings establish telomerase mislocalization as a novel cause of DC, and suggest that telomerase trafficking defects may contribute more broadly to the pathogenesis of telomere-related disease.
MeSH term(s)	Amino Acid Sequence ; Animals ; Dyskeratosis Congenita/enzymology ; Dyskeratosis Congenita/genetics ; Dyskeratosis Congenita/physiopathology ; Humans ; Models, Molecular ; Molecular Chaperones ; Mutation/genetics ; Pedigree ; Protein Transport/genetics ; Protein Transport/physiology ; Sequence Alignment ; Telomerase/genetics ; Telomerase/metabolism
Chemical Substances	Molecular Chaperones ; Telomerase (EC 2.7.7.49) ; WRAP53 protein, human (EC 2.7.7.49)
Language	English
Publishing date	2011-01-01
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, N.I.H., Intramural ; Research Support, Non-U.S. Gov't
ZDB-ID	806684-x
ISSN	1549-5477 ; 0890-9369
ISSN (online)	1549-5477
ISSN	0890-9369
DOI	10.1101/gad.2006411
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Zs.A 2292: Show issues			Location: Je nach Verfügbarkeit (siehe Angabe bei Bestand) bis Jg. 1994: Bestellungen von Artikeln über das Online-Bestellformular Jg. 1995 - 2021: Lesesall (2.OG) ab Jg. 2022: Lesesaal (EG)
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Article: Insertion of a foreign sequence on capsid surface loops of human papillomavirus type 16 virus-like particles reduces their capacity to induce neutralizing antibodies and delineates a conformational neutralizing epitope.

Sadeyen, Jean-Rémy / Tourne, Sylvie / Shkreli, Marina / Sizaret, Pierre-Yves / Coursaget, Pierre

Virology

2003 Volume 309, Issue 1, Page(s) 32–40

Abstract: The aims of this study were to generate chimeric human papillomavirus (HPV)-16 L1 virus-like particles (VLPs) in order to identify immunogenic domains and conformational neutralizing epitopes, and to characterize the regions where a foreign epitope could ...

Abstract	The aims of this study were to generate chimeric human papillomavirus (HPV)-16 L1 virus-like particles (VLPs) in order to identify immunogenic domains and conformational neutralizing epitopes, and to characterize the regions where a foreign epitope could be introduced. We hypothesized that these regions could be on L1 protein loops since they are exposed on the surface of VLPs. The aims of this study were achieved by mutating HPV-16 L1 proteins. Six amino acids encoding for the epitope 78-83 (DPASRE) of the hepatitis B core (HBc) antigen were introduced within the different loops of the L1 protein at positions 56/57, 140/141, 179/180, 266/267, 283/284 or 352/353. All these chimeric L1 proteins were capable of self-assembly into VLPs. The antigenicity and immunogenicity of some of these VLPs were reduced compared to the levels observed with wild-type VLPs. All were nevertheless able to induce neutralizing antibodies. VLPs with insertion at position 266/267 induced lower levels of neutralizing antibodies, suggesting the involvement of residues situated on FG loop in L1 neutralizing epitopes. All the chimeric L1 proteins except the one with insertion at position 56/57 were also able to induce anti-HBc antibodies, thus suggesting exposure of the HBc epitope on the VLP surface. Taken together, our findings indicate the possibility of designing HPV-derived vectors that are less immunogenic and suggest positions for insertion of defined immune epitopes or cell ligands into L1 protein to be exposed on the surface of VLPs.
MeSH term(s)	Base Sequence ; Capsid Proteins/chemistry ; Capsid Proteins/genetics ; Epitopes/chemistry ; Humans ; Neutralization Tests ; Oligodeoxyribonucleotides ; Papillomaviridae/genetics ; Papillomaviridae/immunology
Chemical Substances	Capsid Proteins ; Epitopes ; Oligodeoxyribonucleotides
Language	English
Publishing date	2003-04-25
Publishing country	United States
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	200425-2
ISSN	1096-0341 ; 0042-6822
ISSN (online)	1096-0341
ISSN	0042-6822
DOI	10.1016/s0042-6822(02)00134-4
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Article ; Online: Telomere protection and TRF2 expression are enhanced by the canonical Wnt signalling pathway.

Diala, Irmina / Wagner, Nicole / Magdinier, Frédérique / Shkreli, Marina / Sirakov, Maria / Bauwens, Serge / Schluth-Bolard, Caroline / Simonet, Thomas / Renault, Valérie M / Ye, Jing / Djerbi, Abdelnnadir / Pineau, Pascal / Choi, Jinkuk / Artandi, Steven / Dejean, Anne / Plateroti, Michelina / Gilson, Eric

EMBO reports

2013 Volume 14, Issue 4, Page(s) 356–363

Abstract: The DNA-binding protein TRF2 is essential for telomere protection and chromosome stability in mammals. We show here that TRF2 expression is activated by the Wnt/β-catenin signalling pathway in human cancer and normal cells as well as in mouse intestinal ... ...

Abstract	The DNA-binding protein TRF2 is essential for telomere protection and chromosome stability in mammals. We show here that TRF2 expression is activated by the Wnt/β-catenin signalling pathway in human cancer and normal cells as well as in mouse intestinal tissues. Furthermore, β-catenin binds to TRF2 gene regulatory regions that are functional in a luciferase transactivating assay. Reduced β-catenin expression in cancer cells triggers a marked increase in telomere dysfunction, which can be reversed by TRF2 overexpression. We conclude that the Wnt/β-catenin signalling pathway maintains a level of TRF2 critical for telomere protection. This is expected to have an important role during development, adult stem cell function and oncogenesis.
MeSH term(s)	Animals ; Binding Sites ; Female ; Gene Expression ; Gene Expression Regulation ; HCT116 Cells ; Humans ; Male ; Mice ; Mice, Knockout ; Oligonucleotide Array Sequence Analysis ; Protein Binding ; RNA, Messenger/genetics ; RNA, Messenger/metabolism ; Telomere Homeostasis ; Telomeric Repeat Binding Protein 2/genetics ; Telomeric Repeat Binding Protein 2/metabolism ; Transcriptome ; Wnt Signaling Pathway ; beta Catenin/metabolism
Chemical Substances	CTNNB1 protein, human ; RNA, Messenger ; TERF2 protein, human ; Telomeric Repeat Binding Protein 2 ; beta Catenin
Language	English
Publishing date	2013-02-22
Publishing country	England
Document type	Journal Article ; Research Support, Non-U.S. Gov't
ZDB-ID	2020896-0
ISSN	1469-3178 ; 1469-221X
ISSN (online)	1469-3178
ISSN	1469-221X
DOI	10.1038/embor.2013.16
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Article ; Online: Short telomeres and stem cell exhaustion model Duchenne muscular dystrophy in mdx/mTR mice.

Sacco, Alessandra / Mourkioti, Foteini / Tran, Rose / Choi, Jinkuk / Llewellyn, Michael / Kraft, Peggy / Shkreli, Marina / Delp, Scott / Pomerantz, Jason H / Artandi, Steven E / Blau, Helen M

Cell

2010 Volume 143, Issue 7, Page(s) 1059–1071

Abstract: In Duchenne muscular dystrophy (DMD), dystrophin mutation leads to progressive lethal skeletal muscle degeneration. For unknown reasons, dystrophin deficiency does not recapitulate DMD in mice (mdx), which have mild skeletal muscle defects and potent ... ...

Abstract	In Duchenne muscular dystrophy (DMD), dystrophin mutation leads to progressive lethal skeletal muscle degeneration. For unknown reasons, dystrophin deficiency does not recapitulate DMD in mice (mdx), which have mild skeletal muscle defects and potent regenerative capacity. We postulated that human DMD progression is a consequence of loss of functional muscle stem cells (MuSC), and the mild mouse mdx phenotype results from greater MuSC reserve fueled by longer telomeres. We report that mdx mice lacking the RNA component of telomerase (mdx/mTR) have shortened telomeres in muscle cells and severe muscular dystrophy that progressively worsens with age. Muscle wasting severity parallels a decline in MuSC regenerative capacity and is ameliorated histologically by transplantation of wild-type MuSC. These data show that DMD progression results, in part, from a cell-autonomous failure of MuSC to maintain the damage-repair cycle initiated by dystrophin deficiency. The essential role of MuSC function has therapeutic implications for DMD.
MeSH term(s)	Animals ; Cell Proliferation ; Disease Models, Animal ; Dystrophin/metabolism ; Humans ; Mice ; Mice, Inbred mdx ; Muscular Dystrophy, Animal/genetics ; Muscular Dystrophy, Duchenne/genetics ; Prejudice ; Stem Cells/metabolism ; Telomere/metabolism
Chemical Substances	Dystrophin
Language	English
Publishing date	2010-12-09
Publishing country	United States
Document type	Journal Article ; Research Support, N.I.H., Extramural ; Research Support, Non-U.S. Gov't
ZDB-ID	187009-9
ISSN	1097-4172 ; 0092-8674
ISSN (online)	1097-4172
ISSN	0092-8674
DOI	10.1016/j.cell.2010.11.039
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