Marie-Louise Bang

@article{pmid31647200,

title = {Myopalladin promotes muscle growth through modulation of the serum response factor pathway},

author = {M C Filomena and D L Yamamoto and M Caremani and V K Kadarla and G Mastrototaro and S Serio and A Vydyanath and M Mutarelli and A Garofalo and I Pertici and R Knöll and V Nigro and P K Luther and R L Lieber and M R Beck and M Linari and M L Bang},

year  = {2020},

date = {2020-01-01},

journal = {J Cachexia Sarcopenia Muscle},

volume = {11},

number = {1},

pages = {169--194},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{bang_animal_2017,

title = {Animal Models of Congenital Cardiomyopathies Associated With Mutations in Z-Line Proteins},

author = {Marie-Louise Bang},

doi = {10.1002/jcp.25424},

issn = {1097-4652},

year  = {2017},

date = {2017-01-01},

journal = {Journal of Cellular Physiology},

volume = {232},

number = {1},

pages = {38--52},

abstract = {The cardiac Z-line at the boundary between sarcomeres is a multiprotein complex connecting the contractile apparatus with the cytoskeleton and the extracellular matrix. The Z-line is important for efficient force generation and transmission as well as the maintenance of structural stability and integrity. Furthermore, it is a nodal point for intracellular signaling, in particular mechanosensing and mechanotransduction. Mutations in various genes encoding Z-line proteins have been associated with different cardiomyopathies, including dilated cardiomyopathy, hypertrophic cardiomyopathy, arrhythmogenic right ventricular cardiomyopathy, restrictive cardiomyopathy, and left ventricular noncompaction, and mutations even within the same gene can cause widely different pathologies. Animal models have contributed to a great advancement in the understanding of the physiological function of Z-line proteins and the pathways leading from mutations in Z-line proteins to cardiomyopathy, although genotype-phenotype prediction remains a great challenge. This review presents an overview of the currently available animal models for Z-line and Z-line associated proteins involved in human cardiomyopathies with special emphasis on knock-in and transgenic mouse models recapitulating the clinical phenotypes of human cardiomyopathy patients carrying mutations in Z-line proteins. Pros and cons of mouse models will be discussed and a future outlook will be given. J. Cell. Physiol. 232: 38-52, 2017. textcopyright 2016 Wiley Periodicals, Inc.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{mastrototaro_nebulette_2015,

title = {Nebulette knockout mice have normal cardiac function, but show Z-line widening and up-regulation of cardiac stress markers},

author = {Giuseppina Mastrototaro and Xingqun Liang and Xiaodong Li and Pierluigi Carullo and Nicoletta Piroddi and Chiara Tesi and Yusu Gu and Nancy D Dalton and Kirk L Peterson and Corrado Poggesi and Farah Sheikh and Ju Chen and Marie-Louise Bang},

doi = {10.1093/cvr/cvv156},

issn = {1755-3245},

year  = {2015},

date = {2015-07-01},

journal = {Cardiovascular Research},

volume = {107},

number = {2},

pages = {216--225},

abstract = {AIMS: Nebulette is a 109 kDa modular protein localized in the sarcomeric Z-line of the heart. In vitro studies have suggested a role of nebulette in stabilizing the thin filament, and missense mutations in the nebulette gene were recently shown to be causative for dilated cardiomyopathy and endocardial fibroelastosis in human and mice. However, the role of nebulette in vivo has remained elusive. To provide insights into the function of nebulette in vivo, we generated and studied nebulette-deficient (nebl(-) (/-)) mice. 

METHODS AND RESULTS: Nebl(-) (/-) mice were generated by replacement of exon 1 by Cre under the control of the endogenous nebulette promoter, allowing for lineage analysis using the ROSA26 Cre reporter strain. This revealed specific expression of nebulette in the heart, consistent with in situ hybridization results. Nebl(-) (/-) mice exhibited normal cardiac function both under basal conditions and in response to transaortic constriction as assessed by echocardiography and haemodynamic analyses. Furthermore, histological, IF, and western blot analysis showed no cardiac abnormalities in nebl(-) (/-) mice up to 8 months of age. In contrast, transmission electron microscopy showed Z-line widening starting from 5 months of age, suggesting that nebulette is important for the integrity of the Z-line. Furthermore, up-regulation of cardiac stress responsive genes suggests the presence of chronic cardiac stress in nebl(-) (/-) mice. 

CONCLUSION: Nebulette is dispensable for normal cardiac function, although Z-line widening and up-regulation of cardiac stress markers were found in nebl(-) (/-) heart. These results suggest that the nebulette disease causing mutations have dominant gain-of-function effects.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid26321576,

title = {Roles of Nebulin Family Members in the Ħeart},

author = {M L Bang and J Chen},

year  = {2015},

date = {2015-01-01},

journal = {Circ J},

volume = {79},

number = {10},

pages = {2081--2087},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{bang_muscle_2014,

title = {The muscle ankyrin repeat proteins CARP, Ankrd2, and DARP are not essential for normal cardiac development and function at basal conditions and in response to pressure overload},

author = {Marie-Louise Bang and Yusu Gu and Nancy D Dalton and Kirk L Peterson and Kenneth R Chien and Ju Chen},

doi = {10.1371/journal.pone.0093638},

issn = {1932-6203},

year  = {2014},

date = {2014-01-01},

journal = {PloS One},

volume = {9},

number = {4},

pages = {e93638},

abstract = {Ankrd1/CARP, Ankrd2/Arpp, and Ankrd23/DARP belong to a family of stress inducible ankyrin repeat proteins expressed in striated muscle (MARPs). The MARPs are homologous in structure and localized in the nucleus where they negatively regulate gene expression as well as in the sarcomeric I-band, where they are thought to be involved in mechanosensing. Together with their strong induction during cardiac disease and the identification of causative Ankrd1 gene mutations in cardiomyopathy patients, this suggests their important roles in cardiac development, function, and disease. To determine the functional role of MARPs in vivo, we studied knockout (KO) mice of each of the three family members. Single KO mice were viable and had no apparent cardiac phenotype. We therefore hypothesized that the three highly homologous MARP proteins may have redundant functions in the heart and studied double and triple MARP KO mice. Unexpectedly, MARP triple KO mice were viable and had normal cardiac function both at basal levels and in response to mechanical pressure overload induced by transverse aortic constriction as assessed by echocardiography and hemodynamic studies. Thus, CARP, Ankrd2, and DARP are not essential for normal cardiac development and function at basal conditions and in response to mechanical pressure overload.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{yamamoto_nebulin_2013,

title = {The nebulin SH3 domain is dispensable for normal skeletal muscle structure but is required for effective active load bearing in mouse},

author = {Daniel L Yamamoto and Carmen Vitiello and Jianlin Zhang and David S Gokhin and Alessandra Castaldi and Gerald Coulis and Fabio Piaser and Maria Carmela Filomena and Peter J Eggenhuizen and Paolo Kunderfranco and Serena Camerini and Kazunori Takano and Takeshi Endo and Marco Crescenzi and Pradeep K L Luther and Richard L Lieber and Ju Chen and Marie-Louise Bang},

doi = {10.1242/jcs.137026},

issn = {1477-9137},

year  = {2013},

date = {2013-12-01},

journal = {Journal of Cell Science},

volume = {126},

number = {Pt 23},

pages = {5477--5489},

abstract = {Nemaline myopathy (NM) is a congenital myopathy with an estimated incidence of 150,000 live births. It is caused by mutations in thin filament components, including nebulin, which accounts for about 50% of the cases. The identification of NM cases with nonsense mutations resulting in loss of the extreme C-terminal SH3 domain of nebulin suggests an important role of the nebulin SH3 domain, which is further supported by the recent demonstration of its role in IGF-1-induced sarcomeric actin filament formation through targeting of N-WASP to the Z-line. To provide further insights into the functional significance of the nebulin SH3 domain in the Z-disk and to understand the mechanisms by which truncations of nebulin lead to NM, we took two approaches: (1) an affinity-based proteomic screening to identify novel interaction partners of the nebulin SH3 domain; and (2) generation and characterization of a novel knockin mouse model with a premature stop codon in the nebulin gene, eliminating its C-terminal SH3 domain (NebδSH3 mouse). Surprisingly, detailed analyses of NebδSH3 mice revealed no structural or histological skeletal muscle abnormalities and no changes in gene expression or localization of interaction partners of the nebulin SH3 domain, including myopalladin, palladin, zyxin and N-WASP. Also, no significant effect on peak isometric stress production, passive tensile stress or Young's modulus was found. However, NebδSH3 muscle displayed a slightly altered force-frequency relationship and was significantly more susceptible to eccentric contraction-induced injury, suggesting that the nebulin SH3 domain protects against eccentric contraction-induced injury and possibly plays a role in fine-tuning the excitation-contraction coupling mechanism.},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid19679637,

title = {Nebulin plays a direct role in promoting strong actin-myosin interactions},

author = {M L Bang and M Caremani and E Brunello and R Littlefield and R L Lieber and J Chen and V Lombardi and M Linari},

year  = {2009},

date = {2009-12-01},

journal = {FASEB J},

volume = {23},

number = {12},

pages = {4117--4125},

keywords = {},

pubstate = {published},

tppubtype = {article}

}

@article{pmid16769824,

title = {Nebulin-deficient mice exhibit shorter thin filament lengths and reduced contractile function in skeletal muscle},

author = {M L Bang and X Li and R Littlefield and S Bremner and A Thor and K U Knowlton and R L Lieber and J Chen},

year  = {2006},

date = {2006-06-01},

journal = {J Cell Biol},

volume = {173},

number = {6},

pages = {905--916},

keywords = {},

pubstate = {published},

tppubtype = {article}

}