Increased expression of Myosin binding protein H in the skeletal muscle of amyotrophic lateral sclerosis patients

Handle URI:
http://hdl.handle.net/10754/563293
Title:
Increased expression of Myosin binding protein H in the skeletal muscle of amyotrophic lateral sclerosis patients
Authors:
Conti, Antonio; Riva, Nilo; Pesca, Mariasabina Sabina; Iannaccone, Sandro; Cannistraci, Carlo; Corbo, Massimo; Previtali, Stefano Carlo; Quattrini, Angelo; Alessio, Massimo
Abstract:
Amyotrophic lateral sclerosis (ALS) is a severe and fatal neurodegenerative disease of still unknown pathogenesis. Recent findings suggest that the skeletal muscle may play an active pathogenetic role. To investigate ALS's pathogenesis and to seek diagnostic markers, we analyzed skeletal muscle biopsies with the differential expression proteomic approach. We studied skeletal muscle biopsies from healthy controls (CN), sporadic ALS (sALS), motor neuropathies (MN) and myopathies (M). Pre-eminently among several differentially expressed proteins, Myosin binding protein H (MyBP-H) expression in ALS samples was anomalously high. MyBP-H is a component of the thick filaments of the skeletal muscle and has strong affinity for myosin, but its function is still unclear. High MyBP-H expression level was associated with abnormal expression of Rho kinase 2 (ROCK2), LIM domain kinase 1 (LIMK1) and cofilin2, that might affect the actin-myosin interaction. We propose that MyBP-H expression level serves, as a putative biomarker in the skeletal muscle, to discriminate ALS from motor neuropathies, and that it signals the onset of dysregulation in actin-myosin interaction; this in turn might contribute to the pathogenesis of ALS. © 2013 Elsevier B.V.
KAUST Department:
Applied Mathematics and Computational Science Program; Integrative Systems Biology Lab; Computational Bioscience Research Center (CBRC)
Publisher:
Elsevier BV
Journal:
Biochimica et Biophysica Acta (BBA) - Molecular Basis of Disease
Issue Date:
Jan-2014
DOI:
10.1016/j.bbadis.2013.10.013
PubMed ID:
24184715
Type:
Article
ISSN:
09254439
Sponsors:
This work was supported by MoH, RF07-ALS. The authors declare no conflict of interest
Appears in Collections:
Articles; Applied Mathematics and Computational Science Program; Computational Bioscience Research Center (CBRC)

Full metadata record

DC FieldValue Language
dc.contributor.authorConti, Antonioen
dc.contributor.authorRiva, Niloen
dc.contributor.authorPesca, Mariasabina Sabinaen
dc.contributor.authorIannaccone, Sandroen
dc.contributor.authorCannistraci, Carloen
dc.contributor.authorCorbo, Massimoen
dc.contributor.authorPrevitali, Stefano Carloen
dc.contributor.authorQuattrini, Angeloen
dc.contributor.authorAlessio, Massimoen
dc.date.accessioned2015-08-03T11:45:03Zen
dc.date.available2015-08-03T11:45:03Zen
dc.date.issued2014-01en
dc.identifier.issn09254439en
dc.identifier.pmid24184715en
dc.identifier.doi10.1016/j.bbadis.2013.10.013en
dc.identifier.urihttp://hdl.handle.net/10754/563293en
dc.description.abstractAmyotrophic lateral sclerosis (ALS) is a severe and fatal neurodegenerative disease of still unknown pathogenesis. Recent findings suggest that the skeletal muscle may play an active pathogenetic role. To investigate ALS's pathogenesis and to seek diagnostic markers, we analyzed skeletal muscle biopsies with the differential expression proteomic approach. We studied skeletal muscle biopsies from healthy controls (CN), sporadic ALS (sALS), motor neuropathies (MN) and myopathies (M). Pre-eminently among several differentially expressed proteins, Myosin binding protein H (MyBP-H) expression in ALS samples was anomalously high. MyBP-H is a component of the thick filaments of the skeletal muscle and has strong affinity for myosin, but its function is still unclear. High MyBP-H expression level was associated with abnormal expression of Rho kinase 2 (ROCK2), LIM domain kinase 1 (LIMK1) and cofilin2, that might affect the actin-myosin interaction. We propose that MyBP-H expression level serves, as a putative biomarker in the skeletal muscle, to discriminate ALS from motor neuropathies, and that it signals the onset of dysregulation in actin-myosin interaction; this in turn might contribute to the pathogenesis of ALS. © 2013 Elsevier B.V.en
dc.description.sponsorshipThis work was supported by MoH, RF07-ALS. The authors declare no conflict of interesten
dc.publisherElsevier BVen
dc.subjectAmyotrophic lateral sclerosisen
dc.subjectMyosin binding protein Hen
dc.subjectSkeletal muscleen
dc.titleIncreased expression of Myosin binding protein H in the skeletal muscle of amyotrophic lateral sclerosis patientsen
dc.typeArticleen
dc.contributor.departmentApplied Mathematics and Computational Science Programen
dc.contributor.departmentIntegrative Systems Biology Laben
dc.contributor.departmentComputational Bioscience Research Center (CBRC)en
dc.identifier.journalBiochimica et Biophysica Acta (BBA) - Molecular Basis of Diseaseen
dc.contributor.institutionProteome Biochemistry, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italyen
dc.contributor.institutionDepartment of Neurology, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italyen
dc.contributor.institutionINSPE-Institute of Experimental Neurology, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italyen
dc.contributor.institutionClinical Neurosciences, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italyen
dc.contributor.institutionNeuromuscular Repair, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italyen
dc.contributor.institutionExperimental Neuropathology, San Raffaele Scientific Institute, Via Olgettina 58, 20132 Milan, Italyen
dc.contributor.institutionDepartment of Neurorehabilitation Sciences, Casa Cura Policlinico, Milan, Italyen
dc.contributor.institutionFarmaceutical Sciences, Salerno University, Fisciano, SA, Italyen
kaust.authorCannistraci, Carloen

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