Linked Life Data

11822876

Source:http://linkedlifedata.com/resource/pubmed/id/11822876

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2002-2-1
pubmed:abstractText
To evaluate nebulette's role in cardiac myofibrils, cardiomyocytes expressing green fluorescent protein (GFP)-nebulette constructs were monitored for their ability to contract and myofilament protein distribution was analyzed. Cells expressing full-length GFP-nebulette appear unaffected and exhibit normal beating frequencies. Expression of the GFP linker and SH3 results in loss of the endogenous nebulette and tropomyosin; however, Z-line and thick filaments are undisturbed. Cells expressing either of these domains have dramatically reduced beating frequencies, consistent with the loss of thin filament proteins. This loss was inhibited by the addition of protease inhibitors during culturing. The GFP repeat domain disrupts both myofibrillogenesis and contraction in spreading cardiomyocytes, whereas introduction of this protein into well-spread cardiomyocytes results in localization at the Z-line and a 50% reduction in beating frequency. Ultimately, these cells form bundles containing the GFP repeat and many myofilament proteins. Interestingly, butanedione monoxime inhibition of contraction inhibited the formation of these bundles. These results show that the GFP-nebulette domains have a dominant-negative effect on the distribution and function of the sarcomeric proteins. Taken together with the observation that nebulette colocalizes with alpha-actinin in the pre-, nascent, and mature myofibrils, our data demonstrate the importance of this cardiac-specific nebulin isoform in myofibril organization and function.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0014-4827
pubmed:author
pubmed:copyrightInfo
©2002 Elsevier Science (USA).
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
204-18
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:11822876-Actin Cytoskeleton, pubmed-meshheading:11822876-Actins, pubmed-meshheading:11822876-Animals, pubmed-meshheading:11822876-Carrier Proteins, pubmed-meshheading:11822876-Cells, Cultured, pubmed-meshheading:11822876-Chick Embryo, pubmed-meshheading:11822876-Cytoskeletal Proteins, pubmed-meshheading:11822876-Gene Targeting, pubmed-meshheading:11822876-Humans, pubmed-meshheading:11822876-LIM Domain Proteins, pubmed-meshheading:11822876-Microfilament Proteins, pubmed-meshheading:11822876-Muscle Proteins, pubmed-meshheading:11822876-Mutagenesis, pubmed-meshheading:11822876-Myocardium, pubmed-meshheading:11822876-Myofibrils, pubmed-meshheading:11822876-Protein Structure, Tertiary, pubmed-meshheading:11822876-Recombinant Fusion Proteins, pubmed-meshheading:11822876-Repetitive Sequences, Nucleic Acid, pubmed-meshheading:11822876-Sarcomeres, pubmed-meshheading:11822876-Tropomyosin, pubmed-meshheading:11822876-Troponin
pubmed:year
2002
pubmed:articleTitle
Targeted disruption of nebulette protein expression alters cardiac myofibril assembly and function.
pubmed:affiliation
Department of Chemistry and Biochemistry, University of Texas at Austin, Austin, Texas 78712, USA.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.