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Journal article
Molecular identification and localization of cellular titin, a novel titin isoform in the fibroblast stress fiber
Cell motility and the cytoskeleton, Vol.64(6), pp.418-433
06/2007
PMID: 17366640
Web of Science ID: WOS:000246498800002
Abstract
We previously discovered a large titin-like protein-c-titin-in chicken epithelial brush border and human blood platelet extracts that binds alpha-actinin and organizes arrays of myosin II bipolar filaments in vitro. RT-PCR analysis of total RNA from human megakaryoblastic (CHRF-288-11) and mouse fibroblast (3T3) nonmuscle cells reveal sequences identical to known titin gene exon sequences that encode parts of the Z-line, I-band, PEVK domain, A-band, and M-line regions of striated muscle titins. In the nonmuscle cells, these sequences are differentially spliced in patterns not reported for any striated muscle titin isoform. Rabbit polyclonal antibodies raised against expressed protein fragments encoded by the Z-repeat and kinase domain regions react with the c-titin band in Western blot analysis of platelet extracts and immunoprecipitate c-titin in whole platelet extracts. Immunofluorescent localization demonstrates that the majority of the c-titin colocalizes with alpha-actinin and actin in 3T3 and Indian Muntjac deer skin fibroblast stress fibers. Our results suggest that differential expression of titin gene exons in nonmuscle cells yields multiple novel isoforms of the protein c-titin that are associated with the actin stress fiber structures.
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Details
- Title
- Molecular identification and localization of cellular titin, a novel titin isoform in the fibroblast stress fiber
- Publication Details
- Cell motility and the cytoskeleton, Vol.64(6), pp.418-433
- Resource Type
- Journal article
- Publisher
- Wiley Subscription Services, Inc., A Wiley Company
- Number of pages
- 16
- Copyright
- © 2007 Wiley-Liss, Inc.
- Identifiers
- WOS:000246498800002; 99380171295906600
- Academic Unit
- Biology; Hal Marcus College of Science and Engineering
- Language
- English