Presence of connectin-like protein in white blood cells and platelets.

Hashimoto, Kohzoh; Kamitani, T; Wada, Yuko; Tatsumi, Noriyuki

doi:10.1620/tjem.143.59

Cited by 6 publications

(6 citation statements)

References 20 publications

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“…Only one of the cell lines tested revealed titin staining and this was the human line RD, known to be derived from a rhabdomyosarcoma--a tumor of skeletal muscle origin (3). These results differ from a few reports suggesting that titin may be present in smooth muscle like chicken gizzard (10) and even in human lymphocytes (6). Although these proposals are based primarily on immunofluoreseence microscopical results with polyclonal antibodies, we could accomodate them only by assuming that smooth muscle and noamttscle cells, which are not reactive with any of our monoclonal antibodies, would express titins distinct from those found in sarcomeric muscles.…”

Section: Discussioncontrasting

confidence: 93%

“…This is in line with labeling experiments using titin antibodies on a variety of nonmuscle tissues and cell lines of rodent and human origin as well as cultured chick embryo fibroblasts. Although titin-like proteins have been reported occasionally in some nonmuscle cell types (4,6), our results with T1, T3, and T4 antibodies were uniformly negative (Table I). The sole permanent cell line which showed titin is the RD line derived from a human rhabdomyosarcoma (see reference 3).…”

Section: Titin Expression In Cultured Embryonic Chicken Skeletal and contrasting

confidence: 45%

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Monoclonal antibodies distinguish titins from heart and skeletal muscle.

Hill¹,

Weber²

1986

The Journal of Cell Biology

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Abstract. Murine monoclonal antibodies specific for titin have been elicited using a chicken heart muscle residue as antigen. The three antibodies T 1, T3, and T4 recognize both bands of the titin doublet in immunoblot analysis on polypeptides from chicken breast muscle. In contrast, on chicken cardiac myofibrils two of the antibodies (T 1, T4) react only with the upper band of the doublet indicating immunological differences between heart and skeletal muscle titin. This difference is even more pronounced for rat and mouse. Although all three antibodies react with skeletal muscle titin, T 1 and T4 did not detect heart titin, whereas T3 reacts with this titin both in immunofluorescence microscopy and in immunoblots. Immunofluorescence microscopy of myofibrils and frozen tissues from a variety of vertebrates extends these results and shows that the three antibodies recognize different epitopes. All three titin antibodies decorate at the A

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Section: Discussioncontrasting

confidence: 93%

Section: Titin Expression In Cultured Embryonic Chicken Skeletal and contrasting

confidence: 45%

Monoclonal antibodies distinguish titins from heart and skeletal muscle.

Hill¹,

Weber²

1986

The Journal of Cell Biology

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“…Putative non-muscle titin has been identified in platelets, 26 in fibroblasts, in HeLa cells, 13,15 , in the intestinal epithelial brush border, 4,6 and in avian smooth muscle. 8,10,12 In contrast to striated muscle titin, the giant protein species from smooth muscle and non-muscle tissues have been difficult to characterize due to an overall low level of their expression.…”

Section: Discussionmentioning

confidence: 99%

Expression of Distinct Classes of Titin Isoforms in Striated and Smooth Muscles by Alternative Splicing, and Their Conserved Interaction with Filamins

Labeit

Lahmers

Burkart

et al. 2006

Journal of Molecular Biology

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“…As an elastic component, titin is postulated to maintain the thick filaments in register and resist overstretching of the sarcomere (6,7,16,23,26). Nebulin (6-8 • 105 D molecular weight), which is coextensive with each thin filament in skeletal muscle, is postulated to dictate the uniform thin filament length by providing a template for actin polymerization (8,13,28).Titin-like molecules have been reported to exist in various nonmuscle systems (3,4,16), but the structure and function of these proteins remain uncharacterized. Nebulin has been found only in skeletal muscle and is absent even from cardiac muscle (28).…”

mentioning

confidence: 99%

“…Titin-like molecules have been reported to exist in various nonmuscle systems (3,4,16), but the structure and function of these proteins remain uncharacterized. Nebulin has been found only in skeletal muscle and is absent even from cardiac muscle (28).…”

mentioning

confidence: 99%

Identification and characterization of two huge protein components of the brush border cytoskeleton: evidence for a cellular isoform of titin.

Eilertsen

Keller

1992

The Journal of Cell Biology

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Abstract. Two extremely high molecular weight proteins were found to be components of the intestinal epithelial cell brush border cytoskeleton. The largest brush border protein, designated T-protein, migrated on SDS gels as a doublet of polypeptides with molecular weights similar to muscle titin T I and T II. The other large brush border protein, designated N-protein, was found to have a polypeptide molecular weight similar to muscle nebulin. In Western analysis, a polyclonal antibody raised against brush border T-protein reacted specifically with T-protein in isolated brush borders and cross-reacted with titin in pectoralis and cardiac muscle samples. T-protein was distinguished from the muscle titins by an anti-cardiac titin mAb. A polyclonal antibody raised against N-protein was specific for N-protein in brush borders and crossreacted with nothing in pectoralis muscle. Immunolocalization in cryosections of intestinal epithelia and SDS-PAGE analysis of fractionated brush borders revealed that both T-protein and N-protein are concentrated distinctly in the brush border terminal web region subjacent to the microvilli, but absent from the microvilli. EM of rotary-replicated T-protein samples revealed many of the molecules to be long (912 + 40 nm) and fibrous with a globular head on one end. In some of the molecules, the head domain appeared to be extended in a fibrous conformation yielding T-protein up to 1,700-nm long. The brush border N-protein was found as long polymers with a repeating structural unit of ~450 nm. Our findings indicate that brush border T-protein is a cellular isoform of titin and suggest that both T-protein and N-protein play structural roles in the brush border terminal web.T n~ brush border array of microvilli at the apical end of intestinal epithelial cells is supported by one of the most extensively organized actin-based cytoskeletons found in nonmuscle cells (for review of brush border structure, see references 1, 12, 18). This cytoskeleton is a useful model system with which to identify structural components, because it can be isolated intact and in amounts sufficient for biochemical analysis. Moreover, the multiple domain structure of the brush border cytoskeleton aids in determining the functional and structural contributions of each component.In the brush border, each of the numerous microvilli is supported by a core bundle of parallel actin filaments that is rooted in the underlying terminal web. Numerous filaments of myosin II and fodrin cross-link the microvillar bundle rootlets. This interrootlet domain is encompassed by a circumferential ring of anti-parallel actin filaments. Several major brush border proteins have been characterized and their localization in these brush border domains has yielded insight into their possible functions. Many of the proteins in this integrated system are related to components of various cytoskeletal organizations in other cells (12).We report here the discovery of two huge proteins in the brush border terminal web. These cytoskeletal proteins ten...

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Presence of connectin-like protein in white blood cells and platelets.

Cited by 6 publications

References 20 publications

Monoclonal antibodies distinguish titins from heart and skeletal muscle.

Monoclonal antibodies distinguish titins from heart and skeletal muscle.

Expression of Distinct Classes of Titin Isoforms in Striated and Smooth Muscles by Alternative Splicing, and Their Conserved Interaction with Filamins

Identification and characterization of two huge protein components of the brush border cytoskeleton: evidence for a cellular isoform of titin.

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