Molecular Cloning of a New Intermediate Filament Protein Expressed by Radial Glia and Demonstration of Alternative Splicing in a Novel Heptad Repeat Region Located in the Carboxy-Terminal Tail Domain

Yuan, Yue; Lee, Ju-Ahng; Napier, Audrey; Cole, Gregory J.

doi:10.1006/mcne.1997.0627

Cited by 27 publications

(29 citation statements)

References 40 publications

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“…B: EAP-300-positive periarterial Purkinje fiber (ppf) tissue in the right ventricular wall of an HH42 chick embryo and (C) a sister section showing elevated Nkx-2.5 RNA levels in the same cells. EAP-300/transitin (Yuan et al, 1997) is a marker of Purkinje fibers at the stages shown . ca, coronary artery; e, endocardium; ppf, periarterial Purkinje fiber.…”

Section: Discussionmentioning

confidence: 99%

“…Figure 3A shows Nkx-2.5 protein immunolocalized specifically to the nuclei (green) of subendocardial Purkinje fibers (red, immunolabeled by EAP-300), but not in adjacent working myocytes at HH41. At this stage, EAP-300/transitin (Yuan et al, 1997) is a distinctive marker of pcs cells . Only some periarterial fibers, as identified by EAP-300 immunolabeling (Fig.…”

Section: Nkx-25 Mrna Is Elevated In Peripheral Conduction System Relmentioning

confidence: 98%

“…EAP-300/transitin (primary diluted 1:100 in PBS) and Nkx-2.5 (primary diluted 1:100 in PBS) immunolocalizations were carried out using antibodies characterized previously in Yuan et al (1997) and Kasahara et al (1998), respectively. Immunofluorescent labeling methods used are also detailed in earlier publications Cheng et al, 1999).…”

Section: Immunolocalizationmentioning

confidence: 99%

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Elevated expression of Nkx‐2.5 in developing myocardial conduction cells

et al. 2001

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A number of different phenotypes emerge from the mesoderm-derived cardiomyogenic cells of the embryonic tubular heart, including those comprising the cardiac conduction system. The transcriptional regulation of this phenotypic divergence within the cardiomyogenic lineage remains poorly characterized. A relationship between expression of the transcription factor Nkx-2.5 and patterning to form cardiogenic mesoderm subsequent to gastrulation is well established. Nkx-2.5 mRNA continues to be expressed in myocardium beyond the looped, tubular heart stage. To investigate the role of Nkx-2.5 in later development, we have determined the expression pattern of Nkx-2.5 mRNA by in situ hybridization in embryonic chick, fetal mouse, and human hearts, and of Nkx-2.5 protein by immunolocalization in the embryonic chick heart. As development progresses, significant nonuniformities emerge in Nkx-2.5 expression levels. Relative to surrounding forcegenerating ("working") myocardium, elevated Nkx-2.5 mRNA signal becomes apparent in the specialized cells of the conduction system. Similar differences are found in developing chick, human, and mouse fetal hearts, and nuclear-localized Nkx-2.5 protein is prominently expressed in differentiating chick conduction cells relative to adjacent working myocytes. This tissue-restricted expression of Nkx-2.5 is transient and correlates with the timing of spatio-temporal recruitment of cells to the central and the peripheral conduction system. Our data represent the first report of a transcription factor showing a stage-dependent restriction to different parts of the developing conduction system, and suggest some commonality in this development between birds and mammals. This dynamic pattern of expression is consistent with the hypothesis that Nkx-2.5, and its level of expression, have a role in regulation and/or maintenance of specialized fate selection by embryonic myocardial cells.

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Section: Discussionmentioning

confidence: 99%

Section: Nkx-25 Mrna Is Elevated In Peripheral Conduction System Relmentioning

confidence: 98%

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Elevated expression of Nkx‐2.5 in developing myocardial conduction cells

et al. 2001

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“…To test the physical interaction of Numb and transitin, we first performed far-western blotting analysis (Wakamatsu et al, 1999). Because of the large size of transitin (Yuan et al, 1997), pieces of transitin cDNA were subcloned into bacterial expression vectors (Fig. 3A) to obtain GST-fusion of the transitin recombinants.…”

Section: Physical Interaction Between Numb and Transitinmentioning

confidence: 99%

Transitin, a nestin-like intermediate filament protein, mediates cortical localization and the lateral transport of Numb in mitotic avian neuroepithelial cells

et al. 2007

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Neuroepithelium is an apicobasally polarized tissue that contains neural stem cells and gives rise to neurons and glial cells of the central nervous system. The cleavage orientation of neural stem cells is thought to be important for asymmetric segregation of fatedeterminants, such as Numb. Here, we show that an intermediate filament protein, transitin, colocalizes with Numb in the cell cortex of mitotic neuroepithelial cells, and that transitin anchors Numb via a physical interaction. Detailed immunohistological and time-lapse analyses reveal that basal Numb-transitin complexes shift laterally during mitosis, allowing asymmetric segregation of Numb-transitin to one of the daughter cells, even when the cell cleavage plane is perpendicular to the ventricular surface. In addition, RNA interference (RNAi) knockdown of the transitin gene reveals its involvement in neurogenesis. These results indicate that transitin has important roles in determining the intracellular localization of Numb, which regulates neurogenesis in the developing nervous system of avian embryos.

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“…In a way similar to that of nestin in mammalian embryos, transitin expression is temporally and developmentally regulated in avian myogenic and neurogenic cells (Chabot and Vincent, 1990;Cossette and Vincent, 1991;Kelly et al, 1995). The characterization of the chicken transitin gene revealed a strong relationship to the nestin IF class (Napier et al, 1999) but the C-terminal domain of transitin differs from nestin and contains a unique leucin zipper-like heptad repeat motif (HR domain) unrelated to the repeat motif found in nestin tail domain (Yuan et al, 1997;Napier et al, 1999). Nonetheless, the avian transitin and its splicing variant paranemin (Hemken et al, 1997) are orthologs of the mammalian nestin gene family (Guérette et al, 2007).…”

Section: Introductionmentioning

confidence: 99%

Transitin is required for the differentiation of avian QM7 myoblasts into myotubes

Jalouli

Lapierre

Guérette

et al. 2010

Developmental Dynamics

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*Transitin is a nestin-like intermediate filament protein co-expressed with vimentin in the precursor cells of the myogenic and neurogenic lineages of the avian embryo. To understand its role in myogenesis, stable cell lines expressing transitin-targeted siRNAs were derived from the quail muscle cell line QM7. When cells were cultured in differentiation medium, we found that transitin knockdown prevented myoblast fusion and myotube formation. MyoD mRNA could be detected in transitin siRNA-transfected cells, but upregulation of myogenin and desmin expression was impaired compared to control cells. In addition, transitin siRNA cells maintain high levels of Pax7 expression suggesting that QM7 myoblasts into which transitin expression has been attenuated display a muscle progenitor cell phenotype (Pax7). These observations indicate that transitin plays an important role in the initiation of the myogenic program in avian muscle progenitor cells in acting downstream of MyoD and upstream of myogenin during the lineage progression. V C

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Molecular Cloning of a New Intermediate Filament Protein Expressed by Radial Glia and Demonstration of Alternative Splicing in a Novel Heptad Repeat Region Located in the Carboxy-Terminal Tail Domain

Cited by 27 publications

References 40 publications

Elevated expression of Nkx‐2.5 in developing myocardial conduction cells

Elevated expression of Nkx‐2.5 in developing myocardial conduction cells

Transitin, a nestin-like intermediate filament protein, mediates cortical localization and the lateral transport of Numb in mitotic avian neuroepithelial cells

Transitin is required for the differentiation of avian QM7 myoblasts into myotubes

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