Differential expression and subcellular distribution of dystrophin Dp71 isoforms during differentiation process

Marquez, Flor; Cisneros, Bulmaro; García, Francisco Javier Sánchez; Ceja, Víctor; Velázquez, Francisco; Depardón, Francisco; Cervantes, Lourdes; Rendón, Álvaro; Mornet, Dominique; Rosas-Vargas, Haydeé; Mustre, M; Montañéz, Cecilia

doi:10.1016/s0306-4522(03)00063-0

Cited by 51 publications

(68 citation statements)

References 46 publications

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“…1A) whereas the staining of Dp71d accumulated in the nucleus and to lesser extension in the cytoplasm (Fig. 1B), as previously reported [34].In the antisense-Dp71 cells, cytoplasmic staining of Dp71f and the nuclear signal of Dp71d were dramatically reduced (Figs. 1A and B).…”

Section: Antisense-dp71 Cells Show Decreased Dp71 Protein Expressionsupporting

confidence: 86%

“…localizes in the cell body and neurites while Dp71d accumulates mainly in the nucleus [34]. These results suggest that each Dp71 variant may perform specific tasks in neuronal differentiation.…”

Section: ------------------------------------------------------------mentioning

confidence: 78%

“…A 70-to 75-kDa dystrophin protein (designed Dp71) has a unique seven residues Nterminus fused to the cysteine-rich and C-terminal domains and is the most abundant dystrophin in a wide range of non-muscle tissues [5,17,28].In addition, Dp71 transcripts are alternatively spliced for exons 71-74 and 78 in several tissues; then multiple Dp71 protein products of 70-78 kDa are generated [2,3]. Recently, we determined that alternative splicing regulates the cytoplasmic or nuclear localization of Dp71 [19,34].…”

Section: Introductionmentioning

confidence: 99%

“…We have previously adopted the PC12 cell line as an in vitro neuronal model for studying Dp71 cellular function [12]. These cells express two Dp71 splicing isoforms; both of them spliced out for exon 71 and with exon 78 either present (Dp71d) or spliced out (Dp71f) [34]. Both Dp71 protein isoforms are upregulated during NGF-induced PC12 neuronal differentiation, Dp71f increases 9fold in total extracts, while Dp71d augments up to 7-fold in nuclear extracts; additionally, Dp71 isoforms showed distinct subcellular distributions from each other: Dp71f isoform Table 1 Antibodies …”

Section: Introductionmentioning

confidence: 99%

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Dystrophin Dp71 is required for neurite outgrowth in PC12 cells

Acosta

Montañéz

Fuentes-Mera

et al. 2004

Experimental Cell Research

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:To determine the role of Dp71 in neuronal cells, we generated PC12 cell lines in which Dp71 protein levels were controlled by stable transfection with either antisense or sense constructs. Cells expressing the antisense Dp71 RNA (antisense-Dp71 cells) contained reduced amounts of the two endogenous Dp71 isoforms. Antisense-Dp71 cells exhibited a marked suppression of neurite outgrowth upon the induction with NGF or dibutyryl cyclic AMP. Early responses to NGF-induced neuronal differentiation, such as the cessation of cell division and the activation of ERK1/2 proteins, were normal in the antisense-Dp71 cells. On contrary, the induction of MAP2, a late differentiation marker, was disturbed in these cells. Additionally, the deficiency of Dp71 correlated with an altered expression of the dystrophin-associated protein complex (DAPC) members a and h dystrobrevins. Our results indicate that normal expression of Dp71 is essential for neurite outgrowth in PC12 cells and constitute the first direct evidence implicating Dp71 in a neuronal function. D 2004 Elsevier Inc. All rights reserved.

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Section: Antisense-dp71 Cells Show Decreased Dp71 Protein Expressionsupporting

confidence: 86%

Section: ------------------------------------------------------------mentioning

confidence: 78%

Section: Introductionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

See 2 more Smart Citations

Dystrophin Dp71 is required for neurite outgrowth in PC12 cells

Acosta

Montañéz

Fuentes-Mera

et al. 2004

Experimental Cell Research

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“…Previously, the presence of Dp71 and several DAPC components in the nuclei of different cell types has been described [17,19,20]. The nuclear distribution of Dp71 has been observed in cultured hippocampal neurons [35] and the PC12 cell line [36,37]. Additionally, α-dystrobrevin was found in the nuclei of the human cell line HL-60 [19] whereas β-dystrobrevin was observed in the nuclear compartment of hippocampal pyramidal neurons [17].…”

Section: Discussionmentioning

confidence: 96%

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Fuentes-Mera

Rodríguez-Muñóz

González‐Ramírez

et al. 2006

Experimental Cell Research

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, et al.. Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: members of the nuclear DAPC associate with the nuclear matrix.. Experimental Cell Research, Elsevier, 2006, 312 (16) ABSTRACT: Dystrophin is an essential component in the assembly and maintenance of the dystrophinassociated protein complex (DAPC), which includes members of the dystroglycan, syntrophin, sarcoglycan and dystrobrevin protein families. Distinctive complexes have been described in the cell membrane of different tissues and cultured cells. In this work, we report the identification and characterization of a novel DAPC present in the nuclei of HeLa cells, which contains dystrophin Dp71 as a key component. Using confocal microscopy and cell fractionation analyses, we found the presence of Dp71, β-sarcoglycan, β-dystroglycan, α-and β-syntrophin, α1-and β-dystrobrevin and nNOS in the nuclei of HeLa cells. Furthermore, we demonstrated by coimmunoprecipitation experiments that most of these proteins form a complex in the nuclear compartment. Next, we analyze the possible association of the nuclear DAPC with the nuclear matrix. We found the presence of Dp71, β-dystroglycan, nNOS, β-sarcoglycan, α/β syntrophin, α1-dystrobrevin and β-dystrobrevin in the nuclear matrix protein fractions and in situ nuclear matrix preparations from HeLa cells. Moreover, we found that Dp71, β-dystroglycan and β-dystrobrevin co-immunoprecipitated with the nuclear matrix proteins lamin B1 and actin. The association of members of the nuclear DAPC with the nuclear matrix indicates that they may work as scaffolding proteins involved in nuclear architecture.

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Dp71ab/DAPs complex composition changes during the differentiation process in PC12 cells

Romo-Yáñez

Ceja

Ilarraza-Lomeli

et al. 2007

J of Cellular Biochemistry

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PC12 cells express different Dp71 isoforms originated from alternative splicing; one of them, Dp71ab lacks exons 71 and 78. To gain insight into the function of Dp71 isoforms we identified dystrophin associated proteins (DAPs) that associate in vivo with Dp71ab during nerve growth factor (NGF) induced differentiation of PC12 cells. DAPs expression was analyzed by RT-PCR, Western blot and indirect immunofluorescence, showing the presence of each mRNA and protein corresponding to alpha-, beta-, gamma-, delta-, and epsilon-sarcoglycans as well as zeta-sarcoglycan mRNA. Western blot analysis also revealed the expression of beta-dystroglycan, alpha1-syntrophin, alpha1-, and beta-dystrobrevins. We have established that Dp71ab forms a complex with beta-dystroglycan, alpha1-syntrophin, beta-dystrobrevin, and alpha-, beta- and gamma-sarcoglycans in undifferentiated PC12 cells. In differentiated PC12 cells, the complex composition changes since Dp71ab associates only with beta-dystroglycan, alpha1-syntrophin, beta-dystrobrevin, and delta-sarcoglycan. Interestingly, neuronal nitric oxide synthase associates with the Dp71ab/DAPs complex during NGF treatment, raising the possibility that Dp71ab may be involved in signal transduction events during neuronal differentiation.

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Differential expression and subcellular distribution of dystrophin Dp71 isoforms during differentiation process

Cited by 51 publications

References 46 publications

Dystrophin Dp71 is required for neurite outgrowth in PC12 cells

Dystrophin Dp71 is required for neurite outgrowth in PC12 cells

Characterization of a novel Dp71 dystrophin-associated protein complex (DAPC) present in the nucleus of HeLa cells: Members of the nuclear DAPC associate with the nuclear matrix

Dp71ab/DAPs complex composition changes during the differentiation process in PC12 cells

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