A novel 43-kDa glycoprotein is detected in the nucleus of mammalian cells by autoantibodies from dogs with autoimmune disorders

Soulard, Michel; Barque, Jean-Philippe; Valle, Véronique Della; Hernandez‐Verdun, Danièle; Masson, Claude; Danon, F; Larsen, Christian‐Jacques

doi:10.1016/0014-4827(91)90538-6

Cited by 32 publications

(32 citation statements)

References 37 publications

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“…hnRNP-C like protein, also called estrogen-response element binding protein (ERE-BP), was identified as a competitor of ER for ERE and can cause estrogen unresponsiveness (Chen et al, 2005). A previous work also showed that there is an association between hnRNP-G and hnRNP-C as shown by co-immunoprecipitation experiments (Choi et al, 1986;Soulard et al, 1991). Both testosterone (Sheflin and Spaulding, 2000) and estrogen (Arao et al, 2002) can regulate the expression of hnRNP-D. We found that some of the hormone response elements and putative hnRNP-A/B consensus binding sites are located close to each other in GnRH1 upstream (Fig.…”

Section: Relationship Between the Hnrnp Family And Hormonesmentioning

confidence: 99%

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Zhao

Korzan

Chen

et al. 2008

Molecular and Cellular Neuroscience

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Gonadotropin-releasing hormone 1 (GnRH1) causes the release of gonadotropins from the pituitary to control reproduction. Here we report that two heterogeneous nuclear ribonucleoproteins (hnRNP-A/B and hnRNP-G) bind to the GnRH-I upstream promoter region in a cichlid fish Astatotilapia burtoni. We identified these binding proteins using a newly developed homology based method of mass spectrometric peptide mapping. We show that both hnRNP-A/B and hnRNP-G colocalize with GnRH1 in the pre-optic area of the hypothalamus in the brain. We also demonstrated that these ribonucleoproteins exhibit similar binding capacity in vivo, using immortalized mouse GT1-7 cells where overexpression of either hnRNP-A/B or hnRNP-G significantly down-regulates GnRH1 mRNA levels in GT1-7 cells, suggesting that both act as repressors in GnRH1 transcriptional regulation.

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Section: Relationship Between the Hnrnp Family And Hormonesmentioning

confidence: 99%

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Zhao

Korzan

Chen

et al. 2008

Molecular and Cellular Neuroscience

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“…It is composed of 391 amino acid residues encompassing the RNA binding domain (amino acids 10-88) at the NH 2 terminus of the protein (11). This structural feature suggests the physical association of hnRNP G with RNA, which may be required for its role in RNA processing and metabolism (1,11,13). hnRNP G is detected primarily in the nuclei of mammalian cells and localized on lampbrush chromosomes of amphibian oocytes, supporting its association with nascent RNA transcripts as part of the transcriptional complexes (11).…”

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confidence: 99%

Heterogeneous Nuclear Ribonucleoprotein G Shows Tumor Suppressive Effect against Oral Squamous Cell Carcinoma Cells

Shin¹,

Kang²,

Kim³

et al. 2006

Clinical Cancer Research

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Purpose: Heterogeneous nuclear ribonucleoproteins (hnRNP) are nucleic acid binding proteins involved in RNA processing.We found that hnRNP G is expressed in normal human oral epithelial cells while frequently not found in the cells derived from human oral squamous cell carcinomas (HOSCC). The current study was designed to test the hypothesis that hnRNP G is a tumor suppressor. Experimental Design: We investigated the expression levels of hnRNP G protein in normal, precancerous, and malignant oral tissues by in situ immunohistochemistry. In addition, wild-type or mutant hnRNP G was ectopically overexpressed in HOSCC cells and their effects on cellular replication kinetics, colonogenic efficiency, anchorage-independent growth, and in vivo tumorigenicity were determined. Results: In situ immunohistochemical staining showed robust presence of hnRNP G in the basal cell layers of normal oral epithelium but the level of its staining was markedly reduced in dysplastic or cancerous tissues. Ectopic expression of wild-type hnRNP G in cancer cells lacking hnRNP G expression or containing mutant hnRNP G resulted in severe retardation of proliferation, reduction of colonogenic efficiency, loss of anchorage-independent growth, and reduction of in vivo tumorigenicity in immunocompromised mice. In addition, hnRNP G overexpression led to upregulation of the expression of TXNIP, a cell cycle inhibitory gene, and significantly reduced the expression of the genes that promote cellular proliferation, such as EGR1, JUND, JUNB, FOS, FOSL1, ROS, and KIT. Conclusions: These results indicate that hnRNP G is a tumor suppressor against HOSCC but its mechanisms of action remain to be further investigated.Heterogeneous nuclear ribonucleoproteins (hnRNP) constitute a large family of nucleic acid-binding proteins with more than 30 different members. hnRNPs were first described as chromatin-associated RNA binding proteins with the major role in RNA processing (1). However, recent studies showed that the biological functions of hnRNPs are extremely diverse and include RNA turnover, telomere biogenesis, oncogenesis, and spermatogenesis (2). For example, hnRNP D (AUF1) regulates the turnover rate of a-globin mRNA by associating with the mRNA stability complex (3). hnRNP types D, A1, and C1/C2 interact with human telomerase holoenzyme (4 -6) and are involved in telomere elongation (7). Furthermore, hnRNP B1 is recognized as a biomarker for early detection of lung cancer (8). The hnRNP types A1 and E2 are overexpressed during leukemogenesis and affect the proliferation, survival, and differentiation of normal and leukemic cells (9). hnRNP G, encoded by the RBMX locus found in chromosome X, plays an important role in spermatogenesis along with the RBMY gene product and hnRNP G-T, which interact with Tra2h, an activator of pre-mRNA splicing in spermatocytes (10). Besides its prescribed function in RNA splicing and spermatogenesis, hnRNP G is one of the least characterized protein among the members of hnRNPs for its biological functions.hnRNP ...

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“…This idea is in good agreement with the recent demonstration that hnRNP G retains its role in splice site selection in absence of its RRM. 21 Together, these data favour a model in which the RRM and the C-ter RBD exhibit distinct SAM68, YT521-B, SAFB and Tra2β, were previously shown to interact with hnRNP G. 17,21,35 Whether some of these factors are implicated in recruiting hnRNP G to nascent transcripts, perhaps as part of a preassembled complex, is not known, however.…”

Section: Discussionmentioning

confidence: 61%

Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA binding and targeting nascent transcripts

Kanhoush

Beenders

Perrin

et al. 2010

Nucleus

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A novel 43-kDa glycoprotein is detected in the nucleus of mammalian cells by autoantibodies from dogs with autoimmune disorders

Cited by 32 publications

References 37 publications

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Heterogeneous nuclear ribonucleoprotein A/B and G inhibits the transcription of gonadotropin-releasing-hormone 1

Heterogeneous Nuclear Ribonucleoprotein G Shows Tumor Suppressive Effect against Oral Squamous Cell Carcinoma Cells

Novel domains in the hnRNP G/RBMX protein with distinct roles in RNA binding and targeting nascent transcripts

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