Elevated levels of a specific class of nuclear phosphoproteins in cells transformed with v-ras and v-mos oncogenes and by cotransfection with c-myc and polyoma middle T genes.

Giancotti, Vincenzo; Pani, B.; D’Andrea, Paola; Berlingieri, Maria Teresa; Fiore, Pier Paolo Di; Vecchio, Giancarlo; Philp, Robin; Crane‐Robinson, Colyn; Nicolas, Robert H.

doi:10.1002/j.1460-2075.1987.tb02461.x

Cited by 153 publications

(136 citation statements)

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“…Indeed, increased HMGA levels correlate with the appearance of a malignant phenotype in rat thyroid cells and in experimental thyroid and skin tumours. [7][8][9] HMGA1 levels are high in human thyroid, 10,11 colon, [12][13][14] prostate, 15 pancreas, 16 cervix, 17 ovary 18 and breast 19 carcinomas. We had previously demonstrated that overexpression of HMGA proteins is required for cell transformation, since the blockage of their synthesis prevents tumorigenic transformation of rat thyroid cells by murine transforming retroviruses.…”

Section: Introductionmentioning

confidence: 99%

High Mobility Group A1 (HMGA1) proteins interact with p53 and inhibit its apoptotic activity

et al. 2005

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HMGA gene overexpression and rearrangements are frequent in several tumours, but their oncogenic function is still unclear. Here we report of a physical and functional interaction between High Mobility Group A1 (HMGA1) protein and p53 oncosuppressor. We found that HMGA1 binds p53 in vitro and in vivo, and both proteins are present in the same complexes bound to the Bax gene promoter. HMGA1 interferes with the p53-mediated transcription of p53 effectors Bax and p21 waf1 while cooperates with p53 in the transcriptional activation of the p53 inhibitor mdm2. This transcriptional modulation is associated with a reduced p53-dependent apoptosis in cells expressing exogenous HMGA1 and p53, or in cells expressing endogenously the proteins and in which p53 was activated by UV-irradiation. Furthermore, antisense inhibition of HMGA1b expression dramatically increases the UV-induced p53-mediated apoptosis. These data define a new physical and functional interaction between HMGA1 and p53 that modulates transcription of p53 target genes and inhibits apoptosis.

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Section: Introductionmentioning

confidence: 99%

High Mobility Group A1 (HMGA1) proteins interact with p53 and inhibit its apoptotic activity

et al. 2005

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“…Indeed, elevated expression of HMGI proteins correlates with the appearance of a malignant phenotype in rat thyroid transformed cells and in thyroid and skin experimental tumours (Giancotti et al, 1985(Giancotti et al, , 1987(Giancotti et al, , 1989. Similarly, HMGI(Y) protein levels are high in such human carcinomas as thyroid (Chiappetta et al, 1995(Chiappetta et al, , 1998, colon Abe et al, 1999;Chiappetta et al, 2001), prostate (Tamimi et al, 1993), pancreas (Abe et al, 2000) and cervix (Bandiera et al, 1998), but not in their normal counterparts.…”

Section: Introductionmentioning

confidence: 99%

High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth

et al. 2001

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The HMGI proteins (HMGI, HMGY and HMGI-C) have an important role in the chromatin organization and interact with di erent transcriptional factors. The HMGI genes are expressed at very low levels in normal adult tissues, whereas they are very abundant during embryonic development and in several experimental and human tumours. In order to isolate proteins interacting with the HMGI(Y) proteins, a yeast two-hybrid screening was performed using the HMGI(Y) protein as bait. This analysis led to the isolation of homeodomaininteracting protein kinase-2 (HIPK2), a serine/threonine nuclear kinase. HIPK2 co-immunoprecipitates with the HMGI(Y) protein in 293T cells. The interaction between HIPK2 and HMGI(Y) occurs through the PEST domain of HIPK2 and it is direct because in vitro translated HIPK2 binds HMGI(Y). We also show that HIPK2 is able to phosphorylate the HMGI(Y) protein by an in vitro kinase assay. In order to understand a possible role of HIPK2 gene in cell growth we performed a colony assay which showed an impressive HIPK2 inhibitory e ect on normal thyroid cells. Flow cytometric analysis would indicate the block of cell growth at the G2/M phase of the cell cycle. Since normal thyroid cells do not express detectable HMGI(Y) protein levels, we assume that the HIPK2 inhibitory e ect is independent from the interaction with the HMGI(Y) protein. Oncogene (2001) 20, 6132 ± 6141.

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“…HMGI-C and HMGI(Y) are members of the HMGI family of "highmobility group" (HMG) proteins. They act as architectural transcription factors and are commonly expressed in embryonal cells Hirning-Folz et al, 1998), in transformed cells with a malignant phenotype Bussemakers et al, 1991;Giancotti et al, 1987;1989;Ram et al, 1993), and in a variety of human cancers (Bandiera et al, 1998;Chiappetta et al, 1995;1998;Fedele et al, 1996;Rogalla et al, 1997;Rommel et al, 1997;Tamimi et al, 1993). HMGI-C and HMGI(Y) genes are located at 12q15 and 6p21 (Friedmann et al, 1993), respectively.…”

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HMGI-C and HMGI(Y) Immunoreactivity Correlates with Cytogenetic Abnormalities in Lipomas, Pulmonary Chondroid Hamartomas, Endometrial Polyps, and Uterine Leiomyomas and is Compatible with Rearrangement of the HMGI-C and HMGI(Y) Genes

Tallini

Vanni

Manfioletti

et al. 2000

Laboratory Investigation

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SUMMARY:High-mobility group (HMG) proteins are nonhistone nuclear proteins that play an important role in the regulation of chromatin structure and function. HMGI-C and HMGI(Y) are members of the HMGI family of HMG proteins, and their expression in adult tissues generally correlates with malignant tumor phenotypes. However, HMGI-C and HMGI(Y) dysregulation as a result of specific rearrangements involving 12q15 and 6p21, the respective chromosomal sites in which the HMGI-C and HMGI(Y) genes are located, is also identified in a variety of common benign mesenchymal tumors, such as lipomas and uterine leiomyomata. The general prevalence of HMGI-C and HMGI(Y) protein expression and its correlation with chromosomal alterations in these benign tumors are unknown. We analyzed 95 human tumors (20 lipomas, 21 pulmonary chondroid hamartomas, 26 uterine leiomyomata, and 28 endometrial polyps) representing a selection of the benign lesions in which karyotypic alterations involving the chromosomal regions 12q15 and 6p21 are frequently detected. All cases were successfully karyotyped and some of them analyzed by fluorescent in situ hybridization with probes spanning the HMGI-C and HMGI(Y) genes. The results of this study demonstrate that expression of HMGI-C or HMGI(Y) is a common occurrence in lipomas, pulmonary chondroid hamartomas, leiomyomata, and endometrial polyps; that it correlates with 12q15 and 6p21 chromosomal alterations (p Ͻ 0.001); and that it is compatible with rearrangement of the HMGI-C and HMGI(Y) genes. The expression pattern and cellular localization of the immunoreactivity support the view that in biphasic lesions composed of a mixture of both stromal and epithelial cells, such as pulmonary chondroid hamartoma and endometrial polyps, the mesenchymal component is the site of the HMGI genetic alterations. (Lab Invest 2000, 80:359-369).

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Elevated levels of a specific class of nuclear phosphoproteins in cells transformed with v-ras and v-mos oncogenes and by cotransfection with c-myc and polyoma middle T genes.

Cited by 153 publications

References 23 publications

High Mobility Group A1 (HMGA1) proteins interact with p53 and inhibit its apoptotic activity

High Mobility Group A1 (HMGA1) proteins interact with p53 and inhibit its apoptotic activity

High mobility group I (Y) proteins bind HIPK2, a serine-threonine kinase protein which inhibits cell growth

HMGI-C and HMGI(Y) Immunoreactivity Correlates with Cytogenetic Abnormalities in Lipomas, Pulmonary Chondroid Hamartomas, Endometrial Polyps, and Uterine Leiomyomas and is Compatible with Rearrangement of the HMGI-C and HMGI(Y) Genes

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