Short‐term stability of HIV provirus levels in the peripheral blood of HIV‐infected individuals

Paul, David B.; Kuhns, Mary C.; McNamara, Anne L.; Pottage, John C.; Spear, Gregory T.

doi:10.1002/jmv.1890470317

Cited by 4 publications

(2 citation statements)

References 19 publications

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“…Its diverse localisation and function may be justified since it interacts with wide range of intra and extracellular proteins. Apart from its specific interaction with HA, it binds with numerous cellular proteins of cell surface like Kininogen, 27 Vitronectin, 26 nucleus related like TFII B, 28,29 lamin B receptor, 30 splicing factor 2 (SF2), 14 and mitochondria related like Cytochrome b2 31 and BH3 only protein Hrk. 32 In addition to several cellular proteins, HABP1 also interacts with several bacterial and viral pathogenic proteins suggesting its possible role in a process related with pathogenesis.…”

Section: Introductionmentioning

confidence: 99%

Upregulation of hyaluronan binding protein 1 (HABP1/p32/gC1qR) is associated with Cisplatin induced apoptosis

Kamal

Datta

2006

Apoptosis

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We have earlier reported that overexpression of HABP1 in fibroblast cells causes perturbed cell growth, extensive vacuolation and restricted entry to the S-phase, finally leading to apoptosis (Biochem Biophys Res Commun 2003; 300: 686-693). In the present study, we investigate the regulation of HABP1 expression in cisplatin induced apoptosis in HeLa cells. Apoptosis induced in HeLa cells at 24 h of cisplatin treatment was confirmed by nuclear fragmentation, increase in subdiploid population and the enhanced activation of ERK and upregulation of p53. In association with apoptosis induction, an upregulation of HABP1 expression was observed in HeLa cells at 18 and 24 h of cisplatin treatment. Quantification of HABP1 expression by flow cytometry confirmed a two-fold increase in total intracellular HABP1 expression at 24 h of cisplatin treatment. Under the same condition the HABP1 transcript level measured by semi quantitative RT PCR showed 2.5-fold increase ascertaining transcriptional regulation of HABP1 during cisplatin induced apoptosis. Further, in normal HeLa cells though a small amount of HABP1 can be detected in nucleus, but with apoptosis induction the protein is mainly concentrating around the nuclear periphery at 18 h of cisplatin treatment and is present both in the nucleus as well as in the cytosol at 24 h of treatment, suggesting its nuclear translocation during apoptosis. To substantiate our findings prior to the cisplatin treatment, the expression of HABP1 was reduced by small interfering RNA mediated knockdown. We observed a reduction in apoptotic cell population in cisplatin treated HeLa cells with disrupted HABP1 conferring resistance to cisplatin induced apoptosis. We report here that HABP1 upregulation in the cell is important for cisplatin induced apoptosis.

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Section: Introductionmentioning

confidence: 99%

Upregulation of hyaluronan binding protein 1 (HABP1/p32/gC1qR) is associated with Cisplatin induced apoptosis

Kamal

Datta

2006

Apoptosis

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“…HCV core deposition has indeed been reported in the skin (22) and kidney (23) of cryoglobulinemic patients. Apart from its specific interaction with C1q, it binds with several cell proteins, namely kininogen (24), vitronectin (21), nucleus-related-like TFII B (25-26), lamin B receptor (27), splicing factor 2 (28), mitochondria-related-like cytochrome b2 (29), and BH3 (30). In addition to cell proteins, C1q-R interacts with several pathogenic bacterial and viral proteins, such as adenovirus core protein (31) and HIV rev (32-33), and may thus be a part of the system which imports proteins to the cell.…”

mentioning

confidence: 99%

Role of the Receptor for the Globular Domain of C1q Protein in the Pathogenesis of Hepatitis C Virus-Related Cryoglobulin Vascular Damage

Sansonno

Tucci

Ghebrehiwet

et al. 2009

The Journal of Immunology

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Mixed cryoglobulinemia (MC) is a lymphoproliferative disorder observed in ∼10 to 15% of hepatitis C virus (HCV)-infected patients. Circulating, nonenveloped HCV core protein, which has been detected in cryoprecipitable immune complexes, interacts with immunocytes through the receptor for the globular domain of C1q protein (gC1q-R). In this study, we have evaluated circulating gC1q-R levels in chronically HCV-infected patients, with and without MC. These levels were significantly higher in MC patients than in those without MC and in healthy controls and paralleled specific mRNA expression in PBL. Soluble gC1q-R circulates as a complexed form containing both C1q and HCV core proteins. Higher serum gC1q-R levels negatively correlated with circulating concentrations of the C4d fragment. The presence of sequestered C4d in the vascular bed of skin biopsies from MC patients was indicative of in situ complement activation. In vitro studies showed that release of soluble gC1q-R is regulated by HCV core-mediated inhibition of cell proliferation. Our results indicate that up-regulation of gC1q-R expression is a distinctive feature of MC, and that dysregulated shedding of C1q-R molecules contributes to vascular cryoglobulin-induced damage via the classic complement-mediated pathway.

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The Pivotal Role of C1qR in Mixed Cryoglobulinemia

Sansonno

Dammacco

2011

HCV Infection and Cryoglobulinemia

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Short‐term stability of HIV provirus levels in the peripheral blood of HIV‐infected individuals

Cited by 4 publications

References 19 publications

Upregulation of hyaluronan binding protein 1 (HABP1/p32/gC1qR) is associated with Cisplatin induced apoptosis

Upregulation of hyaluronan binding protein 1 (HABP1/p32/gC1qR) is associated with Cisplatin induced apoptosis

Role of the Receptor for the Globular Domain of C1q Protein in the Pathogenesis of Hepatitis C Virus-Related Cryoglobulin Vascular Damage

The Pivotal Role of C1qR in Mixed Cryoglobulinemia

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