High prevalence of autoantibodies to a nuclear antigen in primary biliary cirrhosis: Molecular cloning of a major antgenic domain

Szostecki, Carin; Guldner, H. H.; Netter, Hans; Will, H.

doi:10.1016/0168-8278(90)91571-d

Cited by 2 publications

(4 citation statements)

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“…As these images are also observed in spontaneously apoptotic NB4 cells (ref. 27 and data not shown), we investigated the earlier effects of arsenic (at the therapeutic concentration of 10 Ϫ6 M) on the localization of the NB antigens [PML, Sp100 (12,13), and NDP52 (17)] as well as PML͞ RAR␣. As 2 O 3 profoundly affected the immunofluorescence pattern obtained with an anti-PML antisera that detects both PML and PML͞RAR␣.…”

Section: Resultsmentioning

confidence: 99%

“…For example, arsenic recruits Sp100 onto NBs but fails to degrade this protein. Should Sp100 exert some functions out of NB (such as transcriptional activation (12,13)), arsenic-induced Sp100 sequestration would then abolish it.…”

Section: Discussionmentioning

confidence: 99%

“…These structures (which belong to the nuclear matrix; ref. 10) were previously identified using autoantibodies from patients with primary biliary cirrhosis (11) that recognize a proposed transcription factor, Sp100 (12,13). The three NB antigens identified to date, Sp100, PML, and NDP52, are all target genes of interferons (IFNs; refs.…”

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confidence: 99%

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Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia

Zhu

Koken²,

Quignon³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

401

323

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Acute promyelocytic leukemia (APL) is associated with the t(15;17) translocation, which generates a PML͞RAR␣ fusion protein between PML, a growth suppressor localized on nuclear matrix-associated bodies, and RAR␣, a nuclear receptor for retinoic acid (RA). PML͞RAR␣ was proposed to block myeloid differentiation through inhibition of nuclear receptor response, as does a dominant negative RAR␣ mutant. In addition, in APL cells, PML͞RAR␣ displaces PML and other nuclear body (NB) antigens onto nuclear microspeckles, likely resulting in the loss of PML and͞or NB functions. RA leads to clinical remissions through induction of terminal differentiation, for which the respective contributions of RAR␣ (or PML͞RAR␣) activation, PML͞ RAR␣ degradation, and restoration of NB antigens localization are poorly determined. Arsenic trioxide also leads to remissions in APL patients, presumably through induction of apoptosis. We demonstrate that in non-APL cells, arsenic recruits the nucleoplasmic form of several NB antigens onto NB, but induces the degradation of PML only, identifying a powerful tool to approach NB function. In APL cells, arsenic targets PML and PML͞RAR␣ onto NB and induces their degradation. Thus, RA and arsenic target RAR␣ and PML, respectively, but both induce the degradation of the PML͞ RAR␣ fusion protein, which should contribute to their therapeutic effects. The difference in the cellular events triggered by these two agents likely stems from RA-induced transcriptional activation and arsenic effects on NB proteins.

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Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia

Zhu

Koken²,

Quignon³

et al. 1997

Proc. Natl. Acad. Sci. U.S.A.

401

323

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“…In this study, we identify and functionally characterize the interaction between ETS1 and SP100. SP100 was first identified as a nuclear autoantigen in patients with the autoimmune disease Primary Biliary Cirrhosis (Szostecki et al, 1990, and its mRNA and protein is potently induced by interferon (IFN) . SP100 is a constituent member of the nuclear body (NB), a subnuclear organelle, also referred to as Kr-bodies, nuclear domain 10 (ND10) or PML oncogenic domains (PODs) (Lamond and Earnshaw, 1998;Seeler et al, 1998;Seeler and Dejean, 1999).…”

Section: Introductionmentioning

confidence: 99%

SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion

Yordy

Sementchenko

et al. 2004

Oncogene

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The ETS1 transcription factor is a member of the Ets family of conserved sequence-specific DNA-binding proteins. ETS1 has been shown to play important roles in various cellular processes such as proliferation, differentiation, lymphoid development, motility, invasion and angiogenesis. These diverse roles of ETS1 are likely to be dependent on specific protein interactions. To identify proteins that interact with ETS1, a yeast two-hybrid screen was conducted. Here, we describe the functional interaction between SP100 and ETS1. SP100 protein interacts with ETS1 both in vitro and in vivo. SP100 is localized to nuclear bodies and ETS1 expression alters the nuclear body morphology in living cells. SP100 negatively modulates ETS1 transcriptional activation of the MMP1 and uPA promoters in a dose-dependent manner, decreases the expression of these endogenous genes, and reduces ETS1 DNA binding. Expression of SP100 inhibits the invasion of breast cancer cells and is induced by Interferon-a, which has been shown to inhibit the invasion of cancer cells. These data demonstrate that SP100 modulates ETS1-dependent biological processes.

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High prevalence of autoantibodies to a nuclear antigen in primary biliary cirrhosis: Molecular cloning of a major antgenic domain

Cited by 2 publications

References 0 publications

Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia

Arsenic-induced PML targeting onto nuclear bodies: Implications for the treatment of acute promyelocytic leukemia

SP100 expression modulates ETS1 transcriptional activity and inhibits cell invasion

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