Novel autoimmune phenomena induced in vivo by a new DNA binding protein Nuc: a study on MRL/n mice

Kanai, Yoshiyuki; Takeda, Osamu; Kanai, Yukiko; Miura, Katsukiyo; Kurosawa, Yoshikazu

doi:10.1016/0165-2478(93)90168-2

Cited by 26 publications

(10 citation statements)

References 18 publications

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“…Nucleobindin was originally cloned as a nuclear antigen in a murine model of systemic lupus erythematosus [12,20]. Interestingly, it has a DNA-binding motif, leucine zipper, a signal peptide sequence, and an EF hand motif for Ca 2÷ binding activity [12,20~2].…”

Section: Discussionmentioning

confidence: 99%

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

et al. 1995

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The heterotrimeric G protein, G~i2, transduces signals from seven membrane spanning receptors to effectors such as adenylyl cyclase and ion channels. The purpose of this study was to identify these or other cellular proteins that interact with G,d2 by use of the yeast two-hybrid system. A human B cell cDNA library was screened by this system using full length Gin2. Four positive colonies were obtained. Two of the four were identified as nucleobindin, a calcium binding protein and a putative antigen to which anti-nuclear antibodies are generated in mice with a disorder that resembles systemic lupus erythematosus. Nucleobindin has a leucinc zipper, EF hands, and a signal peptide sequence and is thought to localize to the nucleus as well as being secreted. The specificity of intehraction between G~2 and nucleobindin was confirmed by an in vitro binding assay using recombinant proteins. Transfeetion of Gai2 and nucleobindin in COS cells increased G~i2 expression relative to cells transfected with Goi2 and mock vector. Our results indicate that the yeast two-hybrid system provides a means to identify novel proteins that interact with G,~ proteins. Nucleobindin appears to represent one of those proteins.

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Section: Discussionmentioning

confidence: 99%

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

et al. 1995

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“…In previous study, Calnuc was isolated from the sera of mice prone to the autoimmune disorder systemic lupus erythematosis (SLE), as well as the growth media of a lymphocyte cell line established from these mice (24,25). Kubota and coworkers found that Calnuc might enhance anti-DNA antibody production when added to cultures of autoimmune MRL/lpr mouse spleen cells, and normal mice injected with Calnuc developed thymic apoptosis and many of the symptoms of SLE (26)(27)(28). It was assumed that overexpression and secretion of the Calnuc protein might be Table III.…”

Section: Discussionmentioning

confidence: 99%

Autoantibodies to Ca2+ binding protein Calnuc is a potential marker in colon cancer detection

Chen

Lin²,

Qiu³

et al. 2007

Int J Oncol

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“…Deliberate immunization of mice with various DNA-binding proteins of exogenous or endogenous origin along with CFA leads to the production of anti-DNA autoantibodies, particularly in lupus-prone genetic backgrounds (63)(64)(65). Even methylated BSA carrier-specific T cells could help in the production of anti-DNA autoantibodies when B/W lupus mice were immunized with methylated BSA-DNA complex (65).…”

Section: Introductionmentioning

confidence: 99%

Structure and specificity of T cell receptors expressed by potentially pathogenic anti-DNA autoantibody-inducing T cells in human lupus.

Desai-Mehta¹,

Mao²,

Rajagopalan³

et al. 1995

J. Clin. Invest.

161

160

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The production of potentially pathogenic anti-DNA autoantibodies in SLE is driven by special, autoimmune T helper (Th) cells. Herein, we sequenced the T cell receptor (TCR) a and P chain genes expressed by 42 autoimmune Th lines from lupus patients that were mostly CD4+ and represented the strongest inducers of such autoantibodies. These autoinmune TCRs displayed a recurrent motif of highly charged residues in their CDR3 loops that were contributed by Nnucleotide additions and also positioned there by the recombination process. Furthermore, Th lines from four of the five patients showed a marked increase in the usage of the Va8 gene family. Several independent Th lines expressed identical TCR a and/or ,B chain sequences indicating again antigenic selection. 10 of these Th lines could be tested further for antigenic specificity. 4 of the 10 pathogenic anti-DNA autoantibody-inducing Th lines responded to the nonhistone chromosomal protein HMG and two responded to nucleosomal histone proteins; all presented by HLA-DR molecules. Another Th line responded to purified DNA more than nucleosomes. Thus, these autoimmune Th cells of lupus patients respond to charged epitopes in various DNA-binding nucleoproteins that are probably processed and presented by the anti-DNA B cells they selectively help. (J. Clin. Invest. 1995. 95:531-541.)

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Novel autoimmune phenomena induced in vivo by a new DNA binding protein Nuc: a study on MRL/n mice

Cited by 26 publications

References 18 publications

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

Autoantibodies to Ca2+ binding protein Calnuc is a potential marker in colon cancer detection

Structure and specificity of T cell receptors expressed by potentially pathogenic anti-DNA autoantibody-inducing T cells in human lupus.

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Novel autoimmune phenomena induced in vivo by a new DNA binding protein Nuc: a study on MRL/n mice

Cited by 26 publications

References 18 publications

Interaction of the protein nucleobindin with Gαi2, as revealed by the yeast two‐hybrid system

Interaction of the protein nucleobindin with Gαi2, as revealed by the yeast two‐hybrid system

Autoantibodies to Ca2+ binding protein Calnuc is a potential marker in colon cancer detection

Structure and specificity of T cell receptors expressed by potentially pathogenic anti-DNA autoantibody-inducing T cells in human lupus.

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Product

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Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system

Interaction of the protein nucleobindin with G_αi2, as revealed by the yeast two‐hybrid system