Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens are encoded by separate genes.

Itoh, Kazuko; Itoh, Yasuhiko; Frank, Mark Barton

doi:10.1172/jci114968

Cited by 175 publications

(67 citation statements)

References 64 publications

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“…However, it is possible that 52-kd RolSS-A protein is not precipitable under these conditions. Although it is also possible that 52-kd RolSS-A protein was not readily labeled, this possibility seems remote because the 52-kd RolSS-A contains methionine (13).…”

Section: Discussionmentioning

confidence: 99%

Clinical Significance of Antibodies to Native or Denatured 60‐kd or 52‐kd Ro/SS‐A Proteins in Sjögren's Syndrome

Tsuzaka

Fujii

Akizuki

et al. 1994

Arthritis & Rheumatism

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Objective. To evaluate the clinical significance of antibodies to native or denatured (anti‐n or anti‐d) 60‐or 52‐kd Ro/SS‐A proteins (60K or 52K) in Sjögren's syndrome (SS). Methods. The presence of antibodies to denatured and native Ro/SS‐A proteins was determined by immunoblotting and immunoprecipitation, respectively. Salivary gland dysfunction was evaluated by salivary function scintigraphy. Results. The incidence of anti—d‐60K without anti—d‐52K was lower among patients with systemic lupus erythematosus with SS (SLE/SS) and among those with primary SS, compared with patients who had SLE without SS, whereas anti—d‐52K without anti—d‐60K was more common in SLE/SS patients and primary SS patients than in SLE patients without SS. All of the patients with anti—Ro/SS‐A had anti—n‐60K. Serologic abnormalities and salivary gland dysfunction were associated with anti—n‐60K in SS, whereas Hashimoto's thyroiditis in SS was related to anti—d‐60K. anti—d‐52K was not associated with any extraglandular or glandular symptoms in SS. Conclusion. The data indicate that anti—n‐60K, which appears to recognize conformational epitopes, is associated with clinical features of SS characterized by glandular dysfunction.

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Section: Discussionmentioning

confidence: 99%

Clinical Significance of Antibodies to Native or Denatured 60‐kd or 52‐kd Ro/SS‐A Proteins in Sjögren's Syndrome

Tsuzaka

Fujii

Akizuki

et al. 1994

Arthritis & Rheumatism

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“…Further investigations will be undertaken to characterize the other members of the enterophilin family. Accordingly, it is interesting to note that multiple transcripts have already been reported for other members of the B30.2 family such as Ro/SS-A, RoRet, or MID1 (30,(63)(64)(65). For the latter gene, other mutations responsible for Opitz syndrome were recently described, and authors reported the presence of at least six isoforms of mRNA (66).…”

Section: Fig 5 Expression Of Enterophilin-1 Along the Small Intestimentioning

confidence: 93%

Enterophilins, a New Family of Leucine Zipper Proteins Bearing a B30.2 Domain and Associated with Enterocyte Differentiation

Gassama‐Diagne

Hullin-Matsuda

et al. 2001

Journal of Biological Chemistry

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Enterocyte terminal differentiation occurs at the crypt-villus junction through the transcriptional activation of cell-specific genes, many of which code for proteins of the brush border membrane such as intestinal alkaline phosphatase, sucrase-isomaltase, or the microvillar structural protein villin. Several studies have shown that this sharp increase in specific mRNA levels is intimately associated with arrest of cell proliferation. We isolated several clones from a guinea pig intestine cDNA library. They encode new proteins characterized by an original structure associating a carboxyl-terminal B30.2/RFP-like domain and a long leucine zipper at the amino terminus. The first member of this novel gene family codes for a 65-kDa protein termed enterophilin-1, which is specifically expressed in enterocytes before their final differentiation. Enterophilin-1 is the most abundant in the small intestine but is still present in significant amounts in colonic enterocytes. In Caco-2 cells, a similar 65-kDa protein was recognized by a specific anti-enterophilin-1 antibody, and its expression was positively correlated with cell differentiation status. In addition, transfection of HT-29 cells with enterophilin-1 full-length cDNA slightly inhibited cell growth and promoted an increase in alkaline phosphatase activity. Taken together, these data identify enterophilins as a new family of proteins associated with enterocyte differentiation.The self-renewing small intestinal epithelium represents an attractive and valuable system to study various processes occurring during cell life such as proliferation, differentiation, or apoptosis. Proliferation is limited to the crypts of Lieberkü hn, where multipotent stem cells achieve continuous renewal of four main epithelial lineages. At the top of the crypt, cells lose their proliferative ability and complete differentiation during a highly organized migration along the crypt-villus axis. Enterocytes, mucus-producing goblet cells, and enteroendocrine cells evolve during a vertical migration to the villus apex (1-3). This process requires 4 to 5 days and results in well-differentiated cells that are finally released into the intestinal lumen upon programmed cell death. In contrast, Paneth cells undergo terminal differentiation while moving down to the base of the crypt (4 -8). The differentiation process and the function of the epithelium also vary along the horizontal axis (from proximal to distal intestine), and in both cases, functional differences reflect various patterns of gene expression as well as the nature of the epithelial cell type (7).How these various events are regulated at the genomic level and the intracellular signaling pathways involved in this differentiation process are still poorly understood. Recently identified genes were found to be necessary either to maintain the proliferative status of stem cells (Tcf-4) (9) or to direct the differentiation process (homeobox transcription factors cdx1 and cdx2) (10 -12). Most of the previous studies were performed with entero...

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“…The 52kD polypeptide is alternatively spliced, yielding an isoform that lacks aminoacids 169-245 of the full-length protein (Chan et al 1995). Although their function is not yet known, both the 60 and the 52 kD Ro have zinc finger motifs capable of binding DNA and regulating gene expression (Chan et al 1991, Itoh et al 1991. The anti-La/SSB is another auto-antibody found in the serum of mothers and affected children.…”

Section: The Neonatal Lupus Syndromementioning

confidence: 99%

Neonatal lupus syndrome: the heart as a target of the immune system

Garcia

Carvalho

2000

An. Acad. Bras. Ciênc.

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Neonatal lupus erythematosus (NLE) is an auto-immune disease related to systemic lupus erythematosus (SLE). Unlike SLE it is not a spontaneous syndrome but rather an acquired one. In NLE the most common disease manifestations are a transient cutaneous lesion and cardiac conduction disturbances. The cutaneous lesions and other non-cardiac manifestations of NLE are transient and disappear about six months after birth, at the time when maternal antibodies disappear from the neonatal circulation. This fact suggests that maternal antibodies may cross the placenta leading to an inflamatory reaction in the fetal tissues. NLE is the principal cause of atria-ventricular block, when it is not associated with congenital birth defects. All the clinical studies to date correlate the heart block in NLE with the presence of certain types of circulating maternal antibodies, against the Ro/SSA nuclear proteins, in the serum of the newborn. In this paper we discuss animal models that have been developed by our and others groups to study the participation of the anti-Ro/SSA antibodies in the pathogenesis of the cardiac conduction blockades that occur in NLE.

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Protein heterogeneity in the human Ro/SSA ribonucleoproteins. The 52- and 60-kD Ro/SSA autoantigens are encoded by separate genes.

Cited by 175 publications

References 64 publications

Clinical Significance of Antibodies to Native or Denatured 60‐kd or 52‐kd Ro/SS‐A Proteins in Sjögren's Syndrome

Clinical Significance of Antibodies to Native or Denatured 60‐kd or 52‐kd Ro/SS‐A Proteins in Sjögren's Syndrome

Enterophilins, a New Family of Leucine Zipper Proteins Bearing a B30.2 Domain and Associated with Enterocyte Differentiation

Neonatal lupus syndrome: the heart as a target of the immune system

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