Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen.

McCauliffe, Daniel P.; Lux, F A; Lieu, Tsu-San; Sanz, Iñaki; Hanke, J H; Newkirk, Marianna M.; Bachinski, Linda L.; Itoh, Yasuhiko; Siciliano, Michael J.; Reichlin, Morris

doi:10.1172/jci114582

Cited by 165 publications

(97 citation statements)

References 54 publications

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“…The peptides were purified by HPLC, and the three main peaks isolated were processed for microsequencing (see Materials and Methods). The amino acid sequences obtained in this analysis correspond to positions 25-41, 65-71, and 287-301 and were found to be 100% identical with that of human CRT (32,33) (Table I). Amino acid sequences were compared using the GenBank database and the FASTA and PSI-BLAST programs (34,35).…”

Section: Figurementioning

confidence: 71%

“…These three proteins are well characterized. The human 48-kDa CRT gene is located on chromosome 19 (32,33), whereas the human genes encoding the 60-and 52-kDa SSA/Ro and the human 48-kDa SSB/La are located on chromosome 1 (1q31) and chromosome 2, respectively (38,39).…”

Section: Discussionmentioning

confidence: 99%

“…As endolysin C cleaves peptide bonds following lysine residues, the (K) at the beginning of the sequences of the various peptides, and at the end of some peptides, indicates that in the homologous protein sequence, these peptides are indeed adjacent to a lysine residue. The results show that p50 is homologous to human CRT (32,33). Amino acid sequences were compared using the GenBank database and the FASTA and PSI-BLAST programs (34,35).…”

Section: Discussionmentioning

confidence: 99%

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Calreticulin, a Potential Cell Surface Receptor Involved in Cell Penetration of Anti-DNA Antibodies

Seddiki

Nato

Lafaye

et al. 2001

The Journal of Immunology

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A 50-kDa protein was purified as a potential receptor, using an affinity matrix containing biotinylated F14.6 or H9.3 anti-DNA mAbs derived from autoimmune (New Zealand Black × New Zealand White)F1 mouse and membrane extracts from cells. This protein was identified as calreticulin (CRT) by microsequencing. Confocal microscopy and FACS analysis showed that CRT was present on the surface of various cells. CRT protein was recognized by a panel of anti-DNA mAbs in ELISA. The binding of F14.6 to lymphocytes and Chinese hamster ovary cells was inhibited by soluble CRT or SPA-600. Thus, the anti-DNA mAbs used in this study bound to CRT, suggesting that CRT may mediate their penetration into the cells and play an important role in lupus pathogenesis.

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Section: Figurementioning

confidence: 71%

Section: Discussionmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Calreticulin, a Potential Cell Surface Receptor Involved in Cell Penetration of Anti-DNA Antibodies

Seddiki

Nato

Lafaye

et al. 2001

The Journal of Immunology

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“…At the level of cDNA, two almost identical amino acid sequences have been reported by Deutscher et al [11] and Ben-Chetrit et al [12]. The N-terminal sequence of these proteins was completely different from a third Ro/ SS-A protein reported by Lieu et al [13] and McCauliffe et al [14]. This protein represents calreticulin [15].…”

Section: Introductionmentioning

confidence: 74%

Complete congenital heart block is associated with increased autoantibody titers against calreticulin

Orth

Dörner

Büschenfelde

et al. 1996

Eur J Clin Investigation

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Abstract. Complete congenital heart block (CCHB) is associated with anti-Ro/SS-A and anti-La/SS-B antibodies. Calreticulin, a calcium-binding, multifunctional protein of the endoplasmic reticulum with C-terminal KDEL-sequence, is not part of the Ro/SS-A ribonucleoprotein complex. In this study anti-calreticulin autoantibody responses in serum samples from 18 infants with CCHB, their mothers and in a control group of 11 antiRo/SS-A or anti-La/SS-B positive infants without heart block and their mothers were analysed. Specific enzymelinked immunosorbent assays were performed. Nine out of 18 sera with CCHB contained IgG anti-calreticulin antibodies. Four sera of those with IgG antibodies also had IgM antibodies. One serum contained anti-calreticulin IgM antibodies only. In the non-CCHB group two sera were positive for IgG and one serum was positive for IgM anti-calreticulin antibodies. Sera of healthy infants were negative both for anti-IgG and anti-IgM calreticulin antibodies. Calreticulin is involved in calcium storage and therefore anti-calreticulin antibodies might influence the development of CCHB. The new finding of IgM autoantibodies and the observed differences in antibody response in infants and mothers support the hypothesis of a fetally mediated and passively acquired autoimmune disease.

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“…p52 cDNA sequence encodes for no RNA-binding region [19,20], however, and p52 does not appear to interact directly with Ro RNAs [11,21], In erythrocytes and platelets, either a 60-kD or a 54-kD protein, but no La, was found complexed with subsets of the hY RNAs [22,23], Other proteins initially thought to be related to Ro (e.g. calreticulin) are also recognized by some anti-Ro sera [24][25][26], Two functions have been proposed for La: to act as a termination factor of RNA polymerase HI transcription, and to play a role in translation of poliovirus RNA [27][28][29], Although all major constituents of Ro RNPs have been cloned and sequenced [19,[30][31][32][33], the function(s) of these auloantigens have not been established (see Addendum). One explanation could be that individual components (protein or RNA) are inactive and that the integrity of the RNP particles is necessary for adequate function.…”

Section: Introductionmentioning

confidence: 99%

Purification of antigenically intact Ro ribonucleoproteins; biochemical and Immunological evidence that the 52-kD protein is not a Ro protein

Boire

Gendron

Monast

et al. 1995

Clinical and Experimental Immunology

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SUMMARYAnti-Ro sera immutioprecipitate Ro dboaucleoproteins (RNPs) from human cell extracts. Ro RNPs are biochemically heterogeneous particles whose functiotis are unknown and whose exact composition remains controversial. In addition to 60-kD Ro and to La proteins, a 52-kD polypeptide (p52) has been proposed to be a stable component of the Ro RNPs. To confirm the immunological studies supporting this hypothesis, we have biochemically purified Ro RNPs from HeLa cells using non-denaturing conditions. Ro RNPs segregated into three distinct populations, one of which only contained hY5 RNA {Ro''^^ RNPs). No p52 co-purified with Ro RNPs. Despite the absence of p52. purified Ro RNPs had biochemical and immunological properties identical to those of unfractionated Ro RNPs. Many anti-Ro sera only recognize p52 in immunoblots. and are said to be monospecific anti-p52, Preincubation with purified Ro""^^ RNPs (free of p52) of all human anti-Ro (including so-called monospecific anti-p52) sera abolished their capacity to immunoprecipitate Ro RNPs from unfractionated HeLa cell extracts. Conversely, preincubation of anti-Ro sera with purified p52 protein specifically inhibited recognition of p52 in immunoblots, but did not interfere with immunoprecipitation of Ro RNPs, Our data demonstrate that anti-p52 antibodies do not target intact Ro RNPs, nor do they target the native 60-kD Ro protein. Contrary to previous reports, p52 protein is not a stable component of antigenically intact Ro RNPs.

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Molecular cloning, expression, and chromosome 19 localization of a human Ro/SS-A autoantigen.

Cited by 165 publications

References 54 publications

Calreticulin, a Potential Cell Surface Receptor Involved in Cell Penetration of Anti-DNA Antibodies

Calreticulin, a Potential Cell Surface Receptor Involved in Cell Penetration of Anti-DNA Antibodies

Complete congenital heart block is associated with increased autoantibody titers against calreticulin

Purification of antigenically intact Ro ribonucleoproteins; biochemical and Immunological evidence that the 52-kD protein is not a Ro protein

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