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Reliable, easy-to-read patient information on common medical conditions — written in plain language, free of jargon, and grounded in current evidence. Browse the most frequent diagnoses, understand what they mean for everyday life, and learn which steps and questions help you have a focused conversation with your doctor.

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Sjogren syndrome antigen B

Introduction

Sjogren syndrome antigen B (autoantigen La), also known as SSB, is a human gene.[1]

La is involved in diverse aspects of RNA metabolism, including binding and protecting 3-prime UUU(OH) elements of newly RNA polymerase III (see MIM 606007)-transcribed RNA, processing 5-prime and 3-prime ends of pre-tRNA precursors, acting as an RNA chaperone, and binding viral RNAs associated with hepatitis C virus. La protein was originally defined by its reactivity with autoantibodies from patients with Sjogren syndrome (MIM 270150) and systemic lupus erythematosus (SLE; MIM 152700) (Teplova et al., 2006).[supplied by OMIM][1]

References

References

  1. ↑ 1.0 1.1 “Entrez Gene: SSB Sjogren syndrome antigen B (autoantigen La)”.
Further reading

Further reading

  • Kohsaka H, Yamamoto K, Fujii H; et al. (1990). “Fine epitope mapping of the human SS-B/La protein. Identification of a distinct autoepitope homologous to a viral gag polyprotein”. J. Clin. Invest. 85 (5): 1566–74. PMID 1692037.
  • Sturgess AD, Peterson MG, McNeilage LJ; et al. (1988). “Characteristics and epitope mapping of a cloned human autoantigen La”. J. Immunol. 140 (9): 3212–8. PMID 2452201.
  • Rauh AJ, Hornig H, Lührmann R (1989). “At least three distinct B cell epitopes reside in the C-terminal half of La protein, as determined by a recombinant DNA approach”. Eur. J. Immunol. 18 (12): 2049–57. PMID 2464497.
  • Chan EK, Sullivan KF, Tan EM (1989). “Ribonucleoprotein SS-B/La belongs to a protein family with consensus sequences for RNA-binding”. Nucleic Acids Res. 17 (6): 2233–44. PMID 2468131.
  • Gottlieb E, Steitz JA (1989). “Function of the mammalian La protein: evidence for its action in transcription termination by RNA polymerase III”. EMBO J. 8 (3): 851–61. PMID 2470590.
  • Chambers JC, Kenan D, Martin BJ, Keene JD (1989). “Genomic structure and amino acid sequence domains of the human La autoantigen”. J. Biol. Chem. 263 (34): 18043–51. PMID 3192525.
  • Chambers JC, Keene JD (1985). “Isolation and analysis of cDNA clones expressing human lupus La antigen”. Proc. Natl. Acad. Sci. U.S.A. 82 (7): 2115–9. PMID 3856888.
  • Svitkin YV, Pause A, Sonenberg N (1994). “La autoantigen alleviates translational repression by the 5′ leader sequence of the human immunodeficiency virus type 1 mRNA”. J. Virol. 68 (11): 7001–7. PMID 7933082.
  • Tröster H, Metzger TE, Semsei I; et al. (1994). “One gene, two transcripts: isolation of an alternative transcript encoding for the autoantigen La/SS-B from a cDNA library of a patient with primary Sjögrens’ syndrome”. J. Exp. Med. 180 (6): 2059–67. PMID 7964483.
  • Fan H, Sakulich AL, Goodier JL; et al. (1997). “Phosphorylation of the human La antigen on serine 366 can regulate recycling of RNA polymerase III transcription complexes”. Cell. 88 (5): 707–15. PMID 9054510.
  • McLaren RS, Caruccio N, Ross J (1997). “Human La protein: a stabilizer of histone mRNA”. Mol. Cell. Biol. 17 (6): 3028–36. PMID 9154801.
  • Grölz D, Bachmann M (1997). “The nuclear autoantigen La/SS-associated antigen B: one gene, three functional mRNAs”. Biochem. J. 323 ( Pt 1): 151–8. PMID 9173875.
  • Helsloot J, Sturgess A (1998). “T cell reactivity to Sjögren’s syndrome related antigen La(SSB)”. J. Rheumatol. 24 (12): 2340–7. PMID 9415639.
  • Broekhuis CH, Neubauer G, van der Heijden A; et al. (2000). “Detailed analysis of the phosphorylation of the human La (SS-B) autoantigen. (De)phosphorylation does not affect its subcellular distribution”. Biochemistry. 39 (11): 3023–33. PMID 10715123.
  • SpÃ¥ngberg K, Wiklund L, Schwartz S (2000). “HuR, a protein implicated in oncogene and growth factor mRNA decay, binds to the 3′ ends of hepatitis C virus RNA of both polarities”. Virology. 274 (2): 378–90. doi:10.1006/viro.2000.0461. PMID 10964780.
  • Intine RV, Sakulich AL, Koduru SB; et al. (2000). “Control of transfer RNA maturation by phosphorylation of the human La antigen on serine 366”. Mol. Cell. 6 (2): 339–48. PMID 10983981.
  • Nashimoto M, Nashimoto C, Tamura M; et al. (2001). “The inhibitory effect of the autoantigen La on in vitro 3′ processing of mammalian precursor tRNAs”. J. Mol. Biol. 312 (5): 975–84. doi:10.1006/jmbi.2001.5026. PMID 11580243.
  • De Nova-Ocampo M, Villegas-Sepúlveda N, del Angel RM (2002). “Translation elongation factor-1alpha, La, and PTB interact with the 3′ untranslated region of dengue 4 virus RNA”. Virology. 295 (2): 337–47. doi:10.1006/viro.2002.1407. PMID 12033793.
  • Intine RV, Dundr M, Misteli T, Maraia RJ (2002). “Aberrant nuclear trafficking of La protein leads to disordered processing of associated precursor tRNAs”. Mol. Cell. 9 (5): 1113–23. PMID 12049746.
  • Fouraux MA, Bouvet P, Verkaart S; et al. (2002). “Nucleolin associates with a subset of the human Ro ribonucleoprotein complexes”. J. Mol. Biol. 320 (3): 475–88. PMID 12096904.

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