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Clinical Chemistry 50: 682-684, 2004; 10.1373/clinchem.2003.027730
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(Clinical Chemistry. 2004;50:682-684.)
© 2004 American Association for Clinical Chemistry, Inc.

Letters to the Editor

Targets of Antibodies to Soluble Liver Antigen in Patients with Autoimmune Hepatitis

Dimitrios-Petrou Bogdanos1, Ilaria Bianchi1, Yun Ma1, Ragai R. Mitry1, Giorgina Mieli-Vergani1 and Diego Vergani1,a

1 Institute of Liver Studies, King’s College Hospital, Denmark Hill, London SE5 9RS, UK

aAuthor for correspondence. Fax 44-20-7346-3700; e-mail diego.vergani@kcl.ac.uk.

The first 20% of the full text of this article appears below.


To the Editor:

Antibodies to a cytosolic soluble liver antigen (SLA), originally detected by an inhibition ELISA using cytosolic liver fractions and proposed as marker of a third type of autoimmune hepatitis (AIH) negative for other autoantibodies, have been also reported in anti-nuclear and/or -smooth muscle antibody type 1 AIH, liver kidney microsomal-type 2 AIH, and autoimmune sclerosing cholangitis (1)(2)(3). Anti-SLA is specific for these autoimmune liver diseases, in which it is associated with a more severe disease course, whereas it is virtually absent in nonhepatic autoimmune disorders (1)(2)(3). The target of anti-SLA has recently been identified by several groups as a UGA serine tRNA-associated protein complex [tRNP(Ser)Sec], through the screening of cDNA libraries (4)(5)(6).

On the basis that not all of the anti-SLA-positive sera identified by inhibition ELISA react with tRNP(Ser)Sec and referring to studies indicating that SLA is a mixture of distinct antigens, Ballot et al. (7) questioned the identity of tRNP(Ser)Sec as the molecular target of anti-SLA antibodies. These investigators set out to reassess the matter, using anti-SLA-positive sera against rat liver cytosolic fraction in one- and two-dimensional immunoblotting analyses. Through peptide mass fingerprint analysis after matrix-assisted laser desorption/ionization time-of-flight mass spectrometry, the authors identified four isoforms of {alpha}-enolase, a cytosolic enzyme of 50 . . . [Full Text of this Article]

Eric Ballot, Arnaud Bruneel and Catherine Johaneta

Laboratoire d’Immunologie, Hôpital Saint-Antoine, AP-HP, 75012 Paris, France

aAuthor for correspondence. Fax 33-1-49283046; e-mail catherine.johanet@sat.ap-hop-paris.fr.






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