Human autoantibodies against a nucleolar protein.

Abstract:

:Autoimmune sera showing prominent immunofluorescence in nucleolus were selected and analysed by immunoblotting techniques. Immunoblots using a nucleolar extract as antigen source revealed sera recognizing a 38 kDa nucleolar protein. Low concentration of Actinomycin D, which inhibits the ribosomal RNA synthesis, caused a loss of fluorescence. This suggests that the nucleolar antigen may be associated with the assembly of packaging of the ribosomes. The present nucleolar antigen has properties similar to the previously described nucleolar phosphoprotein B23 of rat cells and the recently described nucleolar protein NO38 of mouse and Xenopus cells.

authors

Kindås-Mügge I

doi

10.1016/0006-291x(89)92337-1

subject

Has Abstract

pub_date

1989-09-15 00:00:00

pages

1119-27

issue

2

eissn

0006-291X

issn

1090-2104

pii

0006-291X(89)92337-1

journal_volume

163

pub_type

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