Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase

C. V. Dang, E. M. Tan, J. A. Traugh

Research output: Contribution to journalArticle

Abstract

Spontaneously occurring autoantibody to threonyl-tRNA synthetase found in the serum of patients with polymyositis and experimentally induced antibody against highly purified rabbit reticulocyte threonyl-tRNA synthetase were used to analyze the epitopes of threonyl-tRNA synthetase. The PL-7 autoantibody reacted with the native but not the denatured form of threonyl-tRNA synthetase, whereas the experimentally induced antibody recognized both the native and denatured forms of the enzyme. In addition, the PL-7 autoantibody specifically inhibited threonyl-tRNA synthetase activity whereas the experimentally induced antibody had no effect on aminoacylation. Thus, the epitopes recognized by the PL-7 autoantibody are formed by the tertiary structure of the enzyme and are associated with the catalytic site of the synthetase whereas the experimentally induced antibody recognizes epitopes formed by primary sequences not related to the catalytic function of the synthetase.

Original languageEnglish (US)
Pages (from-to)2376-2379
Number of pages4
JournalFASEB Journal
Volume2
Issue number8
StatePublished - 1988
Externally publishedYes

Fingerprint

Threonine-tRNA Ligase
myositis
Myositis
autoantibodies
Autoantibodies
epitopes
Epitopes
antibodies
Antibodies
Ligases
ligases
polymyositis
aminoacylation
Aminoacylation
Polymyositis
reticulocytes
Reticulocytes
Enzymes
enzymes
active sites

ASJC Scopus subject areas

  • Agricultural and Biological Sciences (miscellaneous)
  • Biochemistry, Genetics and Molecular Biology(all)
  • Biochemistry
  • Cell Biology

Cite this

Dang, C. V., Tan, E. M., & Traugh, J. A. (1988). Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase. FASEB Journal, 2(8), 2376-2379.

Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase. / Dang, C. V.; Tan, E. M.; Traugh, J. A.

In: FASEB Journal, Vol. 2, No. 8, 1988, p. 2376-2379.

Research output: Contribution to journalArticle

Dang, CV, Tan, EM & Traugh, JA 1988, 'Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase', FASEB Journal, vol. 2, no. 8, pp. 2376-2379.
Dang, C. V. ; Tan, E. M. ; Traugh, J. A. / Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase. In: FASEB Journal. 1988 ; Vol. 2, No. 8. pp. 2376-2379.
@article{1132d0fabe474f6089c6441e588e38ad,
title = "Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase",
abstract = "Spontaneously occurring autoantibody to threonyl-tRNA synthetase found in the serum of patients with polymyositis and experimentally induced antibody against highly purified rabbit reticulocyte threonyl-tRNA synthetase were used to analyze the epitopes of threonyl-tRNA synthetase. The PL-7 autoantibody reacted with the native but not the denatured form of threonyl-tRNA synthetase, whereas the experimentally induced antibody recognized both the native and denatured forms of the enzyme. In addition, the PL-7 autoantibody specifically inhibited threonyl-tRNA synthetase activity whereas the experimentally induced antibody had no effect on aminoacylation. Thus, the epitopes recognized by the PL-7 autoantibody are formed by the tertiary structure of the enzyme and are associated with the catalytic site of the synthetase whereas the experimentally induced antibody recognizes epitopes formed by primary sequences not related to the catalytic function of the synthetase.",
author = "Dang, {C. V.} and Tan, {E. M.} and Traugh, {J. A.}",
year = "1988",
language = "English (US)",
volume = "2",
pages = "2376--2379",
journal = "FASEB Journal",
issn = "0892-6638",
publisher = "FASEB",
number = "8",

}

TY - JOUR

T1 - Myositis autoantibody reactivity and catalytic function of threonyl-tRNA synthetase

AU - Dang, C. V.

AU - Tan, E. M.

AU - Traugh, J. A.

PY - 1988

Y1 - 1988

N2 - Spontaneously occurring autoantibody to threonyl-tRNA synthetase found in the serum of patients with polymyositis and experimentally induced antibody against highly purified rabbit reticulocyte threonyl-tRNA synthetase were used to analyze the epitopes of threonyl-tRNA synthetase. The PL-7 autoantibody reacted with the native but not the denatured form of threonyl-tRNA synthetase, whereas the experimentally induced antibody recognized both the native and denatured forms of the enzyme. In addition, the PL-7 autoantibody specifically inhibited threonyl-tRNA synthetase activity whereas the experimentally induced antibody had no effect on aminoacylation. Thus, the epitopes recognized by the PL-7 autoantibody are formed by the tertiary structure of the enzyme and are associated with the catalytic site of the synthetase whereas the experimentally induced antibody recognizes epitopes formed by primary sequences not related to the catalytic function of the synthetase.

AB - Spontaneously occurring autoantibody to threonyl-tRNA synthetase found in the serum of patients with polymyositis and experimentally induced antibody against highly purified rabbit reticulocyte threonyl-tRNA synthetase were used to analyze the epitopes of threonyl-tRNA synthetase. The PL-7 autoantibody reacted with the native but not the denatured form of threonyl-tRNA synthetase, whereas the experimentally induced antibody recognized both the native and denatured forms of the enzyme. In addition, the PL-7 autoantibody specifically inhibited threonyl-tRNA synthetase activity whereas the experimentally induced antibody had no effect on aminoacylation. Thus, the epitopes recognized by the PL-7 autoantibody are formed by the tertiary structure of the enzyme and are associated with the catalytic site of the synthetase whereas the experimentally induced antibody recognizes epitopes formed by primary sequences not related to the catalytic function of the synthetase.

UR - http://www.scopus.com/inward/record.url?scp=0023929836&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0023929836&partnerID=8YFLogxK

M3 - Article

C2 - 2452112

AN - SCOPUS:0023929836

VL - 2

SP - 2376

EP - 2379

JO - FASEB Journal

JF - FASEB Journal

SN - 0892-6638

IS - 8

ER -