Clinical Chemistry
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Clinical Chemistry 44: 1919-1924, 1998;
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Right arrow Proteomics and Protein Markers
(Clinical Chemistry. 1998;44:1919-1924.)
© 1998 American Association for Clinical Chemistry, Inc.

Enzymes and Protein Markers

Cardiac troponin T isoforms expressed in renal diseased skeletal muscle will not cause false-positive results by the second generation cardiac troponin T assay by Boehringer Mannheim

Vincent Ricchiuti1, Ellen M. Voss1, Arthur Ney2, Mark Odland2, Page A. W. Anderson3, and Fred S. Apple1,a

Departments of
1 Laboratory Medicine and Pathology and
2 Surgery, Hennepin County Medical Center and the University of Minnesota, Minneapolis, MN 55415.
3 Department of Pediatrics, Duke University Medical Center, Durham, NC 27710.
a Address correspondence to this author at: Hennepin County Medical Center, Clinical Labs MC812, 701 Park Avenue, Minneapolis, MN 55415. Fax 612-904-4229; e-mail fred.apple{at}co.hennepin.mn.us.

The purpose of this study was to determine whether the two monoclonal anti-cardiac troponin T (cTnT) antibodies (MAbs) used in the second generation cTnT assay by Boehringer Mannheim (BM, capture Ab, M11.7; detection Ab, M7) would detect cTnT isoforms expressed in human skeletal muscle in response to chronic renal disease (CRD). cTnT expression was examined in skeletal muscle biopsies obtained from 45 CRD patients, as well as nondiseased human heart (n = 3) and skeletal muscle (n = 3). cTnT proteins were resolved by modified 7.5% sodium dodecyl sulfate-polyacrylamide gel electrophoresis, transferred to nitrocellulose, and probed with the following anti-cTnT MAbs: M11.7; M7; JS-2, Lakeland Biomedical; and 13–11, Duke University. All four antibodies detected the cTnT isoforms (Ta, Te) expressed in human myocardium. In 20 of 45 skeletal muscle biopsies, MAb M11.7 recognized its epitope in one to three proteins, molecular mass 34–36 kDa, designated Te, Td, and Tc; the strongest signal was that of Te. The same proteins were recognized by MAbs JS-2 and 13–11. The BM M7 antibody did not detect the cTnT isoforms in the molecular mass range of 34–36 kDa. However, MAb M7 did detect a cTnT isoform, molecular mass 39 kDa, in 2 of 45 biopsies. This isoform had an electrophoretic mobility similar to the predominant heart cTnT isoform, Ta. We conclude that cTnT isoforms are expressed in the skeletal muscle of CRD patients. However, given the epitopes recognized by the BM MAbs M7 and M11.7 and the variable presence of these cTnT isoforms in skeletal muscle, the second generation BM cTnT assay will not detect these isoforms if they are released from skeletal muscle into the circulation.


Key Words: cTnT, cardiac troponin T • cTnI, cardiac troponin I • MAb, monoclonal antibody • CRD, chronic renal disease • BM, Boehringer Mannheim • TTBS, Tween-Tris-buffered saline.




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