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Clinical Chemistry 52: 414-420, 2006. First published January 12, 2006; 10.1373/clinchem.2005.062307
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Right arrow Proteomics and Protein Markers
(Clinical Chemistry. 2006;52:414-420.)
© 2006 American Association for Clinical Chemistry, Inc.

Proteomics and Protein Markers

Cardiac Troponin T Circulates in the Free, Intact Form in Patients with Kidney Failure

Michael N. Fahie-Wilson1, David J. Carmichael2, Michael P. Delaney3, Paul E. Stevens3, Elizabeth M. Hall4 and Edmund J. Lamb4,a

Departments of1 Clinical Biochemistry and2 Renal Medicine, Southend Hospital, Westcliff-on-Sea, United Kingdom.
Departments of3 Renal Medicine and4 Clinical Biochemistry, East Kent Hospitals NHS Trust, Kent and Canterbury Hospital, Canterbury, United Kingdom.

aAddress correspondence to this author at: Department of Clinical Biochemistry, East Kent Hospitals NHS Trust, Kent and Canterbury Hospital, Canterbury, Kent, United Kingdom CT1 3NG. Fax 44-01227-783077; e-mail edmund.lamb{at}ekht.nhs.uk.

Background: The clinical significance of the increased concentrations of cardiac troponins observed in patients with end stage renal disease (ESRD) in the absence of an acute coronary syndrome (ACS) is controversial. One proposed explanation is that immunoreactive fragments of cardiac troponin T (cTnT) accumulate in ESRD. We used gel-filtration chromatography (GFC) to ascertain whether fragments of cTnT, which could cross-react in the commercial diagnostic immunoassay (Roche Diagnostics), were the cause of the increased cTnT in the serum of patients with ESRD.

Methods: We subjected sera from ESRD patients (n = 21) receiving dialysis and having increased cTnT concentrations to size-separation GFC. We detected cTnT in the chromatography fractions by use of the same antibodies used in the commercial assay for serum cTnT.

Results: In all patients, cTnT immunoreactivity eluted as a major, homogeneous peak in an identical position between the peaks of serum prolactin [relative molecular mass (Mr) 23 000] and albumin (Mr 67 000): the elution pattern of cTnT in samples obtained from ACS patients was identical to that of the ESRD patients. There was no evidence that low–molecular-mass (Mr <23 000) cTnT fragments were the cause of the increased cTnT in the patients studied.

Conclusions: The form of cTnT observed in the serum of patients with kidney failure and immunoreactive in the diagnostic assay is predominantly the free intact form, as in patients with ACS. Our data are consistent with the view that circulating cTnT in renal failure reflects cardiac pathology.




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The authors of the article cited above respond:
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