2003
DOI: 10.1378/chest.124.4_meetingabstracts.153s-a
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Performance and Practicability Evaluation of five Cardiac Troponin I Assays in Patients With Acute Coronary Syndrom

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Cited by 6 publications
(8 citation statements)
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“…The aims of the present study were to determine whether high-intensity exercise elevates cTnI concentrations in fit, athletic, clinically normal horses and to determine at approximately what time after exercise cTnI concentrations peak, in order to determine when to sample horses with suspected exercise-induced cardiac disease. This results in values that are not directly comparable from one analyser to another 12,[47][48][49][50][51][52] . The ranges we obtained in this group of horses at rest were similar to that of concentrations our lab has determined to be normal (# 0.08 ng ml 21 ) using the Stratus CS (unpublished data).…”
Section: Discussionmentioning
confidence: 99%
“…The aims of the present study were to determine whether high-intensity exercise elevates cTnI concentrations in fit, athletic, clinically normal horses and to determine at approximately what time after exercise cTnI concentrations peak, in order to determine when to sample horses with suspected exercise-induced cardiac disease. This results in values that are not directly comparable from one analyser to another 12,[47][48][49][50][51][52] . The ranges we obtained in this group of horses at rest were similar to that of concentrations our lab has determined to be normal (# 0.08 ng ml 21 ) using the Stratus CS (unpublished data).…”
Section: Discussionmentioning
confidence: 99%
“…[7][8][9][10][11][12] Cardiac troponin I analyzers have not been standardized and because each company can use a potentially different and proprietary target amino acid in the assay, values obtained on 1 analyzer may not be directly comparable to values obtained on a different analyzer. [13][14][15][16] In addition, assays may have different reference ranges because of assay differences in the antibody specificity for free and complexed cTnI. The predominant circulating form of cardiac troponins in human beings is cTnI complexed to cardiac troponin C; however, the predominant circulating form in dogs is not known.…”
mentioning
confidence: 99%
“…[17][18][19] Several studies in human medicine have compared analyzers, and although results obtained on different analyzers correlate well, a large (up to 20-fold) difference in the absolute values obtained between some machines has been observed. [13][14][15]17,20,21 The use of and the potential applications for cTnI analysis are growing in veterinary medicine; however, the inability to compare values obtained on different analyzers has limited collaborative studies between institutions to this point. Reference ranges for dogs have been developed for several different analyzers using the 95th percentile as the upper end of the range, and the established ranges are similar for 3 of these analyzers (Biosite Triage Meter a ,0.05-0.12 ng/mL, Dade-Behring Stratus b ,0.03-0.07 ng/mL, and Beckman-Coulter Access AccuTnI c 0.01-0.11 ng/mL).…”
mentioning
confidence: 99%
“…Degradation products of TnT were also found both in animal models of ischemia/reperfusion injury [38,39] and in serum of patients with AMI [40,41]. In 2000, TnI and TnT have been approved as the biomarkers for AMI diagnosis [42], and several kits have been commercially developed and used in clinical studies [43][44][45]. In addition to TnI and TnT, other myofilament proteins, including TnC [46], LC2 [46], aactinin [32] and MyBP-C [47], were also reported as useful markers in animal models of ischemia/reperfusion injury.…”
Section: Degradationmentioning
confidence: 99%
“…Alternatively, the degradation site can be mapped using antibody epitope analysis [62], in which an array of mAb recognizing different regions within protein sequences is used [43][44][45].…”
Section: Degradationmentioning
confidence: 99%