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NILAI DIAGNOSTIK UJI TROPONIN I KUANTITATIF METODE IMMUNOKROMATOGRAFI Siti Fatonah; Anik Widijanti; Tinny Endang Hernowati
INDONESIAN JOURNAL OF CLINICAL PATHOLOGY AND MEDICAL LABORATORY Vol 14, No 1 (2007)
Publisher : Indonesian Association of Clinical Pathologist and Medical laboratory

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.24293/ijcpml.v14i1.920

Abstract

Cardiac troponins are the most sensitive and specific biochemical markers of myocardial damage but there is no standardization of WHO for cardiac troponin I, resulting in a variability for diagnostic value. It is necessary to determine diagnostic value for a new kitof troponin I. To evaluate a new quantitative immunochromatography assay for troponin I at a various cut off level. A cross sectionalstudy was conducted in 64 patients with acute myocardial infarction (AMI) and 55 non-AMI as control from February to September2007. The level of cardiac troponin I (cTnI) was measured and determined it diagnostic value at a various cut off level. The sensitivity,specificity, PPV and NPV of this assay were 91%, 91%, 92% and 89% at cut off level of 1,0 ng/ml (according to the kit), respectively.The cut off of cTnI were divided into five levels: 0.8, 1.0, 1.2, 1.5, and 2.0 with the area under curve were 0.923, 0.908, 0.912, and0.897, respectively. The sensitivity were 94%, 91%, 86%, 81% and 72%, respectively, the specificity were 91%, 91%, 96%, 98% and98%, respectively. This rapid diagnostic test is sensitive and specific to diagnose an acute coronary syndromes.
α-SMA Expression Increased Over Cell Passages and Decreased by Exogenous TGF-β1, In Vitro Studies on Myofibroblast Derived from Orbital Socket Contracture Debby Shintiya Dewi; Elsa Safira Chairinnisa; Hidayat Sujuti; Diana Lirawati; Tinny Endang Hernowati
Journal of Tropical Life Science Vol. 8 No. 2 (2018)
Publisher : Journal of Tropical Life Science

Show Abstract | Download Original | Original Source | Check in Google Scholar | DOI: 10.11594/jtls.08.02.15

Abstract

α-smooth muscle actin (α-SMA), a marker of myofibroblast, induces cytoskeleton reorganization, increases contractility and stimulates cell migration in TGF-β1 induced stress fibers. The aims of the present study were to determine the level of α-SMA expression and morphological cell changes in different passages of myofi-broblasts with varied TGF-β1 concentrations. Myofibroblast cell cultures were derived from fibrotic tissues of fourth degree socket contracture. The α-SMA expression level was measured in myofibroblast cultures pas-sage I, II, and III with and without 10 ng/mL TGF-β1, and in passage III with 2.5; 5; 10; and 20 ng/mL TGF-β1. Results: The levels of α-SMA expression level in passage I to III were I 31.42 ± 3.4; 40.34 ± 8.14 and 56.37 ± 7.57, respectively. Addition of 10 ng/mL TGF-β1 into passage I-III myofibroblast cultures resulted in α-SMA expression level of 31.24 ± 2.93; 36.81 ± 6.09; and 14.29 ± 2.72, respectively. Myoblasts passage III showed the lowest α-SMA expression level following exposure to TGF-β1 10 ng/mL (22.37 ± 12.86) and highest without TGF-β1 (48.34 ± 13.36), however no morphological changes detected. α-SMA expression level increased with cell passages, decreases with addition of TGF-β1 while not affecting morphology of myofibroblast derived from the orbital socket contracture.