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Takao Tanaka - One of the best experts on this subject based on the ideXlab platform.

  • human heart type cytoplasmic fatty acid binding protein h fabp for the diagnosis of acute myocardial infarction clinical evaluation of h fabp in comparison with myoglobin and Creatine Kinase Isoenzyme mb
    Clinical Chemistry and Laboratory Medicine, 2000
    Co-Authors: F Okamoto, Koichi Sohmiya, Yasuhiko Ohkaru, Keishiro Kawamura, Kumiko Asayama, Hiroshi Kimura, Shinzo Nishimura, Hiroo Ishii, N Sunahara, Takao Tanaka
    Abstract:

    : Heart-type fatty acid-binding protein (H-FABP) is a low molecular weight cytoplasmic protein and present abundantly in the myocardium. When the myocardium is injured, as in the case of myocardial infarction, low molecular weight cytoplasmic proteins including H-FABP are released into the circulation and H-FABP is detectable in a blood sample. We have already developed a direct sandwich-ELISA for quantification of human H-FABP using two distinct types of monoclonal antibodies specific for human H-FABP. In this study we investigated the clinical validity of H-FABP as a biochemical diagnostic marker in the early phase of acute myocardial infarction (AMI). To evaluate the diagnostic usefulness of H-FABP in the early phase of AMI, blood samples were obtained from the following patients within 12 hours after the appearance of symptoms, and serum levels of H-FABP were compared with those of conventional diagnostic markers, such as myoglobin and Creatine Kinase Isoenzyme MB (CK-MB). Blood samples were collected from patients with confirmed AMI (n=140), patients with chest pain who were afterwards not classified as AMI by normal CK-MB levels (non-AMI) (n=49) and normal healthy volunteers (n=75). The serum concentration of H-FABP was quantified with our direct sandwich-ELISA. The concentration of myoglobin mass was measured with a commercial RIA kit. The serum CK-MB activity was determined with an immuno-inhibition assay kit. The overall sensitivity of H-FABP, within 12 hours after the appearance of symptoms, was 92.9%, while it was 88.6% with myoglobin and 18.6% with CK-MB. The overall specificity of H-FABP was 67.3%, while it was 57.1% with myoglobin and 98.0% with CK-MB. The diagnostic efficacy rates with these markers were 86.2% (H-FABP), 80.4% (myoglobin) and 39.2% (CK-MB), respectively. The diagnostic validity of H-FABP was further assessed by receiver operating characteristic (ROC) curve analysis. The area under the curve (AUC) of H-FABP was 0.921, which was significantly greater than with myoglobin (AUC: 0.843) and CK-MB (AUC: 0.654). These parameters, such as sensitivity, specificity, diagnostic efficacy and diagnostic accuracy, obtained for patients with chest pain within 3 hours and/or 6 hours after the onset of symptoms were almost the same as those for patients within 12 hours after symptoms. H-FABP is more sensitive than both myoglobin and CK-MB, more specific than myoglobin for detecting AMI within 12 hours after the onset of symptoms, and shows the highest values for both diagnostic efficacy and ROC curve analysis. Thus, H-FABP has great potential as an excellent biochemical cardiac marker for the diagnosis of AMI in the early phase.

  • human heart type cytoplasmic fatty acid binding protein h fabp for the diagnosis of acute myocardial infarction clinical evaluation of h fabp in comparison with myoglobin and Creatine Kinase Isoenzyme mb
    Clinical Chemistry and Laboratory Medicine, 2000
    Co-Authors: F Okamoto, Koichi Sohmiya, Yasuhiko Ohkaru, Keishiro Kawamura, Kumiko Asayama, Hiroshi Kimura, Shinzo Nishimura, Hiroo Ishii, N Sunahara, Takao Tanaka
    Abstract:

    Heart-type fatty acid-binding protein (H-FABP) is a low molecular weight cytoplasmic protein and present abundantly in the myocardium. When the myocardium is injured, as in the case of myocardial infarction, low molecular weight cytoplasmic proteins including H-FABP are released into the circulation and H-FABP is detectable in a blood sample. We have already developed a direct sandwich-ELISA for quantification of human H-FABP using two distinct types of monoclonal antibodies specific for human H-FABP. In this study we investigated the clinical validity of H-FABP as a biochemical diagnostic marker in the early phase of acute myocardial infarction (AMI). To evaluate the diagnostic usefulness of H-FABP in the early phase of AMI, blood samples were obtained from the following patients within 12 hours after the appearance of symptoms, and serum levels of H-FABP were compared with those of conventional diagnostic markers, such as myoglobin and Creatine Kinase Isoenzyme MB (CK-MB). Blood samples were collected from patients with confirmed AMI (n=140), patients with chest pain who were afterwards not classified as AMI by normal CK-MB levels (non-AMI) (n=49) and normal healthy volunteers (n=75). The serum concentration of H-FABP was quantified with our direct sandwich-ELISA. The concentration of myoglobin mass was measured with a commercial RIA kit. The serum CK-MB activity was determined with an immuno-inhibition assay kit. The overall sensitivity of H-FABP, within 12 hours after the appearance of symptoms, was 92.9%, while it was 88.6% with myoglobin and 18.6% with CK-MB. The overall specificity of H-FABP was 67.3%, while it was 57.1% with myoglobin and 98.0% with CK-MB. The diagnostic efficacy rates with these markers were 86.2% (H-FABP), 80.4% (myoglobin) and 39.2% (CK-MB), respectively. The diagnostic validity of H-FABP was further assessed by receiver operating characteristic (ROC) curve analysis. The area under the curve (AUC) of H-FABP was 0.921, which was significantly greater than with myoglobin (AUC: 0.843) and CK-MB (AUC: 0.654). These parameters, such as sensitivity, specificity, diagnostic efficacy and diagnostic accuracy, obtained for patients with chest pain within 3 hours and/or 6 hours after the onset of symptoms were almost the same as those for patients within 12 hours after symptoms. H-FABP is more sensitive than both myoglobin and CK-MB, more specific than myoglobin for detecting AMI within 12 hours after the onset of symptoms, and shows the highest values for both diagnostic efficacy and ROC curve analysis. Thus, H-FABP has great potential as an excellent biochemical cardiac marker for the diagnosis of AMI in the early phase.

F Okamoto - One of the best experts on this subject based on the ideXlab platform.

  • human heart type cytoplasmic fatty acid binding protein h fabp for the diagnosis of acute myocardial infarction clinical evaluation of h fabp in comparison with myoglobin and Creatine Kinase Isoenzyme mb
    Clinical Chemistry and Laboratory Medicine, 2000
    Co-Authors: F Okamoto, Koichi Sohmiya, Yasuhiko Ohkaru, Keishiro Kawamura, Kumiko Asayama, Hiroshi Kimura, Shinzo Nishimura, Hiroo Ishii, N Sunahara, Takao Tanaka
    Abstract:

    : Heart-type fatty acid-binding protein (H-FABP) is a low molecular weight cytoplasmic protein and present abundantly in the myocardium. When the myocardium is injured, as in the case of myocardial infarction, low molecular weight cytoplasmic proteins including H-FABP are released into the circulation and H-FABP is detectable in a blood sample. We have already developed a direct sandwich-ELISA for quantification of human H-FABP using two distinct types of monoclonal antibodies specific for human H-FABP. In this study we investigated the clinical validity of H-FABP as a biochemical diagnostic marker in the early phase of acute myocardial infarction (AMI). To evaluate the diagnostic usefulness of H-FABP in the early phase of AMI, blood samples were obtained from the following patients within 12 hours after the appearance of symptoms, and serum levels of H-FABP were compared with those of conventional diagnostic markers, such as myoglobin and Creatine Kinase Isoenzyme MB (CK-MB). Blood samples were collected from patients with confirmed AMI (n=140), patients with chest pain who were afterwards not classified as AMI by normal CK-MB levels (non-AMI) (n=49) and normal healthy volunteers (n=75). The serum concentration of H-FABP was quantified with our direct sandwich-ELISA. The concentration of myoglobin mass was measured with a commercial RIA kit. The serum CK-MB activity was determined with an immuno-inhibition assay kit. The overall sensitivity of H-FABP, within 12 hours after the appearance of symptoms, was 92.9%, while it was 88.6% with myoglobin and 18.6% with CK-MB. The overall specificity of H-FABP was 67.3%, while it was 57.1% with myoglobin and 98.0% with CK-MB. The diagnostic efficacy rates with these markers were 86.2% (H-FABP), 80.4% (myoglobin) and 39.2% (CK-MB), respectively. The diagnostic validity of H-FABP was further assessed by receiver operating characteristic (ROC) curve analysis. The area under the curve (AUC) of H-FABP was 0.921, which was significantly greater than with myoglobin (AUC: 0.843) and CK-MB (AUC: 0.654). These parameters, such as sensitivity, specificity, diagnostic efficacy and diagnostic accuracy, obtained for patients with chest pain within 3 hours and/or 6 hours after the onset of symptoms were almost the same as those for patients within 12 hours after symptoms. H-FABP is more sensitive than both myoglobin and CK-MB, more specific than myoglobin for detecting AMI within 12 hours after the onset of symptoms, and shows the highest values for both diagnostic efficacy and ROC curve analysis. Thus, H-FABP has great potential as an excellent biochemical cardiac marker for the diagnosis of AMI in the early phase.

  • human heart type cytoplasmic fatty acid binding protein h fabp for the diagnosis of acute myocardial infarction clinical evaluation of h fabp in comparison with myoglobin and Creatine Kinase Isoenzyme mb
    Clinical Chemistry and Laboratory Medicine, 2000
    Co-Authors: F Okamoto, Koichi Sohmiya, Yasuhiko Ohkaru, Keishiro Kawamura, Kumiko Asayama, Hiroshi Kimura, Shinzo Nishimura, Hiroo Ishii, N Sunahara, Takao Tanaka
    Abstract:

    Heart-type fatty acid-binding protein (H-FABP) is a low molecular weight cytoplasmic protein and present abundantly in the myocardium. When the myocardium is injured, as in the case of myocardial infarction, low molecular weight cytoplasmic proteins including H-FABP are released into the circulation and H-FABP is detectable in a blood sample. We have already developed a direct sandwich-ELISA for quantification of human H-FABP using two distinct types of monoclonal antibodies specific for human H-FABP. In this study we investigated the clinical validity of H-FABP as a biochemical diagnostic marker in the early phase of acute myocardial infarction (AMI). To evaluate the diagnostic usefulness of H-FABP in the early phase of AMI, blood samples were obtained from the following patients within 12 hours after the appearance of symptoms, and serum levels of H-FABP were compared with those of conventional diagnostic markers, such as myoglobin and Creatine Kinase Isoenzyme MB (CK-MB). Blood samples were collected from patients with confirmed AMI (n=140), patients with chest pain who were afterwards not classified as AMI by normal CK-MB levels (non-AMI) (n=49) and normal healthy volunteers (n=75). The serum concentration of H-FABP was quantified with our direct sandwich-ELISA. The concentration of myoglobin mass was measured with a commercial RIA kit. The serum CK-MB activity was determined with an immuno-inhibition assay kit. The overall sensitivity of H-FABP, within 12 hours after the appearance of symptoms, was 92.9%, while it was 88.6% with myoglobin and 18.6% with CK-MB. The overall specificity of H-FABP was 67.3%, while it was 57.1% with myoglobin and 98.0% with CK-MB. The diagnostic efficacy rates with these markers were 86.2% (H-FABP), 80.4% (myoglobin) and 39.2% (CK-MB), respectively. The diagnostic validity of H-FABP was further assessed by receiver operating characteristic (ROC) curve analysis. The area under the curve (AUC) of H-FABP was 0.921, which was significantly greater than with myoglobin (AUC: 0.843) and CK-MB (AUC: 0.654). These parameters, such as sensitivity, specificity, diagnostic efficacy and diagnostic accuracy, obtained for patients with chest pain within 3 hours and/or 6 hours after the onset of symptoms were almost the same as those for patients within 12 hours after symptoms. H-FABP is more sensitive than both myoglobin and CK-MB, more specific than myoglobin for detecting AMI within 12 hours after the onset of symptoms, and shows the highest values for both diagnostic efficacy and ROC curve analysis. Thus, H-FABP has great potential as an excellent biochemical cardiac marker for the diagnosis of AMI in the early phase.

Hitoshi Hishida - One of the best experts on this subject based on the ideXlab platform.

  • early detection of successful coronary reperfusion based on serum myoglobin concentration comparison with serum Creatine Kinase Isoenzyme mb activity
    American Heart Journal, 1994
    Co-Authors: Junnichi Ishii, Masanori Nomura, Toshikazu Ando, Hiroshi Hasegawa, Mamoru Kimura, Hiroshi Kurokawa, Masatsugu Iwase, Takeshi Kondo, Yoshihiko Watanabe, Hitoshi Hishida
    Abstract:

    Abstract The usefulness of serum myoglobin (Mb) concentration for early detection of successful reperfusion was compared with that of Creatine Kinase Isoenzyme MB (CKMB) activity in 49 patients with acute myocardial infarction. To determine accurately the time of reperfusion, we performed coronary angiography every 5 minutes during reperfusion therapy. Reperfusion was obtained in 32 patients (reperfused group) but not in 17 patients (nonreperfused group) until 60 minutes after the initiation of reperfusion therapy. Blood samples were taken before and 15, 30, and 60 minutes after the angiographic confirmation of reperfusion in the reperfused group. In the nonreperfused group, samples were taken before and 15, 30, and 60 minutes after the initiation of treatment. We calculated the Mb ratio (value after reperfusion or treatment initiation to value before) and CKMB ratio (value after to value before). When values >2.4 for the Mb ratio or >2.0 for the CKMB ratio were used as the criteria for reperfusion within 60 minutes after initiation of treatment, the sensitivities were 91% and 56% at 15 minutes after reperfusion, 97% and 84% at 30 minutes, and 100% and 100% at 60 minutes, respectively. For each ratio the specificity of detection was 100% at all times evaluated. Thus the Mb ratio accurately detected the success of reperfusion as early as 15 minutes after reperfusion and may be more useful than the CKMB ratio for detecting the success of reperfusion within 30 minutes.

William M. Rand - One of the best experts on this subject based on the ideXlab platform.

  • Increased Serum Total Creatine Kinase and Creatine Kinase Isoenzyme MB After Cryosurgical Ablation of the Prostate
    The Journal of Urology, 1997
    Co-Authors: John P. Long, Mark L. Fallick, William M. Rand
    Abstract:

    AbstractPurpose: Several reports have documented that the MB Isoenzyme of Creatine Kinase is present in prostatic tissue. However, since it has been shown that lower urinary tract manipulations, including transurethral prostatectomy, do not significantly increase serum Creatine Kinase Isoenzyme MB levels, such elevations, which are found in patients after prostatic surgery, are believed to be specific for myocardial infarction. We examined whether cryosurgical ablation of the prostate altered serum Creatine Kinase or Isoenzyme MB levels.Materials and Methods: In 81 consecutive patients undergoing routine cryosurgical ablation of the prostate serum levels of Creatine Kinase and Creatine Kinase Isoenzyme MB were measured from peripheral blood specimens drawn preoperatively, in the recovery room and at 8 and 24 hours postoperatively. Postoperative electrocardiograms were compared to the preoperative study.Results: In 72 of 81 patients (89%) significant elevations in Creatine Kinase and Creatine Kinase isoenz...

Theo Wallimann - One of the best experts on this subject based on the ideXlab platform.

  • development and performance of an enzyme immunoassay to detect Creatine Kinase Isoenzyme mb activity using anti mitochondrial Creatine Kinase monoclonal antibodies
    Scandinavian Journal of Clinical & Laboratory Investigation, 2009
    Co-Authors: Tadashi Hoshino, Theo Wallimann, Uwe Schlattner, Yasuhiro Sakai, Kazuaki Yamashita, Yasushi Shirahase, Kouji Sakaguchi, Ayumi Asaeda, Kouji Kishi, Mitsuru Yanai
    Abstract:

    Objective: The MB fraction of Creatine Kinase (CK-MB) has long been used as a cardiac marker. It is known that the CK-MB immunoinhibition method lacks selectivity and accuracy, because the appearan...

  • Development and performance of an enzyme immunoassay to detect Creatine Kinase Isoenzyme MB activity using anti-mitochondrial Creatine Kinase monoclonal antibodies.
    Scandinavian Journal of Clinical and Laboratory Investigation, 2009
    Co-Authors: Tadashi Hoshino, Theo Wallimann, Uwe Schlattner, Yasuhiro Sakai, Kazuaki Yamashita, Yasushi Shirahase, Kouji Sakaguchi, Ayumi Asaeda, Kouji Kishi, Mitsuru Yanai
    Abstract:

    Objective: The MB fraction of Creatine Kinase (CK-MB) has long been used as a cardiac marker. It is known that the CK-MB immunoinhibition method lacks selectivity and accuracy, because the appearance of macro CK type 2, corresponding to mitochondrial Creatine Kinase (MtCK) in some patient serum may render CK-MB activity measured by conventional method abnormally high. Thus, to improve the specificity and accuracy of the CK-MB assay, we developed two types of monoclonal anti-MtCK antibodies against sarcomeric MtCK and ubiquitous MtCK, and present herein the performance of a new method using these antibodies. Material and methods: The performance of our test for detecting CK-MB activity was compared with other methods, and the range of CK-MB activities in normal human serum was investigated. Results: The two types of monoclonal antibodies developed by us were Isoenzyme-specific to sMtCK or uMtCK. The correlation coefficients of our method and conventional method to electrophoresis were 0.973 and 0.873, respectively. The mean CK-MB activity in normal human serum by our method and the conventional method was 2.4 and 11.7 U/L, respectively. Thus, our data indicated that about 80% of CK-MB activity, determined using the conventional method, seems to correspond to the MtCK activity. Conclusion: Our method is novel in offering higher accuracy of measuring true CK-MB contents in human serum as compared to the conventional method. The possibility of accurately estimating CK-MB activity by our method which can inhibit MtCKs in healthy person and patient serum is likely to bring a break-through in clinical diagnostics.

  • Expression of Creatine Kinase Isoenzyme genes during postnatal development of rat brain cerebellum: evidence for transcriptional regulation.
    Biochemical Journal, 2002
    Co-Authors: Wei Shen, Theo Wallimann, Dianna Willis, Yanping Zhang, Uwe Schlattner, George Molloy
    Abstract:

    Transcription and accumulation of brain-type Creatine Kinase (CKB) mRNA and its protein was examined during postnatal development of rat brain cerebellum, the brain region containing highest CKB mRNA in the adult. CKB protein was extremely low at day 1, increased about 10-fold until week 4 and remained constant until week 10. This time course was paralleled by cerebellar CKB mRNA, which was also extremely low at day 1 and increased 5-fold during the first 3 weeks and then remained constant. High levels of CKB protein were also detected in cultured primary cerebellar granular neurons. Nuclear run-on assays directly showed that CKB mRNA accumulation during postnatal cerebellar development was due to increased transcription. When compared with cerebrum and whole brain, cerebellar CKB mRNA accumulation during postnatal development was temporally delayed. Analysis of myocyte enhancer factor (MEF)-2 and Sp1, factors known to initiate or sustain CKB transcription in tissues other than brain, revealed that MEF-2 in cerebellum was low at week 1 but increased 3.5-fold by week 7, while Sp1 remained unchanged. The increase in CKB protein during cerebellar postnatal development was coincident with that of the ubiquitous mitochondrial CK protein and mRNA, indicating that a functional phosphoCreatine energy shuttle probably exists for efficient ATP regeneration in the cerebellum. This should be beneficial for the many energy-demanding requirements during cerebellar development, as indicated by the observed temporal co-expression of CKB with myelin basic protein, which is involved in axon myelination by oligodendrocytes.

  • sequence homology and structure predictions of the Creatine Kinase Isoenzymes
    Molecular and Cellular Biochemistry, 1994
    Co-Authors: Stephan Muhlebach, Martin Gross, T Wirz, Theo Wallimann, Jeanclaude Perriard, Markus Wyss
    Abstract:

    Comparisons of the protein sequences and gene structures of the known Creatine Kinase Isoenzymes and other guanidino Kinases revealed high homology and were used to determine the evolutionary relationships of the various guamidino Kinases. A ‘CK framework’ is defined, consisting of the most conserved sequence blocks, and ‘diagnostic boxes’ are identified which are characteristic for anyone Creatine Kinase Isoenzyme (e.g. for vertebrate B-CK) and which may serve to distinguish this Isoenzyme from all others (e.g. from M-CKs and Mi-CKs). Comparison of the guanidino Kinases by near-UV and far-UV circular dichroism further indicates pronounced conservation of secondary structure as well as of aromatic amino acids that are involved in catalysis.