The Experts below are selected from a list of 207 Experts worldwide ranked by ideXlab platform
Guo-lin Zou - One of the best experts on this subject based on the ideXlab platform.
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The presence of anti-mitochondrial antibodies in Chinese patients with liver involvement in systemic lupus erythematosus
Rheumatology International, 2006Co-Authors: Chun-yan Wang, Yun Zhang, Guo-lin ZouAbstract:Sixty-six hospitalized patients with systemic lupus erythematosus (SLE) were enrolled into this study. The test for anti-mitochondrial antibodies (AMAs) was performed and biochemical parameters were determined. AMAs were detected in 15 of the 66 patients with SLE. Meanwhile, we compared enzymatic levels in AMA-positive and -negative patients and found that serum Aminotransferase levels were significantly higher in AMA-positive patients than in AMA-negative individuals. Furthermore, we found a positive correlation between serum AMA titration and serum Aminotransferase levels. This study suggests that AMAs might contribute to the elevation of Aminotransferases. Although much remains to be learned about the pathogenesis of autoimmune liver disease associated with AMAs, this report might provide greater insight into the metabolic mechanisms of AMAs in AMA-positive patients.
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Increased serum Aminotransferases associated with anti-mitochondrial antibodies in systemic lupus erythematosus patients with autoimmune liver disease.
Clinica Chimica Acta, 2006Co-Authors: Chun-yan Wang, Guo-lin ZouAbstract:Serum Aminotransferase activities are increased in many liver diseases, but the causes for the elevation might be difficult to determine. Whether the elevation of Aminotransferases correlates with anti-mitochondrial antibodies (AMA) in systemic lupus erythematosus (SLE) patients with autoimmune liver disease deserves further consideration. A meticulous review was done in a large SLE cohort searching for laboratory features of the presence of AMA. Forty-eight hospitalized SLE patients with AMA and 60 randomly selected SLE patients without AMA as a matched case control were enrolled into the retrospective study. Laboratory data were collected, analyzed and compared in SLE patients with and without AMA. Serum activities of Aminotransferases were significantly increased in the 48 SLE patients with AMA compared with the 60 subjects without AMA. Meanwhile, we found a positive correlation between serum AMA titers and serum Aminotransferase activities. Although much remains to be learned about the pathogenesis of autoimmune liver disease associated with AMA, it is possible to suggest that AMA might contribute to the elevation of Aminotransferases in SLE patients with the progressive disease.
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Increased serum Aminotransferases associated with anti-mitochondrial antibodies in systemic lupus erythematosus patients with autoimmune liver disease.
Clinica Chimica Acta, 2005Co-Authors: Chun-yan Wang, Guo-lin ZouAbstract:Abstract Background Serum Aminotransferase activities are increased in many liver diseases, but the causes for the elevation might be difficult to determine. Whether the elevation of Aminotransferases correlates with anti-mitochondrial antibodies (AMA) in systemic lupus erythematosus (SLE) patients with autoimmune liver disease deserves further consideration. Methods A meticulous review was done in a large SLE cohort searching for laboratory features of the presence of AMA. Forty-eight hospitalized SLE patients with AMA and 60 randomly selected SLE patients without AMA as a matched case control were enrolled into the retrospective study. Laboratory data were collected, analyzed and compared in SLE patients with and without AMA. Results Serum activities of Aminotransferases were significantly increased in the 48 SLE patients with AMA compared with the 60 subjects without AMA. Meanwhile, we found a positive correlation between serum AMA titers and serum Aminotransferase activities. Conclusion Although much remains to be learned about the pathogenesis of autoimmune liver disease associated with AMA, it is possible to suggest that AMA might contribute to the elevation of Aminotransferases in SLE patients with the progressive disease.
Chun-yan Wang - One of the best experts on this subject based on the ideXlab platform.
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The presence of anti-mitochondrial antibodies in Chinese patients with liver involvement in systemic lupus erythematosus
Rheumatology International, 2006Co-Authors: Chun-yan Wang, Yun Zhang, Guo-lin ZouAbstract:Sixty-six hospitalized patients with systemic lupus erythematosus (SLE) were enrolled into this study. The test for anti-mitochondrial antibodies (AMAs) was performed and biochemical parameters were determined. AMAs were detected in 15 of the 66 patients with SLE. Meanwhile, we compared enzymatic levels in AMA-positive and -negative patients and found that serum Aminotransferase levels were significantly higher in AMA-positive patients than in AMA-negative individuals. Furthermore, we found a positive correlation between serum AMA titration and serum Aminotransferase levels. This study suggests that AMAs might contribute to the elevation of Aminotransferases. Although much remains to be learned about the pathogenesis of autoimmune liver disease associated with AMAs, this report might provide greater insight into the metabolic mechanisms of AMAs in AMA-positive patients.
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Increased serum Aminotransferases associated with anti-mitochondrial antibodies in systemic lupus erythematosus patients with autoimmune liver disease.
Clinica Chimica Acta, 2006Co-Authors: Chun-yan Wang, Guo-lin ZouAbstract:Serum Aminotransferase activities are increased in many liver diseases, but the causes for the elevation might be difficult to determine. Whether the elevation of Aminotransferases correlates with anti-mitochondrial antibodies (AMA) in systemic lupus erythematosus (SLE) patients with autoimmune liver disease deserves further consideration. A meticulous review was done in a large SLE cohort searching for laboratory features of the presence of AMA. Forty-eight hospitalized SLE patients with AMA and 60 randomly selected SLE patients without AMA as a matched case control were enrolled into the retrospective study. Laboratory data were collected, analyzed and compared in SLE patients with and without AMA. Serum activities of Aminotransferases were significantly increased in the 48 SLE patients with AMA compared with the 60 subjects without AMA. Meanwhile, we found a positive correlation between serum AMA titers and serum Aminotransferase activities. Although much remains to be learned about the pathogenesis of autoimmune liver disease associated with AMA, it is possible to suggest that AMA might contribute to the elevation of Aminotransferases in SLE patients with the progressive disease.
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Increased serum Aminotransferases associated with anti-mitochondrial antibodies in systemic lupus erythematosus patients with autoimmune liver disease.
Clinica Chimica Acta, 2005Co-Authors: Chun-yan Wang, Guo-lin ZouAbstract:Abstract Background Serum Aminotransferase activities are increased in many liver diseases, but the causes for the elevation might be difficult to determine. Whether the elevation of Aminotransferases correlates with anti-mitochondrial antibodies (AMA) in systemic lupus erythematosus (SLE) patients with autoimmune liver disease deserves further consideration. Methods A meticulous review was done in a large SLE cohort searching for laboratory features of the presence of AMA. Forty-eight hospitalized SLE patients with AMA and 60 randomly selected SLE patients without AMA as a matched case control were enrolled into the retrospective study. Laboratory data were collected, analyzed and compared in SLE patients with and without AMA. Results Serum activities of Aminotransferases were significantly increased in the 48 SLE patients with AMA compared with the 60 subjects without AMA. Meanwhile, we found a positive correlation between serum AMA titers and serum Aminotransferase activities. Conclusion Although much remains to be learned about the pathogenesis of autoimmune liver disease associated with AMA, it is possible to suggest that AMA might contribute to the elevation of Aminotransferases in SLE patients with the progressive disease.
Cristina Nowicki - One of the best experts on this subject based on the ideXlab platform.
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structural basis for the relaxed substrate selectivity of leishmania mexicana broad specificity Aminotransferase
Molecular and Biochemical Parasitology, 2015Co-Authors: Cristina Nowicki, W BlankenfeldtAbstract:Abstract Leishmania species are early branching eukaryotic parasites that cause difficult-to-treat tissue-damaging diseases known as leishmaniases. As a hallmark of their parasitic lifestyle, Leishmaniae express a number of Aminotransferases that are involved in important cellular processes and exhibit broader substrate specificity than their mammalian host's counterparts. Here, we have determined the crystal structure of the broad specificity Aminotransferase from Leishmania mexicana (LmexBSAT) at 1.91 A resolution. LmexBSAT is a homodimer and belongs to the α-branch of family-I Aminotransferases. Despite the fact that the protein was crystallized in the absence of substrates and has lost the pyridoxal-5′-phosphate (PLP) cofactor during crystallization, the structure resembles the closed, ligand-bound form of related enzymes such as chicken cytosolic aspartate Aminotransferase. Its broader substrate specificity seems to be rooted in increased flexibility of a substrate-binding arginine (R291) and the interactions of this residue with the N-terminus of the second chain of the dimer.
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A recombinant tyrosine Aminotransferase from Trypanosoma cruzi has both tyrosine Aminotransferase and alanine Aminotransferase activities
FEMS microbiology letters, 1995Co-Authors: Marisa Montemartini, Jacqueline Búa, Esteban J. Bontempi, Cecilia Zelada, Andrés M. Ruiz, Joséa. Santomé, Juan Josécazzulo, Cristina NowickiAbstract:Tyrosine Aminotransferase purified from epimastigotes of Trypanosoma cruzi displays an additional activity of alanine Aminotransferase, absent in all other tyrosine Aminotransferases characterized so far. Since the parasite's genome contains a high number of copies of the tyrosine Aminotransferase gene, we could not rule out the possibility that two very similar proteins, with changed specificity due to a few amino acid substitutions, might be responsible for the two activities. We have now expressed in Escherichia coli a recombinant tyrosine Aminotransferase as a fusion protein with glutathione S-trans-ferase. The purified fusion protein, intact or after thrombin cleavage, displays tyrosine Aminotransferase and alanine Aminotransferase activities with apparent Km values similar to those for the natural enzyme, thus proving that they belong to the same protein.
Jong Shik Shin - One of the best experts on this subject based on the ideXlab platform.
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exploring the active site of amine pyruvate Aminotransferase on the basis of the substrate structure reactivity relationship how the enzyme controls substrate specificity and stereoselectivity
Journal of Organic Chemistry, 2002Co-Authors: Jong Shik ShinAbstract:An active site model of the amine:pyruvate Aminotransferase (APA) from Vibrio fluvialis JS17 was constructed on the basis of the relationship between substrate structure and reactivity. Due to the broad substrate specificity of the APA, various amino donors (chiral and achiral amine, amino acid, and amino acid derivative) and amino acceptors (keto acid, keto ester, aldehyde, and ketone) were used to explore the active site structure. The result suggested a two-binding site model consisting of two pockets, one large (L) and the other small (S). The difference in the size of each binding pocket and strong repulsion for a carboxylate in the S pocket were key determinants to control its substrate specificity and stereoselectivity. The L pocket showed dual recognition mode for both hydrophobic and carboxyl groups as observed in the side-chain pockets of aspartate Aminotransferase and aromatic Aminotransferase. Comparison of the model with those of other Aminotransferases revealed that the L and S pockets corre...
Marisa Montemartini - One of the best experts on this subject based on the ideXlab platform.
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A recombinant tyrosine Aminotransferase from Trypanosoma cruzi has both tyrosine Aminotransferase and alanine Aminotransferase activities
FEMS microbiology letters, 1995Co-Authors: Marisa Montemartini, Jacqueline Búa, Esteban J. Bontempi, Cecilia Zelada, Andrés M. Ruiz, Joséa. Santomé, Juan Josécazzulo, Cristina NowickiAbstract:Tyrosine Aminotransferase purified from epimastigotes of Trypanosoma cruzi displays an additional activity of alanine Aminotransferase, absent in all other tyrosine Aminotransferases characterized so far. Since the parasite's genome contains a high number of copies of the tyrosine Aminotransferase gene, we could not rule out the possibility that two very similar proteins, with changed specificity due to a few amino acid substitutions, might be responsible for the two activities. We have now expressed in Escherichia coli a recombinant tyrosine Aminotransferase as a fusion protein with glutathione S-trans-ferase. The purified fusion protein, intact or after thrombin cleavage, displays tyrosine Aminotransferase and alanine Aminotransferase activities with apparent Km values similar to those for the natural enzyme, thus proving that they belong to the same protein.
