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2 results on '"Huachun Tang"'

1. AG-348 enhances pyruvate kinase activity in red blood cells from patients with pyruvate kinase deficiency

Author

Yingxia Xu, Shin-San Michael Su, Zhiwei Gu, Scott A. Biller, Charles Kung, Xiaobing Lv, Cheng Fang, Collin Hill, Yaguang Si, Zhiyong Luo, Penelope A. Kosinski, Francesco G. Salituro, Lenny Dang, Huachun Tang, Hua Yang, Lee Silverman, Kendall Johnson, Janeta Popovici-Muller, Gui Yao, Jeff Hixon, Gavin Histen, Stefan Gross, Yue Chen, Byron DeLaBarre, and Giovanni Cianchetta

Subjects
Hemolytic anemia, Erythrocytes, Anemia, Immunology, Allosteric regulation, Pyruvate Kinase, Enzyme Activators, Pharmacology, Biology, Pyruvate Metabolism, Inborn Errors, Biochemistry, Piperazines, 03 medical and health sciences, Mice, 0302 clinical medicine, Red Cells, Iron, and Erythropoiesis, medicine, Animals, Humans, Glycolysis, chemistry.chemical_classification, Sulfonamides, Cell Biology, Hematology, Anemia, Hemolytic, Congenital Nonspherocytic, medicine.disease, Molecular biology, Recombinant Proteins, Tissue Donors, Enzyme Activation, Kinetics, Enzyme, chemistry, 030220 oncology & carcinogenesis, Quinolines, Pyruvate kinase, Ex vivo, 030215 immunology, Pyruvate kinase deficiency
Abstract

Pyruvate kinase (PK) deficiency is a rare genetic disease that causes chronic hemolytic anemia. There are currently no targeted therapies for PK deficiency. Here, we describe the identification and characterization of AG-348, an allosteric activator of PK that is currently in clinical trials for the treatment of PK deficiency. We demonstrate that AG-348 can increase the activity of wild-type and mutant PK enzymes in biochemical assays and in patient red blood cells treated ex vivo. These data illustrate the potential for AG-348 to restore the glycolytic pathway activity in patients with PK deficiency and ultimately lead to clinical benefit.

Published
2017

2. Identification of a Differentially-expressed Gene in Fatty Liver of Overfeeding Geese

Author

Sufang Lu, Huachun Tang, Ayong Zhao, and Ruiguo He

Subjects
Male, Molecular Sequence Data, Biophysics, Selenium-Binding Proteins, Hyperphagia, Biology, Biochemistry, Avian Proteins, Eating, Mice, Dogs, Complementary DNA, Geese, Gene expression, medicine, Animals, Humans, Amino Acid Sequence, Selenium binding, Gene, Base Sequence, Fatty liver, General Medicine, medicine.disease, Molecular biology, Rats, Fatty Liver, Reverse transcription polymerase chain reaction, Open reading frame, Gene Expression Regulation, Cattle, Female, Differential display technique
Abstract

In response to overfeeding, geese develop fatty liver. To understand the fattening mechanism, mRNA differential display reverse transcription PCR was used to study the gene expression differences between French Landes grey geese and Xupu white geese in conditions of overfeeding and normal feeding. One gene was found to be up-regulated in the fatty liver in both breeds, and it has a 1797 bp cDNA with 83% identity to chicken SELENBP1. The sequence analysis revealed that its open reading frame of 1413 bp encodes a protein of 471 amino acids, which contains a putative conserved domain of 56 kDa selenium binding protein with high homology to its homologues of chicken (95%), rat (86%), mouse (84%), human (86%), monkey (86%), dog (86%), and cattle (86%). The function of this protein has been briefly reviewed based on published information. In tissue expression analysis, the expression of geese SELENBP1 mRNA was found to be higher in liver or kidney than in other tested tissues. The results showed that overfeeding could increase the mRNA expression level of geese SELENBP1.

Published
2007

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