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Articles by Jie Jiang
Total Records ( 2 ) for Jie Jiang
  Bingye Yang , Jie Jiang , Haoxin Du , Guojun Geng , Zhen Jiang , Chengcai Yao , Qiqing Zhang and Lihua Jin
  Human esophageal cancer is a common occurring malignancy with high mortality rate partially due to lack of tools for early diagnosis. In this study, we have analysed tumour tissue from 50 cases of primary esophageal cancer. Our studies showed that the activity of monoamine oxidase (MAO) and the expression of MAO-A were strikingly decreased in the tumour tissues of 48 (96%) and 44 (88%) patients, respectively. These results suggest that the activity of MAO and the expression of MAO-A may be used as new diagnostic markers for esophageal cancers.
  Indira H. Shrivastava , Jie Jiang , Susan G. Amara and Ivet Bahar
  Glutamate transporters, also referred to as excitatory amino acid transporters (EAATs), are membrane proteins that regulate glutamatergic signal transmission by clearing excess glutamate after its release at synapses. A structure-based understanding of their molecular mechanisms of function has been elusive until the recent determination of the x-ray structure of an archaeal transporter, GltPh. GltPh exists as a trimer, with each subunit containing a core region that mediates substrate translocation. In the present study a series of molecular dynamics simulations have been conducted and analyzed in light of new experimental data on substrate binding properties of EAATs. The simulations provide for the first time a full atomic description of the time-resolved events that drive the recognition and binding of substrate. The core region of each subunit exhibits an intrinsic tendency to open the helical hairpin HP2 loop, the extracellular gate, within tens of nanoseconds exposing conserved polar residues that serve as attractors for substrate binding. The NMDGT motif on the partially unwound part of the transmembrane helix TM7 and the residues Asp-390 and Asp-394 on TM8 are also distinguished by their important role in substrate binding and close interaction with mediating water molecules and/or sodium ions. The simulations reveal a Na+ binding site comprised in part of Leu-303 on TM7 and Asp-405 on TM8 and support a role for sodium ions in stabilizing substrate-bound conformers. The functional importance of Leu-303 or its counterpart Leu-391 in human EAAT1 (hEAAT1) is confirmed by site-directed mutagenesis and Na+ dependence assays conducted with hEAAT1 mutants L391C and L391A.
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