Asian Science Citation Index is committed to provide an authoritative, trusted and significant information by the coverage of the most important and influential journals to meet the needs of the global scientific community.  
ASCI Database
308-Lasani Town,
Sargodha Road,
Faisalabad, Pakistan
Fax: +92-41-8815544
Contact Via Web
Suggest a Journal
Articles by Jing Jin
Total Records ( 3 ) for Jing Jin
  Yang Yang , Shabbir M. Walijee , Jing Jin , Shui-ping Zhao and Dao-Quan Peng


Apolipoprotein A-V (ApoA-V) has been shown to play an important role in the metabolism of plasma triglyceride (TG) levels. However, data for the relationship between serum ApoA-V and TG level and the association between ApoA-V levels and the risk of coronary artery disease (CAD) are inconsistent.


To investigate plasma ApoA-V level and its association with TG in patients with CAD determined by angiography.


Three hundred forty subjects who underwent coronary angiography (CAG) were classified into a CAD group (n = 211) and a non-CAD group (n = 129) according to the results of their CAG. Serum ApoA-V levels were determined by enzyme-linked immunosorbent assays.


Patients in the CAD group had greater ApoA-V levels than controls (192.0 114.6 ng/mL vs 164.4 107.5 ng/mL, P < .05). The concentration of ApoA-V was positively correlated to TG level (r = 0.229, P < .01). This correlation was more intense in non-CAD group (r = 0.306, P < .01) than in CAD group (r = 0.172, P < .05). ApoA-V was positively associated with Gensini score. However, the contribution of ApoA-V to Gensini score and CAD risk disappeared after adjustment for the TG level.


The positive correlation between serum ApoA-V and TG differs in strength between control and CAD patients. The correlation between ApoA-V and CAD is confounded by the effect of TG. We speculate that the increase of ApoA-V may be a consequence of compensation for the increased demand for plasma TG hydrolysis.

  Robin Chan , Pradeep D. Uchil , Jing Jin , Guanghou Shui , David E. Ott , Walther Mothes and Markus R. Wenk
  Retroviruses acquire a lipid envelope during budding from the membrane of their hosts. Therefore, the composition of this envelope can provide important information about the budding process and its location. Here, we present mass spectrometry analysis of the lipid content of human immunodeficiency virus type 1 (HIV-1) and murine leukemia virus (MLV). The results of this comprehensive survey found that the overall lipid content of these viruses mostly matched that of the plasma membrane, which was considerably different from the total lipid content of the cells. However, several lipids are enriched in comparison to the composition of the plasma membrane: (i) cholesterol, ceramide, and GM3; and (ii) phosphoinositides, phosphorylated derivatives of phosphatidylinositol. Interestingly, microvesicles, which are similar in size to viruses and are also released from the cell periphery, lack phosphoinositides, suggesting a different budding mechanism/location for these particles than for retroviruses. One phosphoinositide, phosphatidylinositol 4,5-bisphosphate [PI(4,5)P2], has been implicated in membrane binding by HIV Gag. Consistent with this observation, we found that PI(4,5)P2 was enriched in HIV-1 and that depleting this molecule in cells reduced HIV-1 budding. Analysis of mutant virions mapped the enrichment of PI(4,5)P2 to the matrix domain of HIV Gag. Overall, these results suggest that HIV-1 and other retroviruses bud from cholesterol-rich regions of the plasma membrane and exploit matrix/PI(4,5)P2 interactions for particle release from cells.
  Wei Yang , Chao Qiu , Nabanita Biswas , Jing Jin , Simon C. Watkins , Ronald C. Montelaro , Carolyn B. Coyne and Tianyi Wang
  Claudin-1 (CLDN1), a tight junction (TJ) protein, has recently been identified as an entry co-receptor for hepatitis C virus (HCV). Ectopic expression of CLDN1 rendered several non-hepatic cell lines permissive to HCV infection. However, little is known about the mechanism by which CLDN1 mediates HCV entry. It is believed that an additional entry receptor(s) is required because ectopic expression of CLDN1 in both HeLa and NIH3T3 cells failed to confer susceptibility to viral infection. Here we found that CLDN1 was co-immunoprecipitated with both HCV envelope proteins when expressed in 293T cells. Results from biomolecular fluorescence complementation assay showed that overexpressed CLDN1 also formed complexes with CD81 and low density lipoprotein receptor. Subsequent imaging analysis revealed that CLDN1 was highly enriched at sites of cell-cell contact in permissive cell lines, co-localizing with the TJ marker, ZO-1. However, in both HeLa and NIH3T3 cells the ectopically expressed CLDN1 appeared to reside predominantly in intracellular vesicles. The CLDN1-CD81 complex formed in HeLa cells was also exclusively distributed intracellularly, co-localizing with EEA1, an early endosomal marker. Correspondingly, transepithelial electric resistance, obtained from the naturally susceptible human liver cell line, Huh7, was much higher than that of the HeLa-CLDN1 cell line, suggesting that Huh7 is likely to form functional tight junctions. Finally, the disruption of TJ-enriched CLDN1 by tumor necrosis factor-α treatment markedly reduced the susceptibility of Huh7.5.1 cells to HCV infection. Our results suggest that the specific localization pattern of CLDN1 may be crucial in the regulation of HCV cellular tropism.
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility