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 QIAN Jin-qiao
Total Records ( 2 ) for QIAN Jin-qiao
  HE Ying-ying , LIU Shu-bai , QIAN Jin-qiao , LEE Wen-hui and ZHANG Yun
  βγ-CAT is a naturally existing protein complex of non-lens βγ-crystallin and trefoil factor, purified from Bombina maxima skin secretions. In HUVECs, βγ-CAT can be rapidly endocytosed via intracellular vacuole formation and translocated to the nucleus to regulate cell fuction. In this paper, we found that it contains conserved Walker B motifs (IILYDEPS, residues 6-13) and Walker A motifs (GQSLSGKS, residues 96-103) in the βγ-CAT α-subunit sequence. βγ-CAT showed potential NTP-binding and weak GTPase/ATPase activities in vitro. Through Western blotting analysis, we found that the α- and β-subunits of βγ-CAT participated in a 150 kDa SDS-stable protein complex formation, which also contained positive ubiquitination signals in the βγ-CAT treated HUVEC. Furthermore,under confocal microscopy, the immunofluorescence signals of ubiquitin and βγ-CAT subunits were co-localized in the vacuoles that were distributed in the cytoplasm and nucleus. In addition, βγ-CAT could induce several tumor cell`s detachment and apoptosis, and selectively kill tumor cells. These findings provide a clue to understand the mechanism of βγ-CAT endocysis and nuclear transport, and give an insight to investigate the possible occurrence of similar molecule’s cellular functions and action mechanisms of non-lens βγ-crystallins and trefoil factors in mammals.
  LIU Shu-bai , HE Ying-ying , QIAN Jin-qiao and ZHANG Yun
  βγ-CAT is a naturally existing multifunctional protein complex of non-lens βγ-crystallin and trefoil factor from Bombina maxima skin secretions. In this paper, we first analysed the time-response curve of hemolysis and intracellular potassium efflux induced by βγ-CAT on human erythrocytes. After βγ-CAT (3 nmol/L) in human erythrocytes was treated at 37¡æ for 5 min, we found that about 93.31±5.89% (P<0.01) of the intracellular potassium ions leaked, whereas the percentage of hemolysis was only13.12±1.92 % (P<0.05). We employed electron microscopy to observe the erythrocytes’ morphological changes and found erythrocytes were swollen and some had globular structures occurring on the cell surfaces, and fast releasing hemoglobins. These results indicated that the hemolytic effect of βγ-CAT on human erythrocyte membranes was due to intracellular potassium ion¡¯s rapid efflux. These results demonstrate morphological proof in understanding the mechanism of βγ-CAT pore-forming effect on human erythrocytes.
 
 
 
Copyright   |   Desclaimer   |    Privacy Policy   |   Browsers   |   Accessibility