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Articles by LIU Shu-bai
Total Records ( 3 ) for LIU Shu-bai
  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 Jinqiao and ZHANG Yun
  In vertebrates, non-lens βγ-crystallins are widely expressed in various tissues and their functions are not well known. The molecular mechanisms of trefoil factors (TFFs), which involved in mucosal healing and tumorigenesis, have remained elusive. βγ-CAT is a novel multifunctional protein complex of non-lens βγ-crystallin and trefoil factor from frog skin secretions. Here we report that βγ-CAT could induce sustained contraction of isolated rabbit aortic rings in dosage (2-35 nmol/L) and endothelium dependent manners (P<0.01). In addition, in situ immunofluorescence indicated that positive TNF-α signals were mainly detected at the endothelial cell layer of βγ-CAT (25 nmol/L) treated rings. Furthermore, βγ-CAT induced primary cultured rabbit thoracic aortic endothelial cells (RAECs) rapidly to release TNF-α. After βγ-CAT (25 nmol/L) treated for 10 and 30 min, the levels of the endothelial cells released TNF-α were 34.17±5.10 pg/mL and 98.01±4.67 pg/mL (P<0.01), respectively. In conclusion, βγ-CAT could induce sustained contraction of isolated aortic rings, and the contractile effect might be partially explained by the release of TNF-α. These findings will give new insight into understanding the functions and physiological roles of non-lens βγ-crystallins and trefoil factors.
  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.
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