中华肝脏病杂志
中華肝髒病雜誌
중화간장병잡지
CHINESE JOURNAL OF HEPATOLOGY
2000年
5期
276-278
,共3页
陈平圣%翟为溶%张月娥%张锦生%顾映红
陳平聖%翟為溶%張月娥%張錦生%顧映紅
진평골%적위용%장월아%장금생%고영홍
缺氧%肝星状细胞%基质金属蛋白酶Ⅱ%基质金属蛋白酶组织抑制因子Ⅱ
缺氧%肝星狀細胞%基質金屬蛋白酶Ⅱ%基質金屬蛋白酶組織抑製因子Ⅱ
결양%간성상세포%기질금속단백매Ⅱ%기질금속단백매조직억제인자Ⅱ
Hypoxia%Hepatic stellate cell%Matrix metalloproteinase-2%Tissue inhibitor of metalloproteinase-2
目的:研究缺氧对HSC基质金属蛋白酶Ⅱ(matrix metalloproteinase-2,MMP-2)表达及活性调节的影响。方法:大鼠HSC体外原代培养,以免疫细胞化学及ELISA法分别检测细胞内MMP-2及基质金属蛋白酶组织抑制因子Ⅱ(Tissue inhibitor of metalloproteinase-2,TIMP-2)的表达,和培养上清液中两者的相对量,并以酶图法测培养上清液MMP-2活力。 结果:缺氧培养12h,免疫细胞化学显示MMP-2表达高于对照组(t'=3.4685,P<0.05=,TIMP-2表达则降低(t'=2.5673,P<0.05 =;培养上清液中MMP-2酶活性低于对照组(t′=4.270,P<0.01=。缺氧6h上清液MMP-2蛋白相对含量增加值高于12h及24h组(t值分别为4.0945、2.4652;P值分别为<0.001、0.025=;TIMP-2变化趋势与MMP-2则相反,但各组间差异无显著性。结论 缺氧使肝星状细胞MMP-2含量增加,该影响在早期更明显。
目的:研究缺氧對HSC基質金屬蛋白酶Ⅱ(matrix metalloproteinase-2,MMP-2)錶達及活性調節的影響。方法:大鼠HSC體外原代培養,以免疫細胞化學及ELISA法分彆檢測細胞內MMP-2及基質金屬蛋白酶組織抑製因子Ⅱ(Tissue inhibitor of metalloproteinase-2,TIMP-2)的錶達,和培養上清液中兩者的相對量,併以酶圖法測培養上清液MMP-2活力。 結果:缺氧培養12h,免疫細胞化學顯示MMP-2錶達高于對照組(t'=3.4685,P<0.05=,TIMP-2錶達則降低(t'=2.5673,P<0.05 =;培養上清液中MMP-2酶活性低于對照組(t′=4.270,P<0.01=。缺氧6h上清液MMP-2蛋白相對含量增加值高于12h及24h組(t值分彆為4.0945、2.4652;P值分彆為<0.001、0.025=;TIMP-2變化趨勢與MMP-2則相反,但各組間差異無顯著性。結論 缺氧使肝星狀細胞MMP-2含量增加,該影響在早期更明顯。
목적:연구결양대HSC기질금속단백매Ⅱ(matrix metalloproteinase-2,MMP-2)표체급활성조절적영향。방법:대서HSC체외원대배양,이면역세포화학급ELISA법분별검측세포내MMP-2급기질금속단백매조직억제인자Ⅱ(Tissue inhibitor of metalloproteinase-2,TIMP-2)적표체,화배양상청액중량자적상대량,병이매도법측배양상청액MMP-2활력。 결과:결양배양12h,면역세포화학현시MMP-2표체고우대조조(t'=3.4685,P<0.05=,TIMP-2표체칙강저(t'=2.5673,P<0.05 =;배양상청액중MMP-2매활성저우대조조(t′=4.270,P<0.01=。결양6h상청액MMP-2단백상대함량증가치고우12h급24h조(t치분별위4.0945、2.4652;P치분별위<0.001、0.025=;TIMP-2변화추세여MMP-2칙상반,단각조간차이무현저성。결론 결양사간성상세포MMP-2함량증가,해영향재조기경명현。
Objective: To study the effect of hypoxia on the expression and activity of matrix metalloproteinase-2 (MMP-2) in the hepatic stellate cell (HSC). Methods: The expression of MMP-2 and tissue inhibitor of metalloproteinase-2 (TIMP-2) in cultured rat HSC was detected by immunocytochemistry (ICC). The relative amount of MMP-2 and TIMP-2 in the culture supernatant was assayed by ELISA and the activity of MMP-2 in supernatant was examined by zymography. Results: The expression of MMP-2 was enhanced in hypoxia group as compared with that in control one (t'=3.4685, P<0.05), while the expression of TIMP-2 was decreased (t'=2.5673, P<0.05). The activity of MMP-2 was lower in hypoxia group than in control one (t'=4.270, P<0.01). Comparing the varied duration of hypoxia, the relative amount of MMP-2 protein was the highest in 6 h group (6h vs 12h, t=4.0945, P<0.001; 6h vs 24h, t=2.4652, P<0.025), with a contrary curve in TIMP-2. Conclusion: Hypoxia promotes the expression of MMP-2 and inhibits the expression of TIMP-2 in HSC. It is more notable at early stage of hypoxia.