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利用突变型CHO - K1细胞检测系统测定糖基磷脂酰肌醇甘露糖基转移酶-I(GPIMT - I)的甘露脂供体特异性。

Mannolipid donor specificity of glycosylphosphatidylinositol mannosyltransferase-I (GPIMT-I) determined with an assay system utilizing mutant CHO-K1 cells.

作者信息

DeLuca A W, Rush J S, Lehrman M A, Waechter C J

机构信息

Department of Pharmacology, UT-Southwestern Medical Center, Dallas 75235-9041, USA.

出版信息

Glycobiology. 1994 Dec;4(6):909-15. doi: 10.1093/glycob/4.6.909.

Abstract

The microsomal enzyme glycosylphosphatidylinositol mannosyltransferase I (GPIMT-I) catalyses the transfer of a mannosyl residue from beta-mannosylphosphoryldolichol (beta-Man-P-Dol) to glucosamine-alpha(1,6)(acyl)phosphatidylinositol (GlcN-aPI) to form Man alpha(1,4)GlcN-aPI (ManGlcN-aPI), an intermediate in glycosylphosphatidylinositol (GPI) synthesis. While the transfer of [3H]mannosyl units to endogenous GlcN-aPI was not seen when membrane fractions from normal Chinese hamster ovary (CHO) K1 cells were incubated with exogenous [3H]Man-P-Dol, GPIMT-I activity could be characterized with an in vitro enzyme assay system employing membrane fractions from Lec15 or Lec35 cells. These CHO cell mutants apparently contain elevated levels of endogenous GlcN-aPI due to the inability to synthesize (Lec15) or utilize (Lec35) beta-Man-P-Dol in vivo. The presence of a saturated alpha-isoprene unit in the dolichyl moiety is required for optimal GPIMT-I activity since beta-mannosylphosphorylpolyprenol (beta-Man-P-Poly), which contains a fully unsaturated polyisoprenyl chain, was only 50% as effective as beta-[3H]Man-P-Dol as a mannosyl donor. When beta-[3H]-Man-P-Dol and alpha-[3H]Man-P-Dol were compared as substrates, GPIMT-I exhibited a strict stereospecificity for the mannolipid containing the beta-mannosyl-phosphoryl linkage. beta-[3H]Man-P-dolichols containing 11 or 19 isoprenyl units were equally effective substrates for GPIMT-I. Membrane fractions from Lec 9, a CHO mutant that apparently lacks polyprenol reductase activity and synthesizes very little beta-Man-P-Dol, but accumulates beta-Man-P-Poly, synthesized no detectable Man-GlcN-aPI when incubated with beta-[3H]Man-P-Dol in vitro. This indirect assay suggests that GlcN-aPI does not accumulate in Lec 9 cells, possibly because it is mannosylated via beta-Man-P-Poly, or perhaps the small amount of Man-P-Dol formed by the mutant in vivo.(ABSTRACT TRUNCATED AT 250 WORDS)

摘要

微粒体酶糖基磷脂酰肌醇甘露糖基转移酶I(GPIMT-I)催化一个甘露糖基残基从β-甘露糖基磷酸多萜醇(β-Man-P-Dol)转移至氨基葡萄糖-α(1,6)(酰基)磷脂酰肌醇(GlcN-αPI),形成Manα(1,4)GlcN-αPI(ManGlcN-αPI),这是糖基磷脂酰肌醇(GPI)合成中的一个中间体。当正常中国仓鼠卵巢(CHO)K1细胞的膜组分与外源性[³H]Man-P-Dol一起孵育时,未观察到[³H]甘露糖基单位向内源性GlcN-αPI的转移,但GPIMT-I活性可用一个体外酶分析系统来表征,该系统采用Lec15或Lec35细胞的膜组分。这些CHO细胞突变体由于在体内无法合成(Lec15)或利用(Lec35)β-Man-P-Dol,其内源GlcN-αPI水平显然升高。多萜醇部分中饱和α-异戊二烯单位的存在是GPIMT-I最佳活性所必需的,因为含有完全不饱和多异戊二烯链的β-甘露糖基磷酸多聚戊烯醇(β-Man-P-Poly)作为甘露糖基供体的效率仅为β-[³H]Man-P-Dol的50%。当比较β-[³H]-Man-P-Dol和α-[³H]Man-P-Dol作为底物时,GPIMT-I对含有β-甘露糖基-磷酸键的甘露脂表现出严格的立体特异性。含有11或19个异戊二烯单位的β-[³H]Man-P-多萜醇是GPIMT-I同样有效的底物。Lec 9是一个CHO突变体,显然缺乏多聚戊烯醇还原酶活性,合成的β-Man-P-Dol很少,但积累β-Man-P-Poly,当它在体外与β-[³H]Man-P-Dol一起孵育时,未合成可检测到的Man-GlcN-αPI。这种间接分析表明GlcN-αPI在Lec 9细胞中不积累,可能是因为它通过β-Man-P-Poly进行甘露糖基化,或者也许是该突变体在体内形成的少量Man-P-Dol所致。(摘要截断于250字)

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