Mollicone R, Gibaud A, François A, Ratcliffe M, Oriol R
Faculté de Pharmacie, Châtenay-Malabry, France.
Eur J Biochem. 1990 Jul 20;191(1):169-76. doi: 10.1111/j.1432-1033.1990.tb19107.x.
Based on the capacity to transfer alpha-L-fucose onto type-1 and type-2 synthetic blood group H and sialylated acceptors, a comparison of the alpha-3-fucosyltransferase activities of different human tissues is shown. Three distinct acceptor specificity patterns are described: (I) myeloid alpha-3-fucosyltransferase pattern, in which leukocytes and brain enzymes transfer fucose actively onto H type-2 acceptor and poorly onto sialylated N-acetyllactosamine: (II) plasma alpha-3-fucosyltransferase (EC 2.4.1.152), in which plasma and hepatocyte enzymes transfer, in addition, onto the sialylated N-acetyllactosamine; (III) Lewis alpha-3 4-fucosyltransferase (EC 2.4.1.65), in which gall-bladder kidney and milk enzymes transfer, in addition, onto type-1 acceptors. The small amount (less than 10%) of alpha-3-fucosyltransferase activity found in the plasma of an alpha-3-fucosyltransferase-deficient individual had a myeloid-type acceptor pattern, suggesting that this small proportion of the plasma enzyme is derived from leukocytes. In addition to the three acceptor specificity patterns, these enzyme activities can be differentiated by their optimum pH: 8.0-8.7 for the enzymes from myeloid cells and brain. 7.2-8.0 for liver enzymes and 6.0-7.2 for gallbladder enzymes. Milk samples had two alpha-3-fucosyltransferase activities, the Lewis or alpha-3/4-fucosyltransferase under control of the Lewis gene and an alpha-3-fucosyltransferase with plasma acceptor pattern which was independent of the control of the Lewis gene. The apparent affinity for GDP-fucose of the myeloid-like enzyme was weaker than those of the plasma and Lewis-like enzymes. The apparent affinities for H type 2 and sialylated N-acetyllactosamine were stronger for exocrine secretions as compared to the plasma and myeloid enzymes. The plasma type of alpha-3-fucosyltransferase activity was more sensitive to N-ethylmaleimide and heat inactivation than the samples with myeloid-like alpha-3-fucosyltransferase activity.
基于将α-L-岩藻糖转移至1型和2型合成血型H及唾液酸化受体的能力,展示了不同人体组织的α-3-岩藻糖基转移酶活性的比较。描述了三种不同的受体特异性模式:(I)髓样α-3-岩藻糖基转移酶模式,其中白细胞和脑酶能将岩藻糖积极转移至H 2型受体,而转移至唾液酸化N-乙酰乳糖胺的能力较差;(II)血浆α-3-岩藻糖基转移酶(EC 2.4.1.152),其中血浆和肝细胞酶还能转移至唾液酸化N-乙酰乳糖胺;(III)Lewisα-3,4-岩藻糖基转移酶(EC 2.4.1.65),其中胆囊、肾脏和乳汁中的酶还能转移至1型受体。在α-3-岩藻糖基转移酶缺陷个体的血浆中发现的少量(少于10%)α-3-岩藻糖基转移酶活性具有髓样型受体模式,这表明血浆酶的这一小部分源自白细胞。除了这三种受体特异性模式外,这些酶活性还可通过其最适pH值加以区分:髓样细胞和脑来源的酶为8.0 - 8.7,肝脏酶为7.2 - 8.0,胆囊酶为6.0 - 7.2。乳汁样本有两种α-3-岩藻糖基转移酶活性,一种是受Lewis基因控制的Lewis或α-3/4-岩藻糖基转移酶,另一种是具有血浆受体模式且不受Lewis基因控制的α-3-岩藻糖基转移酶。髓样样酶对GDP-岩藻糖的表观亲和力弱于血浆和Lewis样酶。与血浆和髓样酶相比,外分泌分泌物对H 2型和唾液酸化N-乙酰乳糖胺的表观亲和力更强。血浆型α-3-岩藻糖基转移酶活性比具有髓样样α-3-岩藻糖基转移酶活性的样本对N-乙基马来酰胺和热失活更敏感。