Fransson L A, Karlsson P, Schmidtchen A
Department of Medical and Physiological Chemistry, University of Lund, Sweden.
Biochim Biophys Acta. 1992 Nov 17;1137(3):287-97. doi: 10.1016/0167-4889(92)90149-6.
(1) We have isolated radiolabelled proteoglycans and glycosaminoglycans produced by human embryonic skin fibroblasts in the presence of (a) cycloheximide to inhibit protein synthesis or (b) brefeldin A to impede transport between the endoplasmic reticulum and the Golgi complex or (c) suramin, heparin or primaquine to interfere with internalization, recycling and degradation. Effects on glycosaminoglycan synthesis were assayed separately by using exogenous p-nitrophenyl beta-D-xylopyranoside (and [3H]galactose) or 125I-labelled p-hydroxyphenyl beta-D-xylopyranoside as initiators. (2) Inhibition of protein synthesis or blocking of transport to the Golgi complex prevented production of most of the proteoglycans with one exception: Cell-associated heparan sulphate-proteoglycan was still produced at 20% of the control level. (3) Treatment with suramin or heparin resulted in decreased deposition of proteoglycan in the pericellular matrix but increased accumulation of cell-associated proteoglycan. Primaquine blocked all proteoglycan synthesis. (4) In the presence of cycloheximide, exogenous beta-D-xyloside initiated galactosaminoglycan production. In contrast, in brefeldin A-treated cells, synthesis was completely abolished. Not even formation of the linkage-region trisaccharide could be detected. (5) These results suggest that exogenous xyloside enters the endoplasmic reticulum and is subsequently transported to the trans-Golgi complex where all further steps involved in glycosaminoglycan assembly takes place. (6) Heparan sulphate proteoglycan produced by brefeldin A-treated cells could be derived from (a) an intracellular pool of preformed core protein located to the trans-Golgi complex, or (b) resident proteoglycan that was either deglycanated/reglycanated or chain-extended. As combined treatment with suramin and brefeldin A markedly reduced cell-associated proteoglycan production, the latter possibility is favoured.
(1) 我们已分离出人类胚胎皮肤成纤维细胞在以下情况下产生的放射性标记蛋白聚糖和糖胺聚糖:(a) 用环己酰亚胺抑制蛋白质合成;(b) 用布雷菲德菌素A阻碍内质网与高尔基体复合体之间的运输;(c) 用苏拉明、肝素或伯氨喹干扰内化、再循环和降解。通过使用外源性对硝基苯基β-D-吡喃木糖苷(和[3H]半乳糖)或125I标记的对羟基苯基β-D-吡喃木糖苷作为引发剂,分别测定对糖胺聚糖合成的影响。(2) 抑制蛋白质合成或阻断向高尔基体复合体的运输可阻止大多数蛋白聚糖的产生,但有一个例外:细胞相关的硫酸乙酰肝素蛋白聚糖仍以对照水平的20%产生。(3) 用苏拉明或肝素处理导致蛋白聚糖在细胞周围基质中的沉积减少,但细胞相关蛋白聚糖的积累增加。伯氨喹阻断所有蛋白聚糖的合成。(4) 在环己酰亚胺存在下,外源性β-D-木糖苷引发半乳糖胺聚糖的产生。相反,在布雷菲德菌素A处理的细胞中,合成完全被消除。甚至连连接区三糖的形成都检测不到。(5) 这些结果表明,外源性木糖苷进入内质网,随后被运输到反式高尔基体复合体,在那里发生糖胺聚糖组装所涉及的所有进一步步骤。(6) 布雷菲德菌素A处理的细胞产生的硫酸乙酰肝素蛋白聚糖可能来源于:(a) 位于反式高尔基体复合体的预先形成的核心蛋白的细胞内池;或(b) 经过去糖基化/再糖基化或链延长的驻留蛋白聚糖。由于苏拉明和布雷菲德菌素A联合处理显著降低了细胞相关蛋白聚糖的产生,后一种可能性更大。