Proteoglycan synthesis in human erythroleukaemia (HEL) cells.
Proteoglycan synthesis in human erythroleukaemia (HEL) cells.
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人红白血病 (HEL) 细胞中的蛋白多糖合成。
DOI：
10.1042/bj2820651
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发表时间：
1992
期刊：
影响因子：
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通讯作者：
Senkowski-Richardson,S
中科院分区：
文献类型：
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作者：
Schick,BP;Senkowski-Richardson,S
比较了在对照和二甲基亚砜(DMSO)和佛波酯(PMA)刺激下培养的人红白血病(HEL)细胞硫酸蛋白多糖的合成。与对照组相比，DMSO处理的细胞合成[35S]硫酸盐标记的蛋白多糖减少了约35%，而PMA处理的细胞合成的蛋白多糖增加了3-4倍。对照组和DMSO处理的细胞分泌65%的新合成的蛋白多糖，但PMA处理的细胞分泌90%以上。琼脂糖凝胶CL-6B层析和SDS/PAGE分析表明，细胞和培养上清液中含有多种蛋白多糖。PMA处理的细胞合成了一种低MR蛋白多糖(Kav.0.3(这在对照和DMSO处理的培养中不存在。用辛基-琼脂糖层析法可将对照、DMSO处理和PMA处理的细胞和培养液中的蛋白多糖分离为三个组分。蛋白多糖对胰酶具有抵抗力，但可被Pronase和木瓜酶降解为大小类似于NaOH/NaBH4产生的糖胺聚糖的片段。糖胺聚糖的平均链长(Kav.对照的SephoseCL-6B上的0.20)被DMSO(Kav.0.25)和PMA(Kav.0.30-0.38)。软骨素ABC裂解酶消化对照培养基中的蛋白多糖产生两个核心蛋白，其Mr分别为31,000和36,000。DMSO培养基蛋白多糖只有31,000-mR的核心蛋白，而PMA培养基蛋白多糖的核心蛋白为27,000，31,000和36,000。DMSO或PMA诱导的蛋白多糖合成的变化可能与造血细胞的成熟有关。
Synthesis of sulphated proteoglycans was compared in human erythroleukaemia (HEL) cells grown under control conditions and under stimulation by dimethyl sulphoxide (DMSO) and phorbol 12-myristate 13-acetate (PMA). Synthesis of [35S]sulphate-labelled proteoglycans by DMSO-treated cells was decreased by about 35% relative to controls, but synthesis of proteoglycans by PMA-treated cells increased 3-4-fold. Control and DMSO-treated cells secreted 65% of the newly synthesized proteoglycans, but PMA-treated cells secreted more than 90%. Sepharose CL-6B chromatography and SDS/PAGE suggested the presence of several proteoglycans in the cells and culture medium. The PMA-treated cells synthesized a low-Mr proteoglycan (Kav. 0.3(that was not present in controls and DMSO-treated cultures. The proteoglycans of the cells and medium from control, DMSO-treated and PMA-treated cultures could be separated into three fractions by octyl-Sepharose chromatography. The proteoglycans were resistant to trypsin but were degraded by Pronase and papain to fragments similar in size to the NaOH/NaBH4-generated glycosaminoglycans. The average chain length of the glycosaminoglycans (Kav. 0.20 on Sepharose CL-6B for controls) was decreased by DMSO (Kav. 0.25) and by PMA (Kav. 0.30-0.38). Chondroitin ABC lyase digestion of the proteoglycans from the medium of the control cultures produced two core proteins at Mr 31,000 and 36,000. The DMSO medium proteoglycans had only the 31,000-Mr core protein, and the PMA culture medium proteoglycans had core proteins of Mr 27,000, 31,000 and 36,000. Changes in synthesis of proteoglycans induced by DMSO or PMA may have relevance for the maturation of haematopoietic cells.