Proliferation-dependent changes of proteoglycan metabolism in arterial smooth muscle cells.
Proliferation-dependent changes of proteoglycan metabolism in arterial smooth muscle cells.
复制标题
动脉平滑肌细胞中蛋白多糖代谢的增殖依赖性变化。
DOI：
10.1515/bchm3.1987.368.1.277
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发表时间：
1987
期刊：
影响因子：
--
通讯作者：
E. Buddecke
中科院分区：
文献类型：
--
作者：
A. Schmidt;A. Bunte;E. Buddecke
培养的动脉平滑肌细胞合成并分泌两种类型的硫酸化蛋白聚糖，称为蛋白聚糖A和蛋白聚糖B。蛋白聚糖A被表征为富含硫酸软骨素，而蛋白聚糖B被发现富含硫酸皮肤素[施密特，A. & Buddecke，E.（1985）Eur. 153，260-273]。在对数生长期，动脉平滑肌细胞纳入约3倍以上的[35 S]硫酸盐到总蛋白聚糖分泌到培养基中比没有分裂细胞。当动脉平滑肌细胞停止增殖时，[35 S]蛋白多糖A/B的比值增加。从增殖细胞和非分裂细胞分离的纯化蛋白聚糖A和B的各自分子和化学特征中未检测到差异。无论生长阶段如何，蛋白聚糖A的分子量约为280 kDa，并含有8-9个富含硫酸软骨素的侧链。蛋白聚糖B的分子量约为180 kDa，含有6-7条富含硫酸皮肤素的侧链。蛋白聚糖A和B的[35 S]甲硫氨酸标记的蛋白质核心的分子量约为48 kDa，但可通过其对单特异性抗体的特异性反应来区分。分裂细胞内吞蛋白多糖B的速率比非分裂细胞高100%。在所有生长阶段，蛋白聚糖A的内吞速率比蛋白聚糖B低10倍。
Cultured arterial smooth muscle cells synthesize and secrete two types of sulfated proteoglycans designated as proteoglycan A and proteoglycan B. Proteoglycan A has been characterized as chondroitin sulfate-rich, whereas proteoglycan B was found to be dermatan sulfate-rich [Schmidt, A. & Buddecke, E. (1985) Eur. J. Biochem. 153, 260-273]. During the logarithmic growth phase, arterial smooth muscle cells incorporated about 3 times more [35S]sulfate into the total proteoglycans secreted into the culture medium than did non-dividing cells. When arterial smooth muscle cells stopped proliferating the ratio of [35S]proteoglycan A/B increased. No differences were detected in the respective molecular and chemical characteristics of purified proteoglycans A and B isolated from both proliferating and non-dividing cells. Regardless of the growth phase proteoglycan A had a molecular mass of about 280 kDa and contained 8-9 chondroitin sulfate-rich side chains. Proteoglycan B had a molecular mass of about 180 kDa and contained 6-7 dermatan sulfate-rich side chains. The [35S]methionine-labelled protein cores of proteoglycan A and B had a molecular mass of about 48 kDa, but were distinguishable by their specific reactions to monospecific antibodies. Proliferating cells endocytosed proteoglycan B at a rate up to 100% higher than that of non-dividing cells. In all growth phases proteoglycan A was endocytosed at a 10-fold lower rate than proteoglycan B.