NOVEL NEURITE GROWTH-INHIBITORY PROPERTIES OF AN ASTROCYTE PROTEOGLYCAN
NOVEL NEURITE GROWTH-INHIBITORY PROPERTIES OF AN ASTROCYTE PROTEOGLYCAN
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DOI：
10.1016/0891-0618(93)90045-6
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发表时间：
1993-07-01
影响因子：
2.8
通讯作者：
RIOPELLE, RJ
中科院分区：
文献类型：
--
作者：
GUO, M;DOW, KE;RIOPELLE, RJ
条件培养基（CM）中含有硫酸软骨素/硫酸皮肤蛋白多糖（CDSPG），通过离子交换色谱法与硫酸肝素蛋白多糖（HSPG）共洗脱。用分子筛色谱法从HSPG中分离出CDSPG，结果表明HSPG的分子质量大于300 kDa， CDSPG的分子质量约为50 kDa。特异裂解酶酶切和尿素/聚丙烯酰胺凝胶电泳证实了CDSPG的均匀性，并表明核心蛋白和糖基化蛋白的分子量分别为54 kDa和58 kDa。几乎所有的聚d -赖氨酸底物结合蛋白多糖相关的星形胶质细胞CM的神经突生长促进活性都是由HSPG解释的。在聚d -赖氨酸上，相对于HSPG，固定化CDSPG表现出较少的神经突生长刺激活性。然而，CDSPG通过将HSPG从聚d -赖氨酸底物中取代而抑制了HSPG的促生长活性。生长调节蛋白与生长底物的结合度不同，细胞对生长调节蛋白产生的差异调节可能决定了完全能态神经元再生轴突反应的成功。
Conditioned medium (CM) of primary cultures of GFAP-positive adherent astrocytes from neonatal rat neocortex contained a chondroitin sulphate/dermatan sulphate proteoglycan (CDSPG) that co-eluted with a heparan sulphate proteoglycan (HSPG) by ion-exchange chromatography. The CDSPG was resolved from the HSPG by molecular sieve chromatography, which indicated that the molecular mass of the HSPG was greater than 300 kDa, while that of the CDSPG was approximately 50 kDa. Specific lyase digestion and urea/polyacrylamide gel electrophoresis established the homogeneity of the CDSPG and suggested molecular masses of the core protein and glycosylated protein as 54 kDa and 58 kDa respectively. Virtually all of the poly-D-lysine substrate-bound proteoglycan-associated neurite growth-promoting activity of astrocyte CM was accounted for by the HSPG. On poly-D-lysine the immobilized CDSPG displayed little neurite growth-stimulatory activity relative to the HSPG. However, the CDSPG inhibited the potent growth-promoting activity of the HSPG by displacing it from the poly-D-lysine substrate. Differential cellular regulation of production of growth-modulatory proteins with different binding avidity for the substrate of growth may determine the success of a regenerative axonal response by fully competent neurons.