Funk S E, Sage E H
Department of Biological Structure, University of Washington, Seattle 98195.
Proc Natl Acad Sci U S A. 1991 Apr 1;88(7):2648-52. doi: 10.1073/pnas.88.7.2648.
SPARC (secreted protein, acidic and rich in cysteine) is an extracellular, Ca2(+)-binding protein associated with cellular populations undergoing migration, proliferation, and/or differentiation. Active preparations of SPARC bind to specific components of the extracellular matrix and cause mesenchymal cells to assume a rounded phenotype. In this study we show that SPARC modulates the progression of bovine aortic endothelial cells through the cell cycle. At a concentration of 20 micrograms/ml, SPARC inhibited the incorporation of [3H]thymidine into newly synthesized DNA by approximately 70%, as compared to control cultures within 24 hr after the release from G0 phase. The effect was dose-dependent and reached greater than 90% inhibition at 30 micrograms of SPARC per ml after 24 hr. A 20-residue synthetic peptide (termed 2.1) from a non-Ca2(+)-binding, disulfide-rich domain of SPARC also exhibited a dose-dependent inhibition of [3H]thymidine uptake in endothelial cells within 24 hr after release from G0 phase. An inhibition of 50% was seen with peptide 2.1 at a 0.4 mM concentration. Peptides from other regions of the SPARC protein did not produce this effect. Maximum inhibition of [3H]thymidine uptake by SPARC and peptide 2.1 occurred during the early-to-middle G1 phase of the endothelial-cell cycle. From 0-12 hr after release from G0 phase, cells exhibited delayed entry into S phase, which normally occurred at 24 +/- 2 hr. These results were further corroborated by flow cytometry. In the presence of SPARC at 20 micrograms/ml, 72% fewer cells were in S phase after a 24-hr period; a similar, but less marked, reduction was seen with peptide 2.1. Peptide 2.1 did not cause cell rounding, whereas peptide 1.1, a highly efficient inhibitor of endothelial-cell spreading, exhibited essentially no activity with respect to cell-cycle progression. It therefore appears that the transient, inhibitory effect of SPARC on the entry of endothelial cells into S phase does not depend on the overt changes in cell shape mediated through cytoskeletal rearrangement.
SPARC(分泌性蛋白质,酸性且富含半胱氨酸)是一种细胞外的、与经历迁移、增殖和/或分化的细胞群体相关的Ca2+结合蛋白。SPARC的活性制剂可与细胞外基质的特定成分结合,并使间充质细胞呈现圆形表型。在本研究中,我们表明SPARC可调节牛主动脉内皮细胞的细胞周期进程。在从G0期释放24小时后,与对照培养物相比,在浓度为20微克/毫升时,SPARC可使[3H]胸苷掺入新合成DNA的量减少约70%。该效应呈剂量依赖性,在24小时后,当SPARC浓度为每毫升30微克时,抑制率超过90%。来自SPARC非Ca2+结合、富含二硫键结构域的一个20个残基的合成肽(称为2.1)在从G0期释放24小时后,也表现出对内皮细胞中[3H]胸苷摄取的剂量依赖性抑制作用。在浓度为0.4毫摩尔时,肽2.1的抑制率为50%。来自SPARC蛋白其他区域的肽未产生这种效应。SPARC和肽2.1对[3H]胸苷摄取的最大抑制作用发生在内皮细胞周期的早至中期G1期。从G0期释放后的0至12小时,细胞进入S期的时间延迟,S期通常在24±2小时发生。这些结果通过流式细胞术得到进一步证实。在存在20微克/毫升SPARC的情况下,24小时后处于S期的细胞减少了72%;肽2.1也有类似但不太明显的减少。肽2.1不会导致细胞变圆,而肽1.1是内皮细胞铺展的高效抑制剂,在细胞周期进程方面基本没有活性。因此,似乎SPARC对内皮细胞进入S期的短暂抑制作用并不依赖于通过细胞骨架重排介导的细胞形状的明显变化。