Jones P A, Scott-Burden T, Gevers W
Proc Natl Acad Sci U S A. 1979 Jan;76(1):353-7. doi: 10.1073/pnas.76.1.353.
Smooth muscle cells from rat heart secreted extracellular matrix components at high rates for many generations in culture. The matrix proteins remained anchored to the culture dish and were characterized after removal of cellular material with sodium dodecyl sulfate. Sequential enzyme digestion demonstrated the presence of at least three components, including glycoprotein(s), elastin, and collagen. Prolonged extraction of the matrix with detergent under reducing conditions solubilized a fucosylated glycoprotein having an apparent molecular weight of 250,000 and two other proteins with molecular weights of 72,000 and 45,000, respectively. Sublines derived from discrete colonies of smooth muscle cells synthesized all of the matrix components, and the proportion of collagen secreted by some sublines increased with time in culture. The biosynthesis of a mixed extracellular matrix and the relationships among the component proteins were therefore studied in one system producing milligram quantities of material.
大鼠心脏的平滑肌细胞在培养中能连续多代以高速率分泌细胞外基质成分。基质蛋白一直附着在培养皿上，在用十二烷基硫酸钠去除细胞物质后对其进行了表征。顺序酶消化表明至少存在三种成分，包括糖蛋白、弹性蛋白和胶原蛋白。在还原条件下用去污剂对基质进行长时间提取，可溶解一种表观分子量为250,000的岩藻糖基化糖蛋白以及另外两种分子量分别为72,000和45,000的蛋白质。源自平滑肌细胞离散克隆的亚系合成了所有的基质成分，并且一些亚系分泌的胶原蛋白比例随培养时间增加。因此，在一个能产生毫克量物质的系统中研究了混合细胞外基质的生物合成以及组成蛋白之间的关系。
