Tidball J G
Cell Tissue Res. 1982;222(3):635-45. doi: 10.1007/BF00213861.
Electron-microscopical autoradiography and cytochemical techniques have been used to identify the distinct and separate subcellular structures involved in the secretion of 1) procollagen, 2) dihydroxyphenylalanine (DOPA), which is a precursor of a collagen-crosslinking compound, and 3) DOPA oxidase, which converts DOPA to a putative crosslinking compound of collagen in the axial skeleton of the gorgonian coral Leptogorgia virulata. Some skeletal-protein hydrolysates contain material that co-elutes with DOPA. The data indicate that these skeletogenic cells, corticocytes, are capable of modifying the number of non-reducible, tyrosine-derived crosslinkages of collagen by the secretion of a crosslinking compound that acts extracellularly on collagen. A mechanism for a cell-mediated control of the mechanical properties of collagen is thereby presented.
1）前胶原；2）二羟基苯丙氨酸（DOPA），它是一种胶原交联化合物的前体；3）DOPA氧化酶，其在柳珊瑚Leptogorgia virulata的轴骨骼中将DOPA转化为一种假定的胶原交联化合物。一些骨骼蛋白水解产物含有与DOPA共洗脱的物质。数据表明，这些造骨细胞，即皮质细胞，能够通过分泌一种在细胞外作用于胶原的交联化合物来改变胶原中不可还原的、酪氨酸衍生的交联键数量。由此提出了一种细胞介导的胶原力学性能控制机制。
