[细胞对活骨和体外钙化的不依赖影响(作者译)]。

K J Münzenberg, R Dennert
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引用次数: 0

摘要

毫无疑问,胶原蛋白是骨组织钙化过程中重要的细胞外因子,但这一过程的确切性质尚不清楚。这可以通过磷灰石和胶原蛋白相应晶格距离的成核效应来解释,即,这两种物质的定向晶体过度生长,从而降低了核形成的能量,或者通过原纤维束和磷酸钙晶体之间的一致性来解释,或者通过磷酸盐与胶原蛋白阴离子位置的结合来解释,以及通过非胶原蛋白的成骨效应来解释,然而,与胶原蛋白是可分离的。由于它们的高粘度,蛋白质多糖抑制晶体的形成。然而,碱性可溶性蛋白多糖似乎在体外和活骨组织中促进钙化。甲状腺素和青霉胺破坏骨胶原的交联;这可能解释了它们对骨化的干扰作用。二膦酸盐会像无机焦磷酸盐一样,抑制磷灰石晶体的形成和溶解。然而,我们的研究表明,在体外和体内,二膦酸甲烷明显促进钙化。在体外,也可能在体内,镁抑制磷灰石晶体核的形成。我们的研究还表明,由于镁对甲状旁激素释放的抑制作用,镁也减缓了钙化骨组织的减少。
本文章由计算机程序翻译,如有差异,请以英文原文为准。
[The cell-independent influence on calcification in living bone and in vitro (author's transl)].

While there is no doubt that collagen is an important extra-cellular factor in the calcification of bone tissues, the exact nature of the process remains unclear. It has been explained in turn by the nucleation effect of corresponding lattice distances of apatite and collagen, that is, an oriented crystal overgrowth of the two substances which decreases the energy of nucleus formation, or by conformity between fibril-bundles and calciumphosphate crystal, or by the binding of phosphate to anionic positions of the collagen, as well as by the bone-forming effect of a non-collagen protein which is, however, separable from collagen. Because of their high viscosity proteo-polysaccharides inhibit crystal formation. Alkaline soluble proteo-pholysaccharides, however, appear to promote calcification in vitro and also in tissue of living bone. Lathyrogene and penicillamine impair the cross-linking in the bone collagen; this probably explains their disturbing effect on ossification. Diphosphonates would, like anorganic pyrophosphate, inhibit both the formation and dissolution of apatite crystal. Our research shows, however, that methanie-bis-phosphonate clearly promotes calcification, in vitro and in vivo. In vitro, and probably also in vivo, magnesium inhibits the formation of apatite crystal nucleus. Our research indicates moreover that magnesium also slows down the reduction of calcified bone tissue on account of its inhibiting effect on parathormone emission.

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