Lees S, Prostak K S, Ingle V K, Kjoller K
Bioengineering Department, Forsyth Dental Center, Boston, Massachusetts 02115.
Calcif Tissue Int. 1994 Sep;55(3):180-9. doi: 10.1007/BF00425873.
Transmission electron micrographs of fully mineralized turkey leg tendon in cross-section show the ultrastructure to be more complex than has been previously described. The mineral is divided into two regions. Needlelike-appearing crystallites fill the extrafibrillar volume whereas only platelike crystallites are found within the fibrils. When the specimen is tilted through a large angle, some of the needlelike-appearing crystallites are replaced by platelets, suggesting that the needlelike crystallites are platelets viewed on edge. If so, these platelets have their broad face roughly parallel to the fibril surface and thereby the fibril axis, where the intrafibrillar platelets are steeply inclined to the fibril axis. The projection of the intrafibrillar platelets is perpendicular to the fibril axis. The extrafibrillar volume is at least 60% of the total, the fibrils occupying 40%. More of the mineral appears to be extrafibrillar than within the fibrils. Micrographs of the mineralized tendon in thickness show both needlelike-appearing and platelet crystallites. Stereoscopic views show that the needlelike-appearing crystallites do not have a preferred orientation. From the two-dimensional Fourier transform of a selected area of the cross-sectional image, the platelike crystallites have an average dimension of 58 nm. The needlelike-appearing crystallites have an average thickness of 7 nm. The maximum length is at least 90 nm. Atomic force microscopy (AFM) of unstained, unmineralized turkey leg tendon shows collagen fibrils very much like shadow replicas of collagen in electron micrographs. AFM images of the mineralized tendon show only an occasional fibril. Mineral crystallites are not visible. Because the collagen is within the fibrils, the extrafibrillar mineral must be embedded in noncollagenous organic matter. When the tissue is demineralized, the collagen fibrils are exposed. The structure as revealed by the two modalities is a composite material in which each component is itself a composite. Determination of the properties of the mineralized tendon from the properties of its elements is more difficult than considering the tendon to be just mineral-filled collagen.
完全矿化的火鸡腿肌腱横断面的透射电子显微镜图像显示,其超微结构比之前描述的更为复杂。矿物质分为两个区域。针状微晶填充原纤维外空间,而在原纤维内仅发现板状微晶。当标本大幅倾斜时,一些针状微晶会被血小板取代,这表明针状微晶是从边缘观察到的血小板。如果是这样,这些血小板的宽面大致平行于原纤维表面,从而也平行于原纤维轴,而原纤维内的血小板则与原纤维轴呈陡峭倾斜。原纤维内血小板的投影垂直于原纤维轴。原纤维外空间至少占总体积的60%,原纤维占40%。更多的矿物质似乎位于原纤维外而非原纤维内。矿化肌腱厚度的显微镜图像显示了针状和血小板微晶。立体视图显示,针状微晶没有择优取向。从横断面图像选定区域的二维傅里叶变换可知,板状微晶的平均尺寸为58纳米。针状微晶的平均厚度为7纳米。最大长度至少为90纳米。未染色、未矿化的火鸡腿肌腱的原子力显微镜(AFM)显示,胶原纤维与电子显微镜中胶原的阴影复制品非常相似。矿化肌腱的AFM图像仅偶尔显示出纤维。矿物质微晶不可见。由于胶原蛋白在原纤维内,原纤维外的矿物质必须嵌入非胶原有机物质中。当组织脱矿时,胶原纤维就会暴露出来。这两种方式揭示的结构是一种复合材料,其中每个成分本身也是一种复合材料。从其组成元素的特性来确定矿化肌腱的特性,比将肌腱仅仅视为填充矿物质的胶原蛋白要困难得多。