Collagens in an adult bovine medial collateral ligament: Immunofluorescence localization by confocal microscopy reveals that type XIV collagen predominates at the ligament-bone junction
Collagens in an adult bovine medial collateral ligament: Immunofluorescence localization by confocal microscopy reveals that type XIV collagen predominates at the ligament-bone junction
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DOI：
10.1016/s0945-053x(05)80017-4
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发表时间：
1995-12-01
期刊：
影响因子：
6.9
通讯作者：
Woo, SLY
中科院分区：
文献类型：
--
作者：
Niyibizi, C;Visconti, CS;Woo, SLY
为了了解内侧副韧带的结构和功能，测定了成年牛韧带中的胶原蛋白。将韧带的中段粉碎并用4 M盐酸胍提取，并将残余物用胃蛋白酶消化以溶解胶原。I型胶原蛋白是胃蛋白酶溶解级分中回收的主要原纤维胶原蛋白，III型和V型分别占约5%和2%。VI型胶原蛋白是盐酸胍提取物中存在的主要胶原蛋白，其占提取物中蛋白质的约40%或组织干重的4%。在盐酸胍提取物中还检测到XII型和XIV型胶原作为次要组分。使用共聚焦显微镜的免疫荧光定位显示，XII型和XIV型胶原蛋白与韧带纤维网络和XIV型胶原蛋白是突出的韧带-骨交界处。这些数据强化了这些胶原蛋白与结缔组织中的I型胶原纤维网络相关的概念。鉴于韧带-骨界面处存在的高机械应力，在该连接处存在高浓度的XIV型胶原可能有助于调节该组织的生物力学特性。
To understand the structure and function of medial collateral ligament, collagens present in an adult bovine ligament were determined. The mid-section of the ligament was powdered and extracted with 4 M guanidinium hydrochloride, and the residue was digested with pepsin to solubilize the collagens. Type I collagen was the major fibril collagen recovered in the pepsin solubilized fraction, with types III and V each representing about 5% and 2%, respectively. Type VI collagen was the major collagen present in the guanidinium hydrochloride extract, and it accounted for about 40% of the proteins in the extract or 4% of the tissue dry weight. Type XII and XIV collagens were also detected in the guanadinium hydrochloride extract as minor components. Immunofluorescence localization using confocal microscopy showed that type XII and XIV collagens are associated with the ligament fibrillar network and that type XIV collagen was prominent at the ligament-bone junction. These data reinforce the notion that these collagens are associated with the type I collagen fibrillar network in connective tissues. In view of high mechanical stresses that exist at the ligament-bone interface, presence of type XIV collagen in high concentration at this junction may contribute to the modulation of the biomechanical properties of this tissue.