Type II collagen levels correlate with mineralization by articular cartilage vesicles.
Type II collagen levels correlate with mineralization by articular cartilage vesicles.
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DOI：
10.1002/art.24773
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发表时间：
2009-09
影响因子：
--
通讯作者：
Rosenthal, Ann K.
中科院分区：
文献类型：
--
作者：
Jubeck, Brian;Muth, Emily;Gohr, Claudia M.;Rosenthal, Ann K.
病理性矿化在骨关节炎软骨中很常见，可能由称为关节软骨囊泡 (ACV) 的细胞外细胞器介导。矛盾的是，与从正常猪软骨中分离的 ACV 相比，从患有骨关节炎的人软骨中分离的 ACV 在体外矿化效果较差。我们最近证明胶原蛋白可以调节苹果醋矿化。我们试图比较人类和猪 ACV 上的胶原蛋白和胶原蛋白受体，作为它们不同矿化行为的潜在解释。 ACV 是从老年人和年轻人以及猪的透明关节软骨中通过酶促释放的。使用蛋白质印迹法确定 ACV 上胶原蛋白 I、II、VI 和 X 以及各种胶原蛋白受体的存在。 II 型胶原蛋白通过 ELISA 进行定量。通过测量琼脂糖凝胶中分离的 ACV 和冻融软骨中原位 ACV 对 45Ca 的吸收来评估生物矿化。如前所述，与猪 ACV 相比，分离的人 ACV 对 ATP 的矿化反应较差，但在冻融软骨中的原位矿化情况类似。分离的人体内的 II 型胶原蛋白水平比猪 ACV 高 100 倍。人类 ACV 中的 II 型胶原蛋白具有高分子量。 II 型胶原蛋白的转谷氨酰胺酶交联显示出胶原酶抗性增加，这为人类 ACV 上残留胶原蛋白提供了可能的解释。人和猪 ACV 上的其他胶原蛋白和胶原蛋白受体相似。人 ACV 制剂中 II 型胶原蛋白水平较高，可能是由转谷氨酰胺酶交联增加介导的，可能导致体外分离的人 ACV 中观察到的矿化减少。
Pathologic mineralization is common in osteoarthritic cartilage and may be mediated by extracellular organelles known as articular cartilage vesicles (ACV). Paradoxically, ACVs isolated from osteoarthritic human cartilage mineralize poorly in vitro compared to those isolated from normal porcine cartilage. We recently showed that collagens regulate ACV mineralization. We sought to compare collagens and collagen receptors on human and porcine ACVs as a potential explanation of their different mineralization behaviors. ACVs were enzymatically released from old and young human and porcine hyaline articular cartilage. Western blotting was used to determine the presence of collagens I, II, VI, and X, and various collagen receptors on ACVs. Type II collagen was quantified by ELISA. Biomineralization was assessed by measuring uptake of 45Ca by isolated ACVs in agarose gels and ACVs in situ in freeze-thawed cartilage. As previously shown, isolated human ACVs mineralized poorly in response to ATP compared to porcine ACVs, but mineralized similarly in situ in freeze-thawed cartilage. Type II collagen levels were 100 fold higher in isolated human than in porcine ACVs. Type II collagen in human ACVs was of high molecular weight. Transglutaminase-crosslinking of type II collagen showed increased collagenase resistance, suggesting a possible explanation for residual collagen on human ACVs. Other collagens and collagen receptors were similar on human and porcine ACVs. Higher levels of type II collagen in human ACV preparations, perhaps mediated by increased transglutaminase crosslinking, may contribute to the decreased mineralization observed in isolated human ACVs in vitro.
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影响因子：
4.1
作者：
Alikhani, Mani;Alikhani, Zoubin;Graves, Dana T.
通讯作者：
Graves, Dana T.
影响因子：
--
作者：
Rosenthal, AK;Derfus, BA;Henry, LA
通讯作者：
Henry, LA
影响因子：
3.2
作者：
McGlashan, Susan R.;Jensen, Cynthia G.;Poole, C. Anthony
通讯作者：
Poole, C. Anthony
影响因子：
--
作者：
DERFUS, BA;RACHOW, JW;RYAN, LM
通讯作者：
RYAN, LM
影响因子：
--
作者：
Jubeck B;Gohr C;Fahey M;Muth E;Matthews M;Mattson E;Hirschmugl C;Rosenthal AK
通讯作者：
Rosenthal AK