Proteomic analysis of Col11a1-associated protein complexes.
Proteomic analysis of Col11a1-associated protein complexes.
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DOI：
10.1002/pmic.201100058
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发表时间：
2011-12
期刊：
影响因子：
3.4
通讯作者：
Oxford, Julia Thom
中科院分区：
文献类型：
--
作者：
Brown, Raquel J.;Mallory, Christopher;McDougal, Owen M.;Oxford, Julia Thom
软骨在生长板内的骨骼发育和关节功能中起重要作用。胶原纤维和其他细胞外基质分子之间的相互作用维持软骨的结构完整性，在胚胎发育期间协调复杂的动态事件，并有助于调节纤维形成。为了增加我们对这些事件的理解，使用亲和色谱和液相色谱/串联质谱法来鉴定通过胶原蛋白α 1（XI）的氨基末端结构域与胶原蛋白原纤维表面相互作用的蛋白质，所述胶原蛋白α 1（XI）是在软骨的异型胶原蛋白原纤维的表面处展示的蛋白质结构域。使用在高离子强度缓冲液中均质化从胎牛软骨提取的蛋白质基于对胶原α 1（XI）的氨基末端非胶原结构域的亲和力进行选择。用质谱法测定胰蛋白酶片段的氨基酸序列，用于蛋白质鉴定。细胞外基质分子和细胞蛋白被鉴定为直接或间接与胶原蛋白α 1（XI）的氨基末端结构域相互作用，包括蛋白聚糖、胶原蛋白和基质细胞分子，其中一些也在纤维形成中发挥作用，而另一些已知在维持组织完整性中起作用。这些分子相互作用的表征将提供软骨的细胞外基质分子如何相互作用以及胶原蛋白XI在原纤维形成和维持组织完整性的过程中起什么作用的更透彻的理解。这些信息将有助于组织工程和软骨再生的努力，以治疗软骨组织损伤和退化。
Cartilage plays an essential role during skeletal development within the growth plate and in articular joint function. Interactions between the collagen fibrils and other extracellular matrix molecules maintain structural integrity of cartilage, orchestrate complex dynamic events during embryonic development, and help to regulate fibrillogenesis. To increase our understanding of these events, affinity chromatography and liquid chromatography/tandem mass spectrometry were used to identify proteins that interact with the collagen fibril surface via the amino terminal domain of collagen alpha 1(XI) a protein domain that is displayed at the surface of heterotypic collagen fibrils of cartilage. Proteins extracted from fetal bovine cartilage using homogenization in high ionic strength buffer were selected based on affinity for the amino terminal noncollagenous domain of collagen alpha 1(XI). Mass spectrometry was used to determine the amino acid sequence of tryptic fragments for protein identification. Extracellular matrix molecules and cellular proteins that were identified as interacting with the amino terminal domain of collagen alpha 1(XI) directly or indirectly, included proteoglycans, collagens, and matricellular molecules, some of which also play a role in fibrillogenesis, while others are known to function in the maintenance of tissue integrity. Characterization of these molecular interactions will provide a more thorough understanding of how the extracellular matrix molecules of cartilage interact and what role collagen XI plays in the process of fibrillogenesis and maintenance of tissue integrity. Such information will aid tissue engineering and cartilage regeneration efforts to treat cartilage tissue damage and degeneration.
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影响因子：
12.3
作者：
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通讯作者：
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