Type XI collagen isoforms in skeletal biology

描述(申请人提供)：应聘者：朱莉娅·牛津博士最近 获得了博伊西州立大学终身教职的任命。 她接受过蛋白质生物化学方面的培训，并利用生物信息学 她研究细胞外基质分子在发育和发育中的工具 疾病。环境：博伊西州立大学致力于职业生涯 科研师资的培养与学生的培养 由积极利用当前技术进行研究的教职员工进行。 该大学认识到纳入生物信息学对于 基因组学和蛋白质组学研究和培训，并大力支持这些工作， 最近的NIH布林拨款申请证明了这一点。研究项目：类型 XI胶原蛋白是软骨胶原纤维的重要组成部分。这个 异型纤维集合体与蛋白多糖成分的作用 软骨在发育过程中提供必要的生物力学特性， 并作为成体关节软骨生长。这项研究旨在确定 XI型胶原在细胞外基质中的作用机制 组装和维护组织的完整性。到目前为止，受监管的 XI型胶原纤维的生长可以用空间构型来解释 胶原纤维表面的氨基前肽对其有阻碍作用。这个 实际的机制可能更加复杂。建议的工作如下 旨在测试I(XI)胶原异构体调节 纤维直径和氨基末端结构域参与了分子 与调节细胞外基质的其他成分的相互作用 基质组装和组织完整性。CC I(XI)链可以具有附加 功能；特定异构体的表达可能指示 软骨(即永久软骨或变成骨)。了解 X1型胶原的作用机制与调节基质有关 装配和组织。这些信息可以促进理性的 具有调节过量胶原蛋白潜力的治疗剂的设计 胶原纤维的沉积和组织不良是其特征 纤维化，心脏、肾脏、肝脏、肺等主要器官的问题， 眼睛、血管和皮肤。调整组件装配的能力 细胞外基质可能在组织领域具有重要意义 工程学也是如此。研究职业生涯发展计划：眼前的职业 目标是建立一个富有成效的研究实验室，使 在发育过程中对细胞外基质领域的重大贡献 和疾病。长期目标是将研究和教学努力结合起来， 重点关注肌肉骨骼疾病和发展。把重点放在 分子相互作用将利用蛋白质生物化学、组织培养和 分子生物学。牛津博士将接受必要的培训，包括 负责任地进行研究，支持研究工作并进行教学 学生在学术环境中使用这些方法。

DESCRIPTION (provided by applicant): Candidate: Dr. Julia Oxford has recently received an appointment to a tenure track position at Boise State University. She is trained in protein biochemistry and utilizes bioinformatic tools in her research on extracellular matrix molecules in development and disease. Environment: Boise State University has a commitment to the career development of faculty in scientific research and also the training of students by faculty who are actively carrying out research using current technologes. The University recognizes the importance of the inclusion of bioinformatics for genomics and proteomics research and training and strongly supports these, demonstrated by the recent NIH BRIN grant application. Research project: Type XI collagen is an integral component of the collagen fibrils of cartilage. The heterotypic fibrillar assembly functions with the proteoglycan component of cartilage to provide the necessary biomechanical properties during development, growth and as adult articular cartilage. This research aims to determine the mechanism by which type XI collagen plays a role in extracellular matrix assembly and maintenance of tissue integrity. To date, the effect of regulated fibril growth attributed to type XI collagen has been explained by steric hindrance by the amino propeptides on the surface of collagen fibrils. The actual mechanism is likely to be more complex. The proposed efforts are designed to test the hypothesis that isoforms of an I (XI) collagen modulate fibril diameter and that the amino terminal domain is involved in molecular interactions with other components of the extracellular matrix that mediate matrix assembly and tissue integrity. The cc I (XI) chain may have additional functions; the expression of a specific isoform may indicate the fate of cartilage (i.e. permanent cartilage or to become bone). Understanding the mechanism of type X1 collagen function has relevance to regulated matrix assembly and organization. This information could facilitate the rational design of therapeutic agents with the potential to modulate excessive collagen deposition and poor organization of collagen fibrils characteristic of fibrosis, a problem in major organs such as the heart, kidney, liver, lung, eye, blood vessels and skin. The ability to modulate the assembly of the extracellular matrix could be of great significance in the field of tissue engineering as well. Research career development plan: The immediate career goal is to establish a productive research laboratory that will make significant contribution to the field of extracellular matrix in development and disease. The long term goal is to integrate research and teaching efforts, with focus on musculoskeletal disease and development. The emphasis on molecular interactions will utilize protein biochemistry, tissue culture and molecular biology. Dr. Oxford will receive necessary training, including the responsible conduct of research, to support the research effort and to teach students these methods in an academic setting.