CARTILAGE MATRIX PROTEIN INTERACTIONS--CHANGES WITH AGE

软骨基质蛋白（CMP）是大多数软骨细胞的主要成分。 软骨 已发表的研究提供了一些信息， 组成、性质和分布。 的分离和测序。 来自鸡和人类来源的CMP基因揭示了高度的 同源性，它们都具有广泛的序列，这是共同的， 其他蛋白质的胶原结合区。 海涅格德实验室的工作， 我已经证明CMP也结合蛋白聚糖。 所以CMP可以执行 通过与这两个主要领域的互动， 软骨细胞外基质成分。 在本提案中，研究旨在确认并进一步 表征软骨中CMP的相互作用。 互动将是 研究使用体外结合方法，化学交联， 免疫组织学观察 将产生单克隆抗体， 以促进这项工作。 已知CMP的量和不溶性显著增加 随年龄 本提案的另一个目标是建立 根据这种不溶性，并确定是否CMP，像许多其他 软骨的结构分子，变得越来越碎片化， 年龄 这项研究有望增加我们对正常结构的了解， 软骨组织和随着年龄的增长发生的主要变化。

The cartilage matrix protein (CMP) is a major constituent of most cartilages. Published studies have provided some information on its composition, properties and distribution. Isolation and sequencing of the gene for CMP from chick and human sources reveals a high degree of homology, and they both possess extensive sequences which are common to a collagen-binding region of other proteins. Work from Heinegdrd's lab and mine has demonstrated that CMP also binds proteoglycan. So CMP may perform an important structural role through interactions with these two major elements of cartilage extracellular matrix. In the present proposal, studies are designed to confirm and further characterize the interactions of CMP in cartilage. Interactions will be studied using in vitro binding methods, chemical cross-linking and by immunohistological observation. Monoclonal antibodies will, be raised and characterized to facilitate this work. It is known that the amount and insolubility of CMP increases dramatically with age. An additional goal of the present proposal is to establish the basis of this insolubility, and to determine whether CMP, like many other structural molecules of cartilage, becomes increasingly fragmented with age. This study is expected to add to our knowledge of the normal structural organization of cartilage and of major changes which occur with age.