INTERACTIONS OF FIBRONECTIN MODULES

纤连蛋白模块的相互作用

• 批准号: 2685278
• 负责人: KENNETH C. INGHAM
• 金额: $ 23.74万
• 依托单位: AMERICAN NATIONAL RED CROSS
• 依托单位国家: 美国
• 财政年份: 1978
• 资助国家: 美国
• 起止时间: 1978-01-01 至 2001-03-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2685278
• 关键词: Escherichia coli; SDS polyacrylamide gel electrophoresis; affinity chromatography; aminoacid; calorimetry; circular dichroism; crosslink; extracellular matrix; fibronectins; fluorescence; human tissue; intermolecular interaction; molecular shape; peptide chemical synthesis; polymerase chain reaction; protein structure function

Fibronectin (Fn) is a 55OkDa glycoprotein found in most body fluids and in fibrillar form in most tissues where it mediates adhesion, spreading and migration of many cell types. It plays a major role in embryogenesis, cancer, wound healing, tissue remodeling, hematopoiesis, blood coagulation and fibrinolysis. Fn also facilitates removal of damaged tissue and clot remnants from circulation by phagocytes. Many bacteria and parasites are thought to use Fn as a means of colonizing tissue. Fn is a "mosaic" protein composed of homologous modules (domains) of three different types that are also found in other proteins. The long range goal of this research is to understand the structure and function of each module in Fn, to know which ones are involved in the multiplicity of interactions and which amino acids within those modules participate directly in the recognition process. This will be accomplished by isolating ever smaller fragments by classical or recombinant techniques, characterizing their interactions and folding properties by calorimetry and fluorescence, and determining as much as possible about their structure.This application emphasizes the self- interactions that govern the supertertiary structure of Fn in solution and its transformation into an insoluble fibrillar component of the extracellular matrix. In addition we wish to continue our characterization of hetero-interactions with selected macromolecules (collagen, fibrinogen, heparin, S.aureus peptides) and to collaborate with others to elucidate the 3D structure of various fragments. The knowledge gained will provide a better understanding of the many functions of Fn and may suggest improved methods of intervention in disease processes.

纤维连接蛋白（Fn）是一种55OkDa的糖蛋白，存在于大多数体液中