ORGANIZATION OF LH RECEPTORS ON HORMONE RESPONSIVE CELLS

激素反应细胞上 LH 受体的组织

• 批准号: 2673314
• 负责人: Deborah A Roess
• 金额: $ 6.57万
• 依托单位: COLORADO STATE UNIVERSITY
• 依托单位国家: 美国
• 财政年份: 1995
• 资助国家: 美国
• 起止时间: 1995-06-01 至 2000-05-31
• 项目状态: 已结题
• 来源: https://reporter.nih.gov/project-details/2673314
• 关键词: Leydig cells; biophysics; chemical aggregate; chorionic gonadotropin; cytoskeleton; diffusion; embryo /fetus tissue /cell culture; fluorescence polarization; fluorescent dye /probe; glycosylation; hormone receptor; hormone regulation /control mechanism; laboratory rat; luteinizing hormone; membrane activity; membrane proteins; molecular weight; phosphorescence; protein structure function; receptor binding; temperature; thermodynamics; thermostability; time resolved data; viscosity

Dr. Roess' research has involved the study of luteinizing hormone/chorionic gonadotropin (LH/CG) receptor organization and how this organization modulates receptor function. Her long-term goal is to better understand the role of LH/CG receptor structure in regulation of fertility and how gonadotropins may modulate LH/CG receptor functional events including G-protein interactions, receptor internalization and cAMP activation. During the award period she will examine whether gonadotropin binding causes size changes in functional LH receptor complexes as well as receptor-receptor aggregation on the membrane using biophysical techniques. These studies will use human embryonic kidney cells expressing LH/CG receptors with various C-terminal truncations that affect cAMP activation and receptor internalization. The effects of deglycosylated hCG and native hCG binding on LH/CG receptor association within the membrane will be evaluated on MA-10 cells where binding of deglycosylated hCG to the LH/CG receptor slows receptor down regulation and internalization. Then the association of non-receptor proteins including G-protein subunits and MHC class I antigen with LH/CG receptors will be explored by a photoproximity labeling technique that permits identification and isolation of proteins physically proximal to a known membrane site.

罗斯博士的研究涉及黄体生成素的研究