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受体活性修饰蛋白(receptor activity-modifying proteins,RAMPs)属于单跨膜蛋白家族,分三个结构域,RAMP的N端和跨膜区决定本身的功能和受体表型,胞内C端对于配体的信号传导和受体循环有重要作用。目前发现有三个成员:RAMP1、RAMP2和RAMP3。RAMPs通过改变G蛋白偶联受体的糖基化,作用于配体结合区域来调节受体表型。RAMP1与降钙素受体样受体(calcitonin receptor like receptor,CRLR)结合表现出降钙素基因相关肽(calcitonin gene-related peptide,CGRP)受体表型:RAMP2和RAMP3与CRLR结合则对肾上腺髓质素(adrenomedullin,AM)表现高亲和力,与降钙素受体(calcitonin receptor,CTR)结合则作为胰淀粉样酶(amylin,AMY)受体。由此可见,RAMPs不仅调节受体与配体结合,还影响细胞内的蛋白相互作用调节细胞内信号传导来影响细胞的增殖、迁移、分化等生物学特性。RAMPs还对心血管系统的病理生理有重要调节作用。
Receptor activity-modifying proteins (RAMPs) belong to the family of transmembrane proteins divided into three domains. The N-terminal and transmembrane regions of RAMP determine their function and receptor phenotype, Ligand signaling and receptor circulation have an important role. There are currently three members found: RAMP1, RAMP2 and RAMP3. RAMPs regulate the receptor phenotype by altering the glycosylation of G protein-coupled receptors and acting on the ligand-binding domain. RAMP1 binds to calcitonin receptor like receptor (CRLR) and displays a calcitonin gene-related peptide (CGRP) receptor phenotype: RAMP2 and RAMP3 combine with CRLR to adrenal Adrenomedullin (AM) exhibits high affinity and binds to calcitonin receptor (CTR) as an amylin (AMY) receptor. Thus, RAMPs not only regulate the receptor and ligand binding, but also affect intracellular protein interactions regulate intracellular signaling to affect cell proliferation, migration, differentiation and other biological characteristics. RAMPs also have an important regulatory role on the cardiovascular system’s pathophysiology.