Aldecoa A, Gujer R, Fischer J A, Born W
Research Laboratory for Calcium Metabolism, Departments of Orthopaedic Surgery and Medicine, University of Zurich, Klinik Balgrist, Forchstrasse 340, 8008, Zurich, Switzerland.
FEBS Lett. 2000 Apr 14;471(2-3):156-60. doi: 10.1016/s0014-5793(00)01387-9.
Differential glycosylation of human and rat (r) calcitonin (CT) receptor-like receptors (CRLR) as a result of interactions with accessory receptor activity-modifying proteins (RAMP)1 or -2 was considered to define CT gene-related peptide (CGRP) or adrenomedullin (ADM) receptors in mammalian cells. Here, Drosophila Schneider (S2) cells stably co-expressed rCRLR and RAMP1 or -2 as functional CGRP or ADM receptors. Different from mammalian cells, rCRLR expressed in S2 cells are uniformly glycosylated proteins independent of RAMP1 or RAMP2. Bis(sulfosuccinimidyl)suberate cross-linking revealed receptor components with the size of rCRLR, increased by the molecular weights of the corresponding RAMPs and [(125)I]CGRP or [(125)I]ADM. In conclusion, [(125)I]CGRP/rCRLR/RAMP1 and [(125)I]ADM/rCRLR/RAMP2 complexes have been recognized in Drosophila S2 cells.
由于与辅助受体活性调节蛋白(RAMP)1或 -2相互作用导致的人和大鼠(r)降钙素(CT)受体样受体(CRLR)的差异糖基化,被认为可在哺乳动物细胞中定义降钙素基因相关肽(CGRP)或肾上腺髓质素(ADM)受体。在此,果蝇施奈德(S2)细胞稳定共表达rCRLR和RAMP1或 -2作为功能性CGRP或ADM受体。与哺乳动物细胞不同,S2细胞中表达的rCRLR是均匀糖基化的蛋白质,与RAMP1或RAMP2无关。双(磺基琥珀酰亚胺)辛二酸酯交联显示受体成分的大小与rCRLR相同,并因相应RAMP和[(125)I]CGRP或[(125)I]ADM的分子量而增加。总之,在果蝇S2细胞中已识别出[(125)I]CGRP/rCRLR/RAMP1和[(125)I]ADM/rCRLR/RAMP2复合物。