O'Dorisio M S, Shannon B T, Fleshman D J, Campolito L B
Department of Pediatrics, Ohio State University, Columbus 43205.
J Immunol. 1989 May 15;142(10):3533-6.
Specific, high affinity receptors for vasoactive intestinal peptide (VIP) have been identified on a human pre-B cell line, Nalm 6, and on a human plasma cell line, Dakiki. The single class of high affinity sites exhibited a KD of 12.6 +/- 2.9 nM for VIP in Nalm 6 cells and 9.1 +/- 2.7 nM in Dakiki plasma cells. The homologous peptides, peptide histidine methionine (PHM), growth hormone releasing factor (GHRF), and secretin were all less effective than VIP in competitively inhibiting binding of 125I-VIP to Nalm 6 and Dakiki plasma membranes. The putative receptor was characterized as a 47-kDa protein using covalent cross-linking techniques and VIP stimulated adenylate cyclase in pre-B cells. Human lymphocytes of B cell lineage thus appear to express functional VIP receptors homologous to the receptor identified in T lymphoblasts, brain, pituitary, and intestine.
已在人前B细胞系Nalm 6和人浆细胞系Dakiki上鉴定出血管活性肠肽（VIP）的特异性高亲和力受体。在Nalm 6细胞中，这类单一的高亲和力位点对VIP的解离常数（KD）为12.6±2.9 nM，在Dakiki浆细胞中为9.1±2.7 nM。同源肽，即肽组氨酸甲硫氨酸（PHM）、生长激素释放因子（GHRF）和促胰液素，在竞争性抑制125I-VIP与Nalm 6和Dakiki浆细胞膜的结合方面均不如VIP有效。使用共价交联技术将推定的受体鉴定为一种47 kDa的蛋白质，并且VIP可刺激前B细胞中的腺苷酸环化酶。因此，B细胞谱系的人淋巴细胞似乎表达了与在T淋巴母细胞、脑、垂体和肠道中鉴定出的受体同源的功能性VIP受体。
