Rosenzweig S A, Miller L J, Jamieson J D
J Cell Biol. 1983 May;96(5):1288-97. doi: 10.1083/jcb.96.5.1288.
Using the combined approaches of affinity labeling and light and electron microscopic autoradiography, we investigated the identification and localization of cholecystokinin (CCK)-binding sites on rat pancreatic acinar cells. To define the molecular properties of the CCK-binding site, we incubated rat pancreatic plasma membranes with 125-I-CCK-33 for 15 min at 23 degrees C followed by washing and cross-linking with disuccinimidyl suberate. Specific labeling of a major Mr 85,000 component was revealed as assessed by SDS PAGE under reducing conditions and autoradiography of the dried gels. Components of Mr greater than 200,000, Mr 130,000-140,000, and, Mr 55,000 were labeled under maximal cross-linking conditions. The labeling of all components was specifically inhibited by CCK-8 in a dose-dependent manner (Kd approximately 9 nM). The Mr 85,000 component had identical electrophoretic mobilities under reducing and nonreducing conditions indicating that it likely does not contain intramolecular disulfide bonds. The larger labeled species may be cross-linked oligomers of this binding protein or complexes between it and neighboring polypeptides. For studies on the distribution of CCK-binding sites, pancreatic acini were incubated with 125I-CCK-33 (0.1 nM) in the absence or presence of CCK-8 (1 microM) for 2 or 15 min at 37 degrees C, washed, and fixed in 2% glutaraldehyde. Quantitative autoradiographic analysis indicated that approximately 60% of the total grains were located within +/- 1 HD (1 HD = 100 nm) of the lateral and basal plasmalemma with little or no labeling of the apical plasmalemma. From these data, it was estimated that each acinar cell possesses at least 5,000-10,000 CCK-binding sites on its basolateral plasmalemma. The remaining grains showed no preferential concentration over the cytoplasm or nucleus. Together, these data indicate that CCK interacts with a Mr 85,000 protein located on the basolateral plasmalemma of the pancreatic acinar cell.
我们运用亲和标记以及光镜和电镜放射自显影相结合的方法,研究了大鼠胰腺腺泡细胞上胆囊收缩素(CCK)结合位点的识别与定位。为确定CCK结合位点的分子特性,我们将大鼠胰腺质膜与125I-CCK-33在23℃孵育15分钟,随后洗涤并用辛二酸二琥珀酰亚胺酯进行交联。在还原条件下通过SDS-PAGE和干燥凝胶的放射自显影评估,发现一个主要的分子量为85,000的成分有特异性标记。在最大交联条件下,分子量大于200,000、130,000 - 140,000以及55,000的成分也被标记。所有成分的标记都被CCK-8以剂量依赖方式特异性抑制(解离常数约为9 nM)。分子量为85,000的成分在还原和非还原条件下具有相同的电泳迁移率,表明它可能不包含分子内二硫键。较大的标记物种可能是该结合蛋白的交联寡聚体或它与相邻多肽之间的复合物。为研究CCK结合位点的分布,将胰腺腺泡在37℃下于不存在或存在CCK-8(1 microM)的情况下与125I-CCK-33(0.1 nM)孵育2或15分钟,洗涤后用2%戊二醛固定。定量放射自显影分析表明,约60%的总银粒位于外侧和基底质膜的±1 HD(1 HD = 100 nm)范围内,顶端质膜几乎没有或没有标记。根据这些数据估计,每个腺泡细胞在其基底外侧质膜上至少有5,000 - 10,000个CCK结合位点。其余银粒在细胞质或细胞核上没有优先聚集。这些数据共同表明,CCK与位于胰腺腺泡细胞基底外侧质膜上的一个分子量为85,000的蛋白质相互作用。