Maylié-Pfenninger M F, Jamieson J D
J Cell Biol. 1979 Jan;80(1):77-95. doi: 10.1083/jcb.80.1.77.
The surface saccharide composition of collagenase-dispersed pancreatic cells from adult guinea pig and rat glands was examined by using eight lectins and their ferritin conjugates: Concanavalin A (ConA); Lens culinaris (LCL); Lotus tetragonolobus (LTL); Ricinus communis agglutinins I and II (RCA I, RCA II); Soybean agglutinin (SBA); Ulex europeus lectin (UEL); and wheat germ agglutinin (WGA). Binding studies of iodinated lectins and lectin-ferritin conjugates both revealed one population of saturable, high-affinity receptor sites on the total cell population (approximately 95% acinar cells). Electron microscopy, however, revealed differences in lectin-ferritin binding to the plasmalemma of acinar, centroacinar, and endocrine cells. Whereas acinar cells bound heavily all lectin conjugates, endocrine and centroacinar cells were densely labeled only by ConA, LCL, WGA, and RCA I, and possessed few receptors for LTL, UEL, and SBA. Endocrine and centroacinar cells could be differentiated from each other by using RCA II, which binds to centroacinar cells but not to endocrine cells. Some RCA II receptors appeared to be glycolipids because they were extracted by ethanol and chloroform-methanol in contrast to WGA receptors which resisted solvent treatment but were partly removed by papain digestion. RCA I receptors were affected by neither treatment. The apparent absence of receptors for SBA on endocrine and centroacinar cells, and for RCA II on endocrine cells, was reversed by neuraminidase digestion, which suggested masking of lectin receptors by sialic acid. The absence of LTL and UEL receptors on endocrine and centroacinar cells was not reversed by neuraminidase. We suggest that the differential lectin-binding patterns observed on acinar, centroacinar, and endocrine cells from the adult pancreas surface-carbohydrate-developmental programs expressed during morphogenesis and cytodifferentiation of the gland.
利用8种凝集素及其铁蛋白偶联物，检测了成年豚鼠和大鼠胰腺经胶原酶分散后的细胞表面糖组成：刀豆球蛋白A（ConA）；小扁豆凝集素（LCL）；四棱豆凝集素（LTL）；蓖麻凝集素I和II（RCA I、RCA II）；大豆凝集素（SBA）；欧洲荆豆凝集素（UEL）；以及麦胚凝集素（WGA）。碘化凝集素和凝集素 - 铁蛋白偶联物的结合研究均显示，在整个细胞群体（约95%为腺泡细胞）上存在一群可饱和的高亲和力受体位点。然而，电子显微镜观察发现，凝集素 - 铁蛋白与腺泡细胞、中央腺泡细胞和内分泌细胞的质膜结合存在差异。腺泡细胞与所有凝集素偶联物结合都很强烈，而内分泌细胞和中央腺泡细胞仅被ConA、LCL、WGA和RCA I密集标记，对LTL、UEL和SBA的受体很少。通过使用RCA II可以区分内分泌细胞和中央腺泡细胞，RCA II与中央腺泡细胞结合但不与内分泌细胞结合。一些RCA II受体似乎是糖脂，因为它们可被乙醇和氯仿 - 甲醇提取，而WGA受体则能抵抗溶剂处理，但部分可被木瓜蛋白酶消化去除。RCA I受体不受这两种处理的影响。内分泌细胞和中央腺泡细胞上SBA受体以及内分泌细胞上RCA II受体的明显缺失，经神经氨酸酶消化后得以逆转，这表明唾液酸掩盖了凝集素受体。内分泌细胞和中央腺泡细胞上LTL和UEL受体的缺失未被神经氨酸酶逆转。我们认为，在成年胰腺的腺泡细胞、中央腺泡细胞和内分泌细胞上观察到的不同凝集素结合模式，反映了腺体形态发生和细胞分化过程中表面碳水化合物的发育程序。
