Lechêne de la Porte P, Abouakil N, Lafont H, Lombardo D
Biochim Biophys Acta. 1987 Aug 15;920(3):237-46. doi: 10.1016/0005-2760(87)90100-7.
Immunocytochemistry and subcellular fractionation were used to localize the cholesterol ester hydrolase in the human small intestine. A positive immunoreaction, when using antibodies directed against pancreatic cholesterol ester hydrolase, was mainly found in endocytotic vesicles. Moreover, a label by gold particles was observed in intercellular spaces where lymphatic tissue merges. No specific immunoreactivity was obtained with the mucosa when sera directed against human pancreatic chymotrypsinogen and human pancreatic lipase were used. Conventional subcellular fractionation was performed after extensive washing of enterocytes to rule out any possible contamination by pancreatic enzymes. In these conditions a bile salt-dependent cholesterol ester hydrolase activity was detected in the soluble fraction of cells. Data agree with the concept that the intestinal cholesterol ester hydrolase may have a pancreatic origin. The absorption, if any, of this enzyme by enterocytes seems specific since other pancreatic (pro)enzymes tested (lipase, chymotrypsinogen) are not detected in these cells.
采用免疫细胞化学和亚细胞分级分离法对人小肠中的胆固醇酯水解酶进行定位。使用针对胰腺胆固醇酯水解酶的抗体时，阳性免疫反应主要见于内吞小泡。此外，在淋巴组织融合的细胞间隙中观察到金颗粒标记。当使用针对人胰凝乳蛋白酶原和人胰脂肪酶的血清时，黏膜未获得特异性免疫反应。在对肠上皮细胞进行广泛洗涤以排除胰腺酶的任何可能污染后，进行了常规亚细胞分级分离。在这些条件下，在细胞的可溶性部分检测到了一种胆汁盐依赖性胆固醇酯水解酶活性。数据支持肠道胆固醇酯水解酶可能起源于胰腺的观点。肠上皮细胞对这种酶的吸收（如果有的话）似乎具有特异性，因为在这些细胞中未检测到其他测试的胰腺（前）酶（脂肪酶、胰凝乳蛋白酶原）。
