Aring J, Schlepper-Schaefer J, Burkart V, Kolb H
Diabetes-Forschungsinstitut, Universität Düsseldorf, F.R.G.
Biochim Biophys Acta. 1989 Feb 9;1010(2):140-4. doi: 10.1016/0167-4889(89)90153-5.
The possible interaction of galactose/glucose-specific liver lectins with nonenzymatically glycated human serum albumin was analyzed. The binding activity of the asialoglycoprotein receptor on hepatocytes and of the corresponding lectin on Kupffer cells was determined using freshly isolated liver cells from Wistar rats. Nonenzymatically glucosylated or galactosylated human serum albumin (HSA) did not inhibit lectin binding in a competitive adhesion assay (less than 15% inhibition). In contrast, lactosylated HSA strongly interacted with the two liver lectins (more than 80% inhibition). Lectin binding increased with lactosylation reaching a maximum at 44-49 mol D-galactose bound per mol HSA. In conclusion, at least in certain cases, nonenzymatically glycated proteins may interact with endogenous lectins.
分析了半乳糖/葡萄糖特异性肝凝集素与非酶糖基化人血清白蛋白之间可能的相互作用。使用从Wistar大鼠新鲜分离的肝细胞，测定了肝细胞上脱唾液酸糖蛋白受体和库普弗细胞上相应凝集素的结合活性。在竞争性黏附试验中，非酶糖基化或半乳糖基化的人血清白蛋白（HSA）不抑制凝集素结合（抑制率小于15%）。相比之下，乳糖基化的HSA与两种肝凝集素强烈相互作用（抑制率超过80%）。凝集素结合随乳糖基化增加而增加，在每摩尔HSA结合44 - 49摩尔D - 半乳糖时达到最大值。总之，至少在某些情况下，非酶糖基化蛋白可能与内源性凝集素相互作用。
