Identification of lysosomal sialidase NEU1 and plasma membrane sialidase NEU3 in human erythrocytes
Identification of lysosomal sialidase NEU1 and plasma membrane sialidase NEU3 in human erythrocytes
复制标题
DOI：
10.1002/jcb.24355
复制
发表时间：
2013-01-01
影响因子：
4
通讯作者：
Venerando, Bruno
中科院分区：
文献类型：
--
作者：
D'Avila, Francesca;Tringali, Cristina;Venerando, Bruno
从质膜突出的唾液糖蛋白和神经节苷类分子的唾液化水平调节红细胞功能的多个方面，从与内皮细胞的相互作用到细胞寿命。结果表明：(a)唾液酸酶NEU1和NEU3均存在于红细胞膜上；(b) NEU1在缺乏保护蛋白/组织蛋白酶A （PPCA）的情况下保留在质膜上；(c) NEU1和NEU3作为外周蛋白保留在质膜上，与外部小叶相关，并通过碱性处理释放；(d) NEU1和NEU3在Triton X-100耐洗涤剂膜结构域（DRMs）中分离；(e) NEU3在中性pH下也有活性；(f) NEU1和NEU3在红细胞寿命中逐渐丢失。有趣的是，碱性处理后从红细胞膜释放的唾液酸酶活性保留了其功能，并识别唾液糖蛋白和神经节苷类。另一方面，唾液酸酶在细胞膜上的弱锚定及其在红细胞生命过程中的丢失可能是保持细胞唾液酸含量的工具，以避免红细胞的早期衰老和毛细血管细胞聚集过程。j .细胞。中国生物医学工程学报，2012,31(2):481 - 481。(C) 2012 Wiley期刊公司
The sialylation level of molecules, sialoglycoproteins and gangliosides, protruding from plasma membranes regulates multiple facets of erythrocyte function, from interaction with endothelium to cell lifespan. Our results demonstrate that: (a) Both sialidases NEU1 and NEU3 are present on erythrocyte plasma membrane; (b) NEU1 is kept on the plasma membrane in absence of the protective protein/cathepsin A (PPCA); (c) NEU1 and NEU3 are retained on the plasma membrane, as peripheral proteins, associated to the external leaflet and released by alkaline treatments; (d) NEU1 and NEU3 are segregated in Triton X-100 detergent-resistant membrane domains (DRMs); (e) NEU3 shows activity also at neutral pH; and (f) NEU1 and NEU3 are progressively lost during erythrocyte life. Interestingly, sialidase activity released from erythrocyte membranes after an alkaline treatment preserves its functionality and recognizes sialoglycoproteins and gangliosides. On the other hand, the weak anchorage of sialidases to the plasma membrane and their loss during erythrocyte life could be a tool to preserve the cellular sialic acid content in order to avoid the early ageing of erythrocyte and processes of cell aggregation in the capillaries. J. Cell. Biochem. 114: 204211, 2012. (C) 2012 Wiley Periodicals, Inc.