Plasma Membrane-Associated Glycohydrolases Activation by Extracellular Acidification due to Proton Exchangers

被引:12
作者
Aureli, Massimo [1 ]
Loberto, Nicoletta [1 ]
Bassi, Rosaria [1 ]
Ferraretto, Anita [1 ]
Perego, Silvia [1 ]
Lanteri, Patrizia [1 ]
Chigorno, Vanna [1 ]
Sonnino, Sandro [1 ]
Prinetti, Alessandro [1 ]
机构
[1] Univ Milan, Dipartimento Chim Biochim & Biotecnol Med, I-20090 Segrate, Italy
关键词
Plasma membranes; Glycoconjugates; Glycoproteins; Glycolipids; Glycohydrolases; Optimal pH; Proton modulators; CARBONIC-ANHYDRASE-IX; HUMAN-MELANOMA CELLS; INTRACELLULAR PH; SIALIDASE NEU3; HUMAN GLIOMAS; NONLYSOSOMAL GLUCOSYLCERAMIDASE; NA+/H+ EXCHANGERS; HUMAN FIBROBLASTS; N-GLYCANS; IN-VIVO;
D O I
10.1007/s11064-012-0725-1
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
In this paper, we show that the pH optimum for the plasma membrane (PM)-associated activity of four glycohydrolases (conduritol B epoxide sensitive beta-glucosidase, beta-glucosidase GBA2, beta-hexosaminidase and beta-galactosidase) measured on intact cells is acidic. Moreover, we show that drugs able to modify the efflux of protons across the PM, thus locally affecting the extracellular proton concentration close to the PM, are able to modulate the activities of these enzymes. These data strongly suggest that pH-dependent modulation of PM-associated glycohydrolases activities could be an effective way to locally modulate the cell surface glycoconjugate composition.
引用
收藏
页码:1296 / 1307
页数:12
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