Wong Y W, Low M G
Department of Physiology and Cellular Biophysics, College of Physicians and Surgeons of Columbia University, New York, NY 10032.
Clin Chem. 1992 Dec;38(12):2517-25.
Alkaline phosphatase (ALP) is attached to the cell surface in mammalian tissues via a glycosyl-phosphatidylinositol (GPI) anchor and can be released from the membrane by GPI-specific phospholipases. In a range of cultured human cell lines, however, the sensitivity of ALP to phospholipases was observed to be variable in magnitude (approximately 20-90%). The mechanism of phospholipase resistance was explored with phospholipases of different bond specificities. The results suggest that phospholipase resistance is the result of acylation of the inositol ring in the GPI anchor. The occurrence of phospholipase-resistant forms of ALP may have important implications for the in vivo release and disposition of plasma ALP.
碱性磷酸酶(ALP)在哺乳动物组织中通过糖基磷脂酰肌醇(GPI)锚定连接到细胞表面,并且可以被GPI特异性磷脂酶从膜上释放出来。然而,在一系列培养的人类细胞系中,观察到ALP对磷脂酶的敏感性在程度上存在差异(约20 - 90%)。利用具有不同键特异性的磷脂酶探究了磷脂酶抗性的机制。结果表明,磷脂酶抗性是GPI锚定中肌醇环酰化的结果。ALP的磷脂酶抗性形式的出现可能对血浆ALP的体内释放和处置具有重要意义。