Metz C N, Thomas P, Davitz M A
Department of Pathology, New York University Medical Center, NY 10016.
Am J Pathol. 1992 Jun;140(6):1275-81.
A large number of eukaryotic proteins have been shown to be anchored to the cell membrane by glycosylphosphatidylinositol (GPI). This glycolipid anchor can serve as a substrate for anchor-specific phospholipases that convert the GPI-anchored membrane proteins into soluble forms. Soluble forms of many GPI anchored proteins have been identified in vivo in connective tissue, plasma, and urine. The authors have discovered that mammalian plasma contains a GPI-specific phospholipase D (GPI-PLD). Because it recognizes a portion of the conserved glycan core structure, all GPI-anchored proteins are potential substrates. The authors report the development of a murine monoclonal antibody specific for one form of the human GPI-PLD and the immunohistochemical localization of this enzyme to mast cells.
大量真核生物蛋白质已被证明通过糖基磷脂酰肌醇（GPI）锚定在细胞膜上。这种糖脂锚可作为锚定特异性磷脂酶的底物，该酶能将GPI锚定的膜蛋白转化为可溶性形式。在结缔组织、血浆和尿液中已在体内鉴定出许多GPI锚定蛋白的可溶性形式。作者发现哺乳动物血浆中含有一种GPI特异性磷脂酶D（GPI-PLD）。由于它识别保守聚糖核心结构的一部分，所有GPI锚定蛋白都是潜在底物。作者报道了一种针对人GPI-PLD一种形式的鼠单克隆抗体的研制及其在肥大细胞中的免疫组化定位。
