Lasch J, Moschner S, Sann H, Zellmer S, Koelsch R
Institute of Physiological Chemistry, Medical Faculty, Martin-Luther-University Halle, Germany.
Biol Chem. 1998 Jun;379(6):705-9. doi: 10.1515/bchm.1998.379.6.705.
The physiological function of the GPI-anchored ectoenzyme aminopeptidase P (APP) is still elusive. Most researchers suppose that this enzyme inactivates biologically active peptides like bradykinin, neuropeptide tyrosine (NPY) and others (Vanhoof et al., 1995). We demonstrate by immunohistology with a specific antibody raised in rabbits and measurement of enzymatic activity in suspensions and of confluent monolayers on microscopic coverslips ('monolayer kinetics') that APP is a cell surface enzyme (ectoenzyme) of endothelial and lymphoid cells.
糖基磷脂酰肌醇(GPI)锚定的胞外酶氨肽酶P(APP)的生理功能仍然不清楚。大多数研究人员认为,这种酶可使生物活性肽如缓激肽、神经肽Y(NPY)等失活(Vanhoof等人,1995年)。我们通过用兔制备的特异性抗体进行免疫组织化学以及测量悬浮液和显微镜盖玻片上汇合单层细胞的酶活性(“单层动力学”)证明,APP是内皮细胞和淋巴细胞的一种细胞表面酶(胞外酶)。