Spiryda L B
Department of Cell Biology, Mount Sinai School of Medicine, New York, New York 10029, USA.
J Neurosci Res. 1998 Oct 15;54(2):137-46. doi: 10.1002/(SICI)1097-4547(19981015)54:2<137::AID-JNR2>3.0.CO;2-F.
Protein zero (P0) is a member of the immunoglobulin gene superfamily (IgCAM) that is expressed at high levels in myelinated vertebrates in central (fish and amphibia) and peripheral (all species) myelin. This glycoprotein is the major adhesive component of peripheral myelin, where it mediates self-adhesion of the Schwann cell plasma membrane. Although the expression of P0 is naturally limited to Schwann cells, the molecular mechanisms of P0-mediated adhesion can be considered general and "obligatory" because, when expressed in a variety of cell lines, P0 induces strong intercellular adhesion. Modeling studies, X-ray crystallographic analysis, and experimental site-directed mutagenesis have provided excellent working models for understanding how P0 mediates adhesion at the atomic level. These models remain to be experimentally tested. However, in humans, certain mutations in P0 produce dysmyelinating disease, possibly due to disruptions in the predicted P0 lattice.
零蛋白（P0）是免疫球蛋白基因超家族（IgCAM）的成员，在有髓鞘的脊椎动物的中枢（鱼类和两栖类）和外周（所有物种）髓鞘中高水平表达。这种糖蛋白是外周髓鞘的主要黏附成分，在其中介导施万细胞质膜的自身黏附。尽管P0的表达天然地局限于施万细胞，但P0介导黏附的分子机制可被认为是普遍且“必不可少的”，因为当在多种细胞系中表达时，P0会诱导强烈的细胞间黏附。建模研究、X射线晶体学分析和实验性定点诱变提供了出色的工作模型，用于理解P0如何在原子水平介导黏附。这些模型仍有待实验验证。然而，在人类中，P0的某些突变会导致脱髓鞘疾病，可能是由于预测的P0晶格受到破坏。
