| First Author | Klugmann M | Year | 1997 |
| Journal | Neuron | Volume | 18 |
| Issue | 1 | Pages | 59-70 |
| PubMed ID | 9010205 | Mgi Jnum | J:38856 |
| Mgi Id | MGI:86232 | Doi | 10.1016/s0896-6273(01)80046-5 |
| Citation | Klugmann M, et al. (1997) Assembly of CNS myelin in the absence of proteolipid protein. Neuron 18(1):59-70 |
| abstractText | Two proteolipid proteins, PLP and DM20, are the major membrane components of central nervous system (CNS) myelin. Mutations of the X-linked PLP/DM20 gene cause dysmyelination in mouse and man and result in significant mortality. Here we show that mutant mice that lack expression of a targeted PLP gene fail to exhibit the known dysmyelinated phenotype. Unable to encode PLP/DM20 or PLP-related polypeptides, oligodendrocytes are still competent to myelinate CNS axons of all calibers and to assemble compacted myelin sheaths. Ultrastructurally, however, the electron-dense 'intraperiod' lines in myelin remain condensed, correlating with its reduced physical stability. This suggests that after myelin compaction, PLP forms a stabilizing membrane junction, similar to a zipper. Dysmyelination and oligodendrocyte death emerge as an epiphenomenon of other PLP mutations and have been uncoupled in the PLP null allele from the risk of premature myelin breakdown. |
