| First Author | Gotow T | Year | 1999 |
| Journal | Eur J Neurosci | Volume | 11 |
| Issue | 11 | Pages | 3893-903 |
| PubMed ID | 10583478 | Mgi Jnum | J:59860 |
| Mgi Id | MGI:1352230 | Doi | 10.1046/j.1460-9568.1999.00820.x |
| Citation | Gotow T, et al. (1999) Abnormal expression of neurofilament proteins in dysmyelinating axons located in the central nervous system of jimpy mutant mice. Eur J Neurosci 11(11):3893-903 |
| abstractText | Myelination in the peripheral nervous system is considered to increase the phosphorylation level of neurofilament proteins in the axon, resulting in an increase in axonal calibre. To understand the relationship between myelination and neurofilament proteins in axons, we examined jimpy mutant mice with a point mutation in the proteolipid protein gene and dysmyelination in the central nervous system. The jimpy mice exhibited a characteristic similarity in neurofilament nature to the myelin-deficient mice in the peripheral nervous system reported previously. The following novel results were obtained in the jimpy mice: dysmyelinated axons, in which the amount of non-phosphorylated neurofilament-H was drastically increased without a significant reduction of the phosphorylated form, compared with the control myelinated axons, did not suffer any decrease in their diameters. Expression levels of all neurofilament subunit proteins and their mRNAs were enhanced in the central nervous system tissue. Because the above biochemical data were obtained from the cytoskeletal fraction, at least some of the increased neurofilament-H and -M proteins appeared to be coassembled into neurofilaments but remained non-phosphorylated. Axonal neurofilaments of the jimpy were, probably due to this abnormal stoichiometry and phosphorylation state in neurofilaments, more compact and random in alignment with less prominent cross-bridges than those of the control, providing possible evidence for disturbing the axonal transport of other organelles. These results suggest that myelination regulates both the expression and phosphorylation of neurofilament proteins, and is essential for the cytoplasmic organization of myelinated axons. |
