Abnormal myelination in the spinal cord of PTPα-knockout mice.
PTPα interacts with F3/contactin to form a membrane-spanning co-receptor complex to transduce extracellular signals to Fyn tyrosine kinase. As both F3 and Fyn regulate myelination, we investigated a role for PTPα in this process. Here, we report that both oligodendrocytes and neurons express PTPα that evenly distributes along myelinated axons of the spinal cord. The ablation of PTPα in vivo leads to early formation of transverse bands that are mainly constituted by F3 and Caspr along the axoglial interface. Notably, PTPα deficiency facilitates abnormal myelination and pronouncedly increases the number of non-landed oligodendrocyte loops at shortened paranodes in the spinal cord. Small axons, which are normally less myelinated, have thick myelin sheaths in the spinal cord of PTPα-null animals. Thus, PTPα may be involved in the formation of axoglial junctions and ensheathment in small axons during myelination of the spinal cord.
The Key Laboratory of Stem Cell and Regenerative Medicine; Institute of Molecular and Clinical Medicine; Kunming Medical College; Kunming, China; Institute of Neuroscience; Soochow University; Suzhou, China.
Quan-Hong
QH
Ma
Tao
T
Xiang
Zara Zhuyun
ZZ
Yang
Xu
X
Zhang
Jude
J
Taylor
Zhi-Cheng
ZC
Xiao
D000818:Animals; D051379:Mice; D018345:Mice, Knockout; D009186:Myelin Sheath / Q000378:metabolism* / Q000473:pathology*; D054630:Receptor-Like Protein Tyrosine Phosphatases, Class 4 / Q000172:deficiency* / Q000235:genetics; D013116:Spinal Cord / Q000378:metabolism* / Q000473:pathology*
C516843:Ptpra protein, mouse; D054630:Receptor-Like Protein Tyrosine Phosphatases, Class 4
Axon; Caspr; F3/contactin; Myelination; PTPÎ±