• International Journal of Oral Biology
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• 제36권4호
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• pp.167-172
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• 2011

LAR-RPTP (leukocyte common antigen-related receptor protein tyrosine phosphatase) is an important regulator in the nervous system, but little is known about its expression pattern in rat trigeminal ganglion (TG) neurons. To examine whether LAR-RPTP is expressed in the TG in the current study, we sacrificed rats at 0, 7, 10 and 56 day postpartum (dpp) and a second group of rats at 3 and 5 days after an experimental tooth extraction as a TG injury model. RT-PCR was then used to determine the level of LAR-RPTP expression in the TG and immunohistology was employed to detect the subcellular localization of the protein. The mRNA expression of LAR-RPTP during the developmental stages in the TG was found to gradually increase. After experimental tooth extraction however, these transcript levels had significantly decreased at three days. LAR-RPTP protein signals in the TG were found to be cytoplasmic in the normal animals but interestingly, at five days after an experimental tooth extraction, these signals were rare. These results indicate that LAR-RPTP may be regulated during both the developmental as well as regenerative processes that take place in the TG. This further suggests that LAR-RPTP is not only involved in primary axonogenesis but possibly also in the molecular control of axons during TG repair.

• Molecules and Cells
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• 제41권7호
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• pp.622-630
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• 2018

Leukocyte common antigen-related protein tyrosine phosphatases (LAR-RPTPs) are cellular receptors of heparan sulfate (HS) and chondroitin sulfate (CS) proteoglycans that regulate neurite outgrowth and neuronal regeneration. LAR-RPTPs have also received particular attention as the major presynaptic hubs for synapse organization through selective binding to numerous postsynaptic adhesion partners. Recent structural studies on LAR-RPTP-mediated trans-synaptic adhesion complexes have provided significant insight into the molecular basis of their specific interactions, the key codes for their selective binding, as well as the higher-order clustering of LAR-RPTPs necessary for synaptogenic activity. In this review, we summarize the structures of LAR-RPTPs in complex with various postsynaptic adhesion partners and discuss the molecular mechanisms underlying LAR-RPTP-mediated synaptogenesis.