Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:B0FTZ7 (catenin)
 18,795 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

We examined the effects of peripheral axotomy on the immunoreactivity of E-cadherin and cadherin-associated protein alpha N-catenin in the spinal cord. E-cadherin is known to be exclusively expressed in lamina II of Rexed in the spinal cord dorsal horn. This expression disappeared by day 7 after axotomy and reappeared following nerve ligature (partial axonal regeneration model) on day 63. In contrast, it remained undetectable following nerve clipping (complete degeneration model). Alpha N-catenin was diffusely stained in the gray matter, and the immunoreactivity was specifically intense in the central canal and superficial dorsal horn. The expression of alpha N-catenin in the superficial dorsal horn was similarly reduced by day 7 after axotomy, but recovered by day 63 after nerve ligature. In contrast, it remained at the reduced level after nerve clipping. The alteration of alpha N-catenin immunoreactivity showed a similar pattern consistent with that of E-cadherin. Administration of nerve growth factor (NGF) rescued the immunoreactivity of substance P, which is known to disappear after peripheral axotomy, but not influence that of both E-cadherin or alpha N-catenin. These results clearly showed that peripheral axotomy simultaneously alters the immunoreactivity of E-cadherin and alpha N-catenin in the spinal cord, suggesting a correlation in the expression of both E-cadherin and alpha N-catenin in vivo. E-cadherin-alpha N-catenin complex might be crucial for plasticity of the spinal cord dorsal horn after peripheral axotomy.
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PMID:Alteration of E-cadherin and alpha N-catenin immunoreactivity in the mouse spinal cord following peripheral axotomy. 937 Feb 28

Alpha N-catenin is a cadherin-binding protein, widely expressed in the nervous system; and it plays a crucial role in cadherin-mediated cell-cell adhesion. Here we report the effects of alpha N-catenin gene deficiency on brain morphogenesis. In addition to the previously reported phenotypes, we found that some of the axon tracts did not normally develop, in particular, axons of the anterior commissure failed to cross the midline, migrating, rather, to ectopic places. In restricted nuclei, a population of neurons was missing or their laminar arrangement was distorted. The ventricular structures were also deformed. These results indicate that alpha N-catenin has diverse roles in the organization of the central nervous system, but only in limited portions of the brain.
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PMID:Alpha N-catenin deficiency causes defects in axon migration and nuclear organization in restricted regions of the mouse brain. 1669 66