more information
Search within Results:

Select All    Deselect All
 |   | 
Details
   print
  Record Links
Author (up) Chou, S.M.; Wang, H.S.; Komai, K. file  url
openurl 
  Title Colocalization of NOS and SOD1 in neurofilament accumulation within motor neurons of amyotrophic lateral sclerosis: an immunohistochemical study Type Journal Article
  Year 1996 Publication Journal of Chemical Neuroanatomy Abbreviated Journal J Chem Neuroanat  
  Volume 10 Issue 3-4 Pages 249-258  
  Keywords Amyotrophic Lateral Sclerosis/*enzymology; Citrulline/metabolism; Cyclic GMP/metabolism; Cytoplasm/metabolism; Humans; Immunohistochemistry; Motor Neurons/chemistry/*enzymology; Neurofilament Proteins/*metabolism; Nitrates/metabolism; Nitric Oxide/analysis/*metabolism; Nitrogen/metabolism; Oxidation-Reduction; Superoxide Dismutase/analysis/*metabolism; Tyrosine/metabolism  
  Abstract Peroxynitrite, formed from nitric oxide and superoxide, may affect neurofilament assembly and cause neurofilament accumulation in motoneurons. This hypothesis may reconcile the mutations of two genes: superoxide dismutase-1 in some patients with familial amyotrophic lateral sclerosis, and the gene for the heavy neurofilament in some patients with sporadic amyotrophic lateral sclerosis previously reported. We found colocalization of superoxide dismutase-1 and nitric oxide synthase in the foci of neurofilament accumulation as 'conglomerates' in upper motor neurons and 'axonal spheroids' in lower motor neurons. In addition, all the specific molecules related to the reactions, including calmodulin, 3', 5'-cyclic guanosine-monophosphate, citrulline, and nitrotyrosine were found strongly immunopositive in the site of neurofilament accumulation. Our data support the view that the neurofilament aggregates are tightly linked with superoxide dismutase-1 and nitric oxide synthase activities. Both enzymes may focally contribute to peroxynitrite formation at light neurofilament, which is rich in both tyrosine and arginine residues and hence considered as the vulnerable site for nitrotyrosine formation. Nitrotyrosine is known to inhibit phosphorylation and if it impairs phosphorylation of neurofilament subunits, either light or heavy, may alter the slow axonal transport culminating in proximo-distal accumulation of NF and slowly progressive motoneuron death.  
  Call Number Serial 1254  
Permanent link to this record
Select All    Deselect All
 |   | 
Details
   print

Save Citations: