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Neurosci Lett. 1999 May 14;266(3):161-4.

The developmental expression and activity of peptidylarginine deiminase in the mouse.

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Structural Biology and Biochemistry, The Hospital for Sick Children, Toronto, Ontario, Canada.


We have measured the expression and activity of peptidylarginine deiminase (PAD, EC, the enzyme responsible for converting arginyl residues in proteins to citrullines, in normal mouse brain homogenate. PAD transcripts were detected as early as five days and were maximal at one month of age. The enzyme protein was also detected at 5 days in an antibody dependent assay and was maximal at 2 months of age, 1 month later than the maximum expression of transcripts. As expected, enzyme activity had a similar developmental profile to that of the enzyme protein. In isolated mouse brain compact myelin, the activity was highest at 15 days and fell rapidly to 15% of this level by 1-2 months. In the 'loose' myelin fraction (heavy myelin) it remained at the same high level form from 15 days to 8 months. The activity in compact myelin was about 15 times greater than the activity in brain homogenate, suggesting much of the enzyme was localized to myelin.

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