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Oocyte specific regulation of PGK-1 isozyme activity in female germ cells of the mouse

Published online by Cambridge University Press:  14 April 2009

Andy McMahon
Andy McMahon
Affiliation:
MRC Mammalian Development Unit, Wolfson House (University College London), 4 Stephenson Way, London, NW1 2HE
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The expression of electrophoretic variant forms of the X-linked enzyme phosphoglycerate kinase (PGK-1) was examined during the ontogeny of the female germ-line following X-chromosome reactivation. Non-growing oocytes from foetal and neonatal ovaries of heterozygous females show a higher PGK-1A isozyme activity, a reflection of prior non-random X-inactivation favouring activity of the X-chromosome carrying the Pgk-1a allele and Xcec locus. On oocyte growth, the total PGK-1 enzyme activity increases 40–50 fold and the pattern of PGK-1 isozyme expression changes giving an electrophoretic pattern now skewed in favour of the PGK-1B isozymic form. Activity of the PGK-1B isozyme exceeds that of PGK-1A in all growing oocytes with a total activity greater than 0·075 nmol h−1 oocyte−1. Mice homozygous for either Pgk-1 allele show similar PGK-1 specific activities in somatic tissues where one X-chromosome is active, but oocytes of Pgk-lb homozygotes show a higher specific activity compared to those of Pgk-1a homozygotes. Thus increased activity of the PGK-1B isozyme relative to the PGK-1A isozyme is specific to growing oocytes.

Type
Research Article
Information
Genetics Research , Volume 42 , Issue 1 , August 1983 , pp. 77 - 89
Copyright
Copyright © Cambridge University Press 1983

References

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