PMID: 1954255Nov 11, 1991

Developmental expression of glycogenolytic enzymes in rabbit tissues: possible relationship to fetal lung maturation

Biochimica Et Biophysica Acta
C B NewgardJ M Johnston


Glycogen can be degraded in mammalian tissues by one of three isozymes of glycogen phosphorylase, termed muscle (M), liver (L) and brain (B) after the tissues in which they are preferentially expressed in adult animals, or by members of the family of alpha-glucosidases. In the current study, we have examined the developmental expression of these enzymes and their respective mRNAs in rabbit tissues, with particular emphasis on the developing lung, a tissue in which glycogen serves as an important source of carbon for surfactant phospholipid biosynthesis. Native gel activity assays and RNA blot hybridization analysis revealed that the B isoform of glycogen phosphorylase predominates in fetal and adult lung tissues, accompanied by a low level of expression of the M isoform. Total B and M phosphorylase activities increased during fetal lung development, with a peak at day 28 of gestation, then decreased to the adult level at term. This peak in activity coincided with the peak period of glycogen degradation in developing lung. While the increase in M isozyme activity was correlated with an increase in the level of its mRNA, B isoform mRNA showed no significant alteration during development, suggesting that the increase in B isoform ...Continue Reading


Nov 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·C B NewgardR J Fletterick
Aug 18, 1986·FEBS Letters·K NakanoR J Fletterick
Dec 1, 1986·Proceedings of the National Academy of Sciences of the United States of America·F MartiniukR Hirschhorn
Jun 1, 1966·Biochemistry·M M ApplemanE H Fischer
Jan 1, 1982·Pediatric Research·J R Bourbon, A Jost
Jan 1, 1960·Acta Anatomica·S SOROKIN
Mar 28, 2006·The Journal of Biological Chemistry·Geetha BabuShao-Cong Sun

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DNA, Double-Stranded
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