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C J de Groot D Zonneveld R T de Laaf M A Dingemanse P G Mooren A F Moorman W H Lamers R Charles 《Biochimica et biophysica acta》1986,866(1):61-67
Carbamoyl-phosphate synthase gene expression is found to be primarily regulated by conditions that enhance hepatic glucocorticosteroid levels (hormone injections) and cyclic AMP levels (induction of diabetes). After birth, changes in the level of carbamoyl-phosphate synthase protein follow changes in the level of carbamoylphosphate synthase mRNA, suggesting a pretranslational control mechanism. In fetal rats, carbamoyl-phosphate synthase gene expression is regulated by the same factors as in adults. However, both the level to which carbamoyl-phosphate synthase mRNA can accumulate and the extent to which mRNA can be translated appear to be limited, indicating control mechanisms at the pretranslational and translational level. Finally, in the immediate postnatal period, a transient but pronounced decrease in the rate of degradation of carbamoyl-phosphate synthase protein may play a role in the accumulation of the enzyme. 相似文献
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Fiber-specific regulation of Ca(2+)-ATPase isoform expression by thyroid hormone in rat skeletal muscle 总被引:1,自引:0,他引:1
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José A. A. Sant''Ana Pereira Arnold De Haan Andy Wessels Antoon F. M. Moorman Anthony J. Sargeant 《The Histochemical journal》1995,27(9):715-722
Summary In the present study we report a novel histochemical method which, by sequential pre-incubations in alkaline and acidic media,
selectively differentiates muscle fibres expressing myosin heavy chain IIX, on the basis of a specific profile for myofibrillar
actomyosin ATPase (mATPase) activity. The enzyme reactions were tested for specificity by means of anti-myosin heavy chain
monoclonal antibodies, which were characterized on Western blots of muscle homogenates. Enzyme histochemical reactions with
the traditional pH buffers were compared to those of the new method and, in conjunction with the immunoreactions, used to
confirm the relationship between MyHC expression and the distinct profiles for mATPase. Imrnunohistochemical reactions demonstrated
that the new method only differentiates those fibres expressing myosin heavy chain IIX. The method revealed a continuum in
which the intermediate staining intensities corresponded to hybrid fibres expressing myosin heavy chain IIX in combination
with either the IIA or IIB forms. Quantitative histochemistry and immunohistochemistry (by image analysis), used to examine
the relationship between staining intensities for mATPase and amounts of myosin heavy chain IIX expression, revealed that
the new method discriminates well between hybrid fibres expressing variable amounts of the IIX isoform (r2 = 0.93). 相似文献
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E H Rings H A Büller P A de Boer R J Grand R K Montgomery W H Lamers R Charles A F Moorman 《FEBS letters》1992,300(2):183-187
This study describes the intracellular compartmentalization of three different mRNAs in the polarized rat fetal enterocyte. They encode proteins that are known to be localized within different regions of the epithelial cell namely (i) the apical, membrane-bound glycoprotein, lactase-phlorizin hydrolase (lactase), (ii) the mitochondrially localized enzyme, carbamoylphosphate synthetase (CPS), and (iii) the cytoplasmically localized enzyme, phosphoenolpyruvate carboxykinase (PEPCK). These mRNAs are found in close proximity to their respective protein products, i.e. the apical membrane, mitochondria and cytoplasm, respectively. The significance of these observations is twofold; (i) they indicate that mRNAs are sorted into specific domains of the cytosol of intestinal epithelial cells; and (ii) they imply the presence of two distinct pathways of mRNA targeting one that allows transport of mRNAs that are translated on ribosomes associated with the rough endoplasmic reticulum (lactase mRNA), and the other that allows sorting of mRNAs that are translated on free polysomes (CPS and PEPCK mRNA). 相似文献