Complementary distribution of carbamoylphosphate synthetase (ammonia) and glutamine synthetase in rat liver acinus is regulated at a pretranslational level. 1988

A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
Department of Anatomy and Embryology, University of Amsterdam, The Netherlands.

We studied the distribution of the mRNAs for carbamoylphosphate synthetase (ammonia) and glutamine synthetase in frozen sections of adult rat liver by in situ hybridization to [35S]-labeled cDNA probes. The density of silver grains resulting from hybridization to the labeled cDNA probe for carbamoylphosphate synthetase is highest around the portal venules, decreases towards the central venule, and is virtually absent from an area two to three cells wide that lines the central venules in which mRNA for glutamine synthetase is predominantly localized. Therefore, both mRNAs show the same complementary distribution within the liver acinus that was found for the proteins they encode, demonstrating that compartmentalization of the expression of these enzymes is controlled at a pretranslational level. In addition, we found that carbamoylphosphate synthetase mRNA is present mainly in the epithelium of the crypts of the proximal part of the small intestine, whereas carbamoylphosphate synthetase protein is present in the epithelium of both crypts and villi.

UI MeSH Term Description Entries
D008025 Ligases A class of enzymes that catalyze the formation of a bond between two substrate molecules, coupled with the hydrolysis of a pyrophosphate bond in ATP or a similar energy donor. (Dorland, 28th ed) EC 6. Ligase,Synthetases,Synthetase
D008099 Liver A large lobed glandular organ in the abdomen of vertebrates that is responsible for detoxification, metabolism, synthesis and storage of various substances. Livers
D009693 Nucleic Acid Hybridization Widely used technique which exploits the ability of complementary sequences in single-stranded DNAs or RNAs to pair with each other to form a double helix. Hybridization can take place between two complimentary DNA sequences, between a single-stranded DNA and a complementary RNA, or between two RNA sequences. The technique is used to detect and isolate specific sequences, measure homology, or define other characteristics of one or both strands. (Kendrew, Encyclopedia of Molecular Biology, 1994, p503) Genomic Hybridization,Acid Hybridization, Nucleic,Acid Hybridizations, Nucleic,Genomic Hybridizations,Hybridization, Genomic,Hybridization, Nucleic Acid,Hybridizations, Genomic,Hybridizations, Nucleic Acid,Nucleic Acid Hybridizations
D002222 Carbamoyl-Phosphate Synthase (Ammonia) An enzyme that catalyzes the formation of carbamoyl phosphate from ATP, carbon dioxide, and ammonia. This enzyme is specific for arginine biosynthesis or the urea cycle. Absence or lack of this enzyme may cause CARBAMOYL-PHOSPHATE SYNTHASE I DEFICIENCY DISEASE. EC 6.3.4.16. Carbamoyl Phosphate Synthetase I,CP Synthase I,Carbamoyl-Phosphate Synthetase (Ammonia),Carbamoyl-Phosphate Synthetase I,Carbamoylphosphate Synthetase I,Carbamyl Phosphate Synthase (Ammonia),Carbamyl-Phosphate Synthase (Ammonia),Synthase I, CP,Synthetase I, Carbamoyl-Phosphate,Synthetase I, Carbamoylphosphate
D002451 Cell Compartmentation A partitioning within cells due to the selectively permeable membranes which enclose each of the separate parts, e.g., mitochondria, lysosomes, etc. Cell Compartmentations,Compartmentation, Cell,Compartmentations, Cell
D005974 Glutamate-Ammonia Ligase An enzyme that catalyzes the conversion of ATP, L-glutamate, and NH3 to ADP, orthophosphate, and L-glutamine. It also acts more slowly on 4-methylene-L-glutamate. (From Enzyme Nomenclature, 1992) EC 6.3.1.2. Glutamine Synthetase,Glutamate Ammonia Ligase (ADP),Glutamate Ammonia Ligase,Ligase, Glutamate-Ammonia,Synthetase, Glutamine
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D012333 RNA, Messenger RNA sequences that serve as templates for protein synthesis. Bacterial mRNAs are generally primary transcripts in that they do not require post-transcriptional processing. Eukaryotic mRNA is synthesized in the nucleus and must be exported to the cytoplasm for translation. Most eukaryotic mRNAs have a sequence of polyadenylic acid at the 3' end, referred to as the poly(A) tail. The function of this tail is not known for certain, but it may play a role in the export of mature mRNA from the nucleus as well as in helping stabilize some mRNA molecules by retarding their degradation in the cytoplasm. Messenger RNA,Messenger RNA, Polyadenylated,Poly(A) Tail,Poly(A)+ RNA,Poly(A)+ mRNA,RNA, Messenger, Polyadenylated,RNA, Polyadenylated,mRNA,mRNA, Non-Polyadenylated,mRNA, Polyadenylated,Non-Polyadenylated mRNA,Poly(A) RNA,Polyadenylated mRNA,Non Polyadenylated mRNA,Polyadenylated Messenger RNA,Polyadenylated RNA,RNA, Polyadenylated Messenger,mRNA, Non Polyadenylated
D051381 Rats The common name for the genus Rattus. Rattus,Rats, Laboratory,Rats, Norway,Rattus norvegicus,Laboratory Rat,Laboratory Rats,Norway Rat,Norway Rats,Rat,Rat, Laboratory,Rat, Norway,norvegicus, Rattus

Related Publications

A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
May 1998, The Journal of nutrition,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
December 1997, Histochemistry and cell biology,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
December 1991, European journal of cell biology,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
June 1993, European journal of biochemistry,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
April 1981, The Journal of biological chemistry,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
January 1987, The journal of histochemistry and cytochemistry : official journal of the Histochemistry Society,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
February 1990, Proceedings of the National Academy of Sciences of the United States of America,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
January 2008, Cells, tissues, organs,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
November 1998, The American journal of physiology,
A F Moorman, and P A de Boer, and W J Geerts, and L van den Zande, and W H Lamers, and R Charles
January 1987, Pediatric pathology,
Copied contents to your clipboard!