Degranulation of Rat Cerebellum Induces Selective Variations in Gene Expression

Eliyahu, Daniel; Soreq, Hermona

doi:10.1111/j.1471-4159.1982.tb08631.x

Cited by 10 publications

(1 citation statement)

References 40 publications

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“…Polyadenylated RNA prepared from these frozen tissues induced the incorporation of [35S]methionine into TCA-insoluble protein in reticulocyte lysates. Both the yield of mRNA and its translation efficiency were lower from brain tissues than from the carcinoma, but close to the values observed using fresh rat cerebellum tissues (Soreq et al, 1982b;Eliyahu and Soreq, 1982). We therefore concluded that all the mRNA preparations were both intact and translatable.…”

Section: Resultssupporting

confidence: 82%

Expression of cholinesterase gene(s) in human brain tissues: translational evidence for multiple mRNA species.

Soreq¹,

Zevin-Sonkin²,

Razon³

1984

The EMBO Journal

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To resolve the origin(s) of the molecular heterogeneity of human nervous system cholinesterases (ChEs), we used Xenopus oocytes, which produce biologically active ChE when microinjected with unfractionated brain mRNA. The RNA was prepared from primary gliomas, meningiomas and embryonic brain, each of which expresses ChE activity with distinct substrate specificities and molecular forms. Sucrose gradient fractionation of DMSO‐denatured mRNA from these sources revealed three size classes of ChE‐inducing mRNAs, sedimenting at approximately 32S, 20S and 9S. The amounts of these different classes of ChE‐inducing mRNAs varied between the three tissue sources examined. To distinguish between ChEs produced in oocytes and having different substrate specificities, their activity was determined in the presence of selective inhibitors. Both ‘true’ (acetylcholine hydrolase, EC 3.1.1.7) and ‘pseudo’ (acylcholine acylhydrolase, EC 3.1.1.8) multimeric cholinesterase activities were found in the mRNA‐injected oocytes. Moreover, human brain mRNAs inducing ‘true’ and ‘pseudo’ ChE activities had different size distribution, indicating that different mRNAs might be translated into various types of ChEs. These findings imply that the heterogeneity of ChEs in the human nervous system is not limited to the post‐translational level, but extends to the level of mRNA.

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Section: Resultssupporting

confidence: 82%

Expression of cholinesterase gene(s) in human brain tissues: translational evidence for multiple mRNA species.

Soreq¹,

Zevin-Sonkin²,

Razon³

1984

The EMBO Journal

View full text Add to dashboard Cite

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Post-Transcriptional Regulation of Ontogenetically Modulated Proteins in the Nervous System

Soreq

1984

The Role of Cell Interactions in Early Neurogenesis

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The use of mRNA translationin vitro andin ovo followed by crossed immunoelectrophoretic autoradiography to study the biosynthesis of human cholinesterases

et al. 1986

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The synthesis of various cholinesterases in different fetal human tissues was studied using in vitro and in ovo translation of poly(A)+ RNA, followed by crossed immunoelectrophoretic autoradiography. When unfractionated poly(A)+ mRNA from fetal brain, muscle, or liver was translated in vitro, in the reticulocyte lysate cell-free system, polypeptides were synthesized which reacted with antibodies against either "true" acetylcholinesterase (acetylcholine hydrolase; EC 3.1.1.7) or "pseudo", butyrylcholinesterase (acylcholine acylhydrolase; EC 3.1.1.8). The two nascent cholinesterases could be separated by crossed immunoelectrophoresis followed by autoradiography, suggesting that acetylcholinesterase and butyrylcholinesterase are produced in all three tissues from nascent polypeptides containing different immunological domains. To examine whether the biosynthesis of cholinesterases includes posttranslational processing events, Xenopus oocytes were microinjected with mRNA from these tissues. Immunoelectrophoretic analysis of oocyte intracellular homogenates and incubation medium revealed various precipitation arcs, reflecting the synthesis and posttranslational processing of multiple forms of tissue-specific exported and intracellular acetylcholinesterase and butyrylcholinesterase. These findings demonstrate that polymorphic cholinesterases are produced from nascent polypeptide products which undergo further posttranslational processing events in a tissue-specific manner before they become mature compartmentalized cholinesterases.

show abstract

Degranulation of Rat Cerebellum Induces Selective Variations in Gene Expression

Cited by 10 publications

References 40 publications

Expression of cholinesterase gene(s) in human brain tissues: translational evidence for multiple mRNA species.

Expression of cholinesterase gene(s) in human brain tissues: translational evidence for multiple mRNA species.

Post-Transcriptional Regulation of Ontogenetically Modulated Proteins in the Nervous System

The use of mRNA translationin vitro andin ovo followed by crossed immunoelectrophoretic autoradiography to study the biosynthesis of human cholinesterases

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