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Determination of Acetylcholine Release in the Striatum of Anesthetized Rats Using In Vivo Microdialysis and a Radioimmunoassay (1991)

Kawashima, Koichiro ; Hayakawa, Toru ; Kashima, Yuko ; [et al.]

Oxford, UK : Blackwell Publishing Ltd

Journal of neurochemistry 57 (1991), S. 0

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ISSN: 1471-4159

Source: Blackwell Publishing Journal Backfiles 1879-2005

Topics: Medicine

Notes: A vertical-type in vivo microdialysis probe and a sensitive, specific radioimmunoassay (RIA) were used to study the mechanism of acetylcholine (ACh) release in the striatum of anesthetized rats. Without the use of physostigmine, a cholincsterase inhibitor, our RIA could still detect the amount of ACh present in the perfusate (5.6 ± 0.6 fmol/min, n = 16). Tetrodotoxin (1 μM) produced a significant decrease in the amount of ACh collected in the perfusate, suggesting that basal ACh determined under the present experimental conditions was related to cholinergic neural activity. Atropine (0.1–1 μM) applied topically via the dialysis probe did not affect the amount of ACh recovered in the perfusate in the absence of physostigmine. Addition of physostigmine (10 μM) to the perfusion fluid produced about a 100-fold increase in the amount of ACh collected. In the presence of physostig mine, topical administration of atropine and pirenzepine (0.01–1 μM) through a dialysis probe produced a further three-to fourfold increase in ACh output, whereas a slight increase was produced by AF-DX 116 at the highest concentration (1 μM). These results indicate that presynaptic modulation of ACh release in the striatum does not occur under basal conditions, and that presynaptic M, muscarinic receptors are involved in the modulation of ACh release when the ACh concentration is raised under certain conditions.

Type of Medium: Electronic Resource

URL: http://dx.doi.org/10.1111/j.1471-4159.1991.tb08233.x

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The rice mitochondrial nad3 gene has an extended reading frame at its 5′ end: nucleotide sequence analysis of rice trnS, nad3, and rps12 genes (1991)

Suzuki, Takeshi ; Kazama, Shigeru ; Hirai, Atsushi ; [et al.]

Springer

Current genetics 20 (1991), S. 331-337

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ISSN: 1432-0983

Keywords: Rice ; NADH dehydrogenase subunit 3 ; Mitochondrial DNA ; Ribosomal protein S12 ; tRNASer

Source: Springer Online Journal Archives 1860-2000

Topics: Biology

Notes: Summary The nucleotide sequences of the tRNASer (trnS), pseudo-tRNA, NADH dehydrogenase subunit 3 (nad3), and ribosomal protein S12 (rps12) genes from rice mitochondrial DNA (mtDNA) were determined. Both trnS and nad3 were confirmed to be single copy genes by Southern blot analysis. The nad3 and rps12 genes were arranged in tandem, and the two were co-transcribed. The order of the above four genes in rice mtDNA differed from the linear order observed for the wheat and maize genes. In rice mitochondria, the trnS and pseudo-tRNA genes were found upstream of the cytochrome c oxidase subunit I gene, instead of the nad3 and rps12 genes as observed in maize and wheat. Additionally, while the rice nad3 and rps12 genes remain paired, they too are in a different sequence environment from the wheat and maize genes. The apparent split of the two pairs of genes indicates the occurrence of a mitochondrial intramolecular recombinational event. Another peculiarity is that the sequence upstream of the translational initiation codon of the rice nad3 gene is different from that of the wheat and maize versions. The ATG initiation codon of wheat and maize nad3 is replaced by TTG in the rice nad3. A subsequent deduction of the amino acid sequence, accompanied by a primer extension analysis, indicates that the predicted rice NAD3 protein has an additional 37 amino acid residues at its N-terminus compared to the wheat and maize NAD3 proteins. cDNA sequence analysis showed no introns or the occurrence of RNA editing at the newly replaced TTG codon.