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- 저자 : FFRENCH-CONSTANT, (검색결과 3 건)
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Anthony, Nicola,Rocheleau, Thomas,Mocelin, Giovani,Lee, Hwa-Jung,ffrench-Constant, Richard 梨花女子大學校 藥學硏究所 1995 藥學硏究論文集 Vol.- No.5
A degenerate PCR strategy was used to isolate a fragment of the acctylcholinesterase gene (Ace) homolog from Aedes aegypti and screen for a cDNA clone containing the complete open reading frame of the gene. The predicted amino acid sequence of the Aedes gene shares 64% identity with Ace from of Drosophila and 87% identity with the acetylcholinesterase gene from another mosquito species Anopheles stephensi. High levels of expression of the Aedes gene were achieved by infection of S/21 cells with a recombinant baculovirus containing the Aedes Ace cDNA. The catalytic properties and sensitivity of the recombinant enzyme to insecticide inhibition are described and discussed in relation to the role of insensitive AChE in conferring resistance to organophosphorus and carbamate insecticides
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LEE, H.-J.,ZHANG, H.-G.,JACKSON, M. B.,FFRENCH-CONSTANT, R. H. 梨花女子大學校 藥學硏究所 1995 藥學硏究論文集 Vol.- No.5
4'-Ethynyl-4-n-〔2,3-^3H_2〕propylbicycloorthobenzoate (〔^3H〕EBOB) is a novel radioligand for the convulsant binding site of vertebrate and invertebrate γ-aminobutyric acid (GABA) receptors. Previous studies in membranes from house fly heads have shown 〔^3H〕EBOB to have high affinity for the cyclodiene binding site, which was reduced fourfold in cyclodiene-resistant strains. Following our recent identification of single amino acid replacements in the Drosophila GABA receptor gene Rdl conferring resistance to cyclodienes, we were interested in correlating 〔^3H〕EBOB binding and physiology with specific replacements of alanine302 in Rdl. Here we report that [3H]EBOB binding is not detectable in resistant strains carrying either the resistance-associated alanine302> serine (Drosophila melanogaster or D. simulans) or the alanine302> glycine (D. simulans) replacement. Thus, despite high specific binding to membranes from susceptible flies, no binding higher than nonspecific was observed in resistant preparations. EBOB (100 nM) was also shown to functionally block GABA-gated chloride ion currents generated in insect cells infected with a recombinant susceptible Rdl baculovirus, while cells expressing constructs containing the alanine302> serine replacement showed 10-fold insensitivity to block. These results indicate that the presence of alanine302 is central to the binding of 〔^3H〕EBOB to GABA receptors containing Rdl subunits and confirm the usefulness of this radioligand for the study of this important binding site.
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ZHANG, HAI-GUANG,LEE, HWA-JUNG,ROCHELEAU, THOMAS,FFRENCH-CONSTANT, RICHARD H.,JACKSON, MEYER B. 梨花女子大學校 藥學硏究所 1997 藥學硏究論文集 Vol.- No.6
Few γ-aminobutyric acid (GABA) receptor subunits have been cioned from insects. These include Resistance to dieldrin, or Rdl, and a homologue of the vertebrate GABA_A receptor βsubunit. Unlike most vertebrate GABA_A receptor subunits, Rdl forms a highly functional homomultimeric receptor. This receptor is picrotoxin (PTX) sensitive but bicuculline (BIC) insensitive and cannot be readily classified within the known GABA_A receptor subtypes. In contrast, functional expression of the βsubunit homologue has not been reported. We report that coinfection of cells with recombinant baculoviruses containing Rdl plus βsubunits induces GABA receptors with distinct pharmacological and kinetic properties. Coinfection produces two separate receptor populations: one highly sensitive to PTX but BIC insensitive (Rdl homomultimers) and the other PTX insensitive and BIC sensitive (Rdl plus β heteromultimers). Putative Rdl plus βchannels also show reduced GABA sensitivity; slow desensitization. rapid bursting, and shorter mean open time. These studies not only localize PTX and BIC sensitivity to two distinct GABA receptor subunits but also demonstrate assembly of two highly divergent GABA receptor subunits. Furthermore, the difference in channel conductance and gating between in vivo and recombinant channels implies the existence of uncharacterized GABA receptor subunits in Drosophlia.
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