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Yoshida, Hisahiro; Ito, Kenichi; Yoshida, Yataro

doi:10.3925/jjtc1958.29.607

Cited by 83 publications

(157 citation statements)

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“…In addition, syntaxins bind another synaptic vesicle protein, synaptotagmin [2,24,25], though the latter dissociates from the former in digitonin ( [2] and T.A. et al, unpublished observations).…”

Section: Discussionmentioning

confidence: 99%

A complex of rab3A, SNAP‐25, VAMP/synaptobrevin‐2 and syntaxins in brain presynaptic terminals

et al. 1993

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Two monoclonal antibodies (SPM-1 and SPM-2) immunoprecipitate brain N-type calcium channels. On immunoaffinity chromatography of digitonin extracts of bovine brain membranes on SPM-l-and SPM-2Sepharose, proteins of 36 (syntaxins A and B), 28 and 19 kDa are specifically retained by both columns. Here we show that the 19 and 28 kDa bands contain VAMPIsynaptobrevin-2, and rab3A/smg25A and SNAP-25, respectively. Since SPM-1 and SPM-2 recognize only syntaxins and the 28 kDa band (rab3AIsmg25A and SNAP-25), respectively, the results indicate that all these proteins form a complex. Our results suggest tight linkage between the components involved in neurotransmitter release.Rab3A/smg25A; Syntaxin; VAMP/synaptobrevin-2; SNAP-25; Neurotransmitter release

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Section: Discussionmentioning

confidence: 99%

A complex of rab3A, SNAP‐25, VAMP/synaptobrevin‐2 and syntaxins in brain presynaptic terminals

et al. 1993

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“…Cyanogen bromide activated Sepharose 4B, protein A-Sepharose CL-4B, CHAPS and wheat germ agglutinin (WGA) were from Sigma. Monoclonal antibodies against synaptotagmin (mAb 1D 12 [9]), syntaxin (mAbl0H5 [10]) and synaptophysin (mAbl71B5, kindly provided by Dr S. Fujita, Mitsubishi Kasei Institute for Life Science) and polyclonal anti-calcium channel antibodies BINt [6] and CR2 [11], were prepared as previously described. Antibodies were raised against synthetic peptides HYEQSADYYKGEE-(C) (residues 144-156 of and ,8 SNAP [12]), (C)-ANQRATKMLGSG (residues 195-206 of SNAP-25 [13]), and SATAATVPPAAPAGEGGPP-(C) (residues 2 20 of VAMP2 [14]), coupled to keyhole limpet hemocyanin.…”

Section: Methodsmentioning

confidence: 99%

Interaction of a synaptobrevin (VAMP)‐syntaxin complex with presynaptic calcium channels

et al. 1995

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“…It has been well known that hydrolysis of verdoheme to biliverdin can take place in acidic solution [11]. However, the enzymatic degradation of verdoheme to ferric biliverdin-iron chelate by HO requires O 2 and reducing equivalents [16][17][18] and both lactam oxygen atoms present in the biliverdin-iron chelate derive from molecular oxygen [19,20].…”

Section: Introductionmentioning

confidence: 99%

Electrochemical reduction of ferrous α-verdoheme in complex with heme oxygenase-1

Satō

Higashimoto

Sakamoto

et al. 2007

Journal of Inorganic Biochemistry

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The heme oxygenase (HO) reaction consists of three successive oxygenation reactions, i.e. heme to α-hydroxyheme, α-hydroxyheme to verdoheme, and verdoheme to biliverdin-iron chelate. Of these, the least understood step is the conversion of verdoheme to biliverdin-iron chelate. For the cleavage of the oxaporphyrin ring of ferrous verdoheme, involvement of a verdoheme π-neutral radical has been proposed. To probe this hypothetical mechanism in the HO reaction, we performed electrochemical reduction of ferrous verdoheme complexed with rat HO-1 under anaerobic conditions. On the basis of the electrochemical spectral changes, the midpoint potential for the oneelectron reduction of the oxaporphyrin ring of ferrous verdoheme was found to be −0.47 ± 0.01 V vs the normal hydrogen electrode (NHE). Because this potential is far lower than those of both flavins of NADPH-cytochrome P450 reductase, and of NADPH, it is concluded that the one-electron reduction of the oxaporphyrin ring of ferrous verdoheme is unlikely to occur and that the formation of the π-neutral radical cannot be the initial step in the degradation of verdoheme by HO. Rather, it appears more reasonable to consider an alternative mechanism in which binding of O 2 to the ferrous iron of verdoheme is the first step in the degradation of verdoheme.

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Untitled

Cited by 83 publications

References 0 publications

A complex of rab3A, SNAP‐25, VAMP/synaptobrevin‐2 and syntaxins in brain presynaptic terminals

A complex of rab3A, SNAP‐25, VAMP/synaptobrevin‐2 and syntaxins in brain presynaptic terminals

Interaction of a synaptobrevin (VAMP)‐syntaxin complex with presynaptic calcium channels

Electrochemical reduction of ferrous α-verdoheme in complex with heme oxygenase-1

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