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Title: Martentoxin, a novel K+ channel-blocking peptide: purification, cDNA and genomic cloning, and electrophysiological and pharmacological characterization
Author: Ji, YH ; Wang, WX ; Ye, JG ; He, LL ; Li, YJ ; Yan, YP ; Zhou, Z
Source: JOURNAL OF NEUROCHEMISTRY
Issued Date: 2003
Volume: 84, Issue:2, Pages:325-335
Keyword: biosensor binding assay ; Ca2+-activated K+ channels ; genomic organization ; martentoxin ; patch-clamp recording ; ACTIVATED POTASSIUM CHANNEL ; ANDROCTONUS-MAURETANICUS-MAURETANICUS ; SCORPION PANDINUS IMPERATOR ; ADRENAL CHROMAFFIN CELLS ; BUTHUS-MARTENSI ; BINDING-SITES ; BETA-SUBUNIT ; RAT-BRAIN ; VENOM ; CHARYBDOTOXIN
Subject: Biochemistry & Molecular Biology ; Neurosciences & Neurology
Corresponding Author: Ji, YH (reprint author), Chinese Acad Sci, Shanghai Inst Biol Sci, Inst Physiol, 320 Yue Yang Rd, Shanghai 200031, Peoples R China,
English Abstract: Martentoxin, a novel K+-channel-specific peptide has-been purified and characterized from the venom of the East-Asian scorpion (Buthus martensi Karsch). The whole cDNA precursor sequence suggested that martentoxin was composed of 37 residues with a unique sequence compared with other scorpion neurotoxins. The genomic DNA of martentoxin showed an additional intron situated unexpectedly in the 5' UTR region, besides one located close to the C-terminal of the signal peptide. The patch-clamp recording found that martentoxin at the applied dose of 100 nM could strongly block large-conductance Ca2+-activated K+ (BKCa) currents in adrenal medulla chromaffin cells, and BKCa currents blocked by martentoxin could be fully recovered within 30 seconds after washing, which is at least 10 times faster than recovery after charybdotoxin. Meanwhile, a biosensor binding assay showed a fast association rate and a slow dissociation rate of martentoxin binding on rat brain synaptosomes. The binding of martentoxin on rat brain synaptosomes could be inhibited regularly by charybdotoxin, and gradually by toosendanin in a concentration-dependent manner, but hot by either apamin or P03 from Buthus martensi. The results thus indicate that martentoxin is a new member in the family of K+-channel-blocking ligands.
Indexed Type: sci
Language: 英语
Content Type: 期刊论文
URI: http://ir.sibs.ac.cn/handle/331001/2031
Appears in Collections:神经所(总)_期刊论文

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Ji, YH; Wang, WX; Ye, JG; He, LL; Li, YJ; Yan, YP; Zhou, Z.Martentoxin, a novel K+ channel-blocking peptide: purification, cDNA and genomic cloning, and electrophysiological and pharmacological characterization,JOURNAL OF NEUROCHEMISTRY,2003,84(2):325-335
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