Catalogo Articoli (Spogli Riviste)

OPAC HELP

Titolo:
A single amino acid substitution in MDEG2 specifically alters desensitization of the proton-activated cation current
Autore:
Ugawa, S; Ueda, T; Minami, Y; Horimoto, M; Shimada, S;
Indirizzi:
Nagoya City Univ, Sch Med, Dept Anat 2, Mizuho Ku, Nagoya, Aichi 4678601, Japan Nagoya City Univ Nagoya Aichi Japan 4678601 Nagoya, Aichi 4678601, Japan Osaka Univ, Grad Sch Med, Dept Internal Med & Therapeut, Suita, Osaka 5650871, Japan Osaka Univ Suita Osaka Japan 5650871 erapeut, Suita, Osaka 5650871, Japan
Titolo Testata:
NEUROREPORT
fascicolo: 10, volume: 12, anno: 2001,
pagine: 2141 - 2145
SICI:
0959-4965(20010720)12:10<2141:ASAASI>2.0.ZU;2-N
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUTATIONS CAUSING NEURODEGENERATION; CAENORHABDITIS-ELEGANS; ION CHANNELS; NA+ CHANNEL; SODIUM-CHANNEL; CLONING; SUBUNIT; FAMILY; BRAIN; EXPRESSION;
Keywords:
amino acid substitution; desensitization; electrophysiology; MDEG2; Xenopus oocyte;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
17
Recensione:
Indirizzi per estratti:
Indirizzo: Ugawa, S Nagoya City Univ, Sch Med, Dept Anat 2, Mizuho Ku, 1 Kawasumi,Mizuho Cho, Nagoya, Aichi 4678601, Japan Nagoya City Univ 1 Kawasumi,Mizuho Cho Nagoya Aichi Japan 4678601
Citazione:
S. Ugawa et al., "A single amino acid substitution in MDEG2 specifically alters desensitization of the proton-activated cation current", NEUROREPORT, 12(10), 2001, pp. 2141-2145

Abstract

To clarify functional roles of MDEG2 (mammalian degenerin-2), a modulatorysubunit of proton-activated cation channels, in MDEGI/MDEG2 heteromer, we replaced the Gly481 residue in MDEG2 with cysteine or phenylalanine and characterized them electrophysiologically. Expression of MDEG1 in Xenopus oocytes elicited proton-activated cation currents that were rapidly desensitized. Co-expression of MDEG1 and MDEG2 (or MDEG2-G481C) displayed similar current traces as MDEG1 alone. In contrast, co-expression of MDEG1 and MDEG2-G481F dramatically attenuated desensitization of the proton-activated currents. Interestingly. the G481F mutation in MDEG2 did not alter other channel properties including maximal whole-cell currents, ionic selectivity. pH-sensitivity and affinity for amiloride. Thus, Gly481 in MDEG2. specifically controls inactivation process of the MDEG1/MDEG2 channel. NeuroReport 12:2141-2145 (C) 2001 Lippincott Williams & Wilkins.

ASDD Area Sistemi Dipartimentali e Documentali, Università di Bologna, Catalogo delle riviste ed altri periodici
Documento generato il 02/10/20 alle ore 01:39:46