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Titolo:
Imidazoline receptor antisera-selected (IRAS) cDNA: Cloning and characterization
Autore:
Piletz, JE; Ivanov, TR; Sharp, JD; Ernsberger, P; Chang, CH; Pickard, RT; Gold, G; Roth, B; Zhu, H; Jones, JC; Baldwin, J; Reis, DJ;
Indirizzi:
Univ Mississippi, Med Ctr, Dept Psychiat, Div Neurobiol & Behav Res, Jackson, MS 39216 USA Univ Mississippi Jackson MS USA 39216 & Behav Res, Jackson, MS 39216 USA Univ Mississippi, Med Ctr, Dept Pharmacol & Toxicol, Jackson, MS 39216 USAUniv Mississippi Jackson MS USA 39216 ol & Toxicol, Jackson, MS 39216 USA Univ Mississippi, Med Ctr, Dept Physiol & Biophys, Jackson, MS 39216 USA Univ Mississippi Jackson MS USA 39216 ol & Biophys, Jackson, MS 39216 USA Eli Lilly & Co, Lilly Res Labs, Indianapolis, IN 46285 USA Eli Lilly & CoIndianapolis IN USA 46285 Labs, Indianapolis, IN 46285 USA Cornell Univ, Coll Med, Dept Neurol & Neurosci, New York, NY USA Cornell Univ New York NY USA d, Dept Neurol & Neurosci, New York, NY USA
Titolo Testata:
DNA AND CELL BIOLOGY
fascicolo: 6, volume: 19, anno: 2000,
pagine: 319 - 329
SICI:
1044-5498(200006)19:6<319:IRA(CC>2.0.ZU;2-9
Fonte:
ISI
Lingua:
ENG
Soggetto:
MUSCLE SARCOPLASMIC-RETICULUM; CHANNEL RYANODINE RECEPTOR; LEUCINE-RICH REPEAT; BINDING-SITES; RELEASE CHANNEL; SIGNAL-TRANSDUCTION; LIGAND-BINDING; GROWTH-FACTOR; HIGH-AFFINITY; RAT-BRAIN;
Tipo documento:
Article
Natura:
Periodico
Settore Disciplinare:
Life Sciences
Citazioni:
61
Recensione:
Indirizzi per estratti:
Indirizzo: Piletz, JE Univ Mississippi, Med Ctr, Dept Psychiat, Div Neurobiol & BehavRes, 2500 N State St, Jackson, MS 39216 USA Univ Mississippi 2500 N State St Jackson MS USA 39216 39216 USA
Citazione:
J.E. Piletz et al., "Imidazoline receptor antisera-selected (IRAS) cDNA: Cloning and characterization", DNA CELL B, 19(6), 2000, pp. 319-329

Abstract

The imidazoline-1 receptor (IR1) is considered a novel target for drug discovery. Toward cloning an IR1, a truncated cDNA clone was isolated from a human hippocampal lambda gt11 cDNA expression library by relying on the selectivity of two antisera directed against candidate IR proteins. Amplification reactions were performed to extend the 5' and 3' ends of this cDNA, followed by end-to-end PCR and conventional cloning. The resultant 5131-basepair molecule, designated imidazoline receptor-antisera-selected (IRAS) cDNA, was shown to encode a 1504-amino acid protein (IRAS-1). No relation exists between the amino acid sequence of IRAS-1 and proteins known to bind imidazolines (e.g., it is not an alpha(2)-adrenoceptor or monoamine oxidase subtype). However, certain sequences within IRAS-1 are consistent with signalingmotifs found in cytokine receptors, as previously suggested for an IR1. Anacidic region in IRAS-1 having an amino acid sequence nearly identical to that of ryanodine receptors led to the demonstration that ruthenium red, a dye that binds the acidic region in ryanodine receptors, also stained IRAS-1 as a 167-kD band on SDS gels and inhibited radioligand binding of native I-1 sites in untransfected PC-12 cells (a source of authentic I1 binding sites). Two epitope-selective antisera were also generated against IRAS-1, and both reacted with the same 167-kD band on Western blots. In a host-cell-specific manner, transfection of IRAS cDNA into Chinese hamster ovary cells led to high-affinity I1 binding sites by criteria of nanomolar affinity formoxonidine and rilmenidine. Thus, IRAS-1 is the first protein discovered with characteristics of an IR1.

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Documento generato il 10/07/20 alle ore 12:53:16