Fc receptor-? subunits with both polar or non-polar amino acids at position of T22 are capable of restoring surface expression of the high-affinity IgE receptor and degranulation in ? subunit-deficient rat basophilic leukemia cells

Kód výsledku v IS VaVaI

<a href="https://www.isvavai.cz/riv?ss=detail&h=RIV%2F68378050%3A_____%2F13%3A00390079" target="_blank" >RIV/68378050:_____/13:00390079 - isvavai.cz</a>

Výsledek na webu

<a href="http://dx.doi.org/10.1016/j.molimm.2012.08.007" target="_blank" >http://dx.doi.org/10.1016/j.molimm.2012.08.007</a>

DOI - Digital Object Identifier

<a href="http://dx.doi.org/10.1016/j.molimm.2012.08.007" target="_blank" >10.1016/j.molimm.2012.08.007</a>

Jazyk výsledku

angličtina

Název v původním jazyce

Fc receptor-? subunits with both polar or non-polar amino acids at position of T22 are capable of restoring surface expression of the high-affinity IgE receptor and degranulation in ? subunit-deficient rat basophilic leukemia cells

Popis výsledku v původním jazyce

The high-affinity IgE receptor (Fc?RI) is formed by the IgE-binding ? subunit, ? subunit and ? subunits homodimer. All three subunits are required for proper expression of the receptor on the plasma membrane of mast cells and basophils. However, the exact molecular mechanism of inter-subunit interactions required for correct expression and function of the Fc?RI complex remains to be identified. A recent study suggested that polar aspartate at position 194 within the transmembrane domain of the ? subunitcould interact by hydrogen bonding with polar threonine at position 22 in the transmembrane domains of the ? subunits. To verify this, we used previously isolated rat basophilic leukemia (RBL)-2H3 variant cells deficient in the expression of the Fc?RI-?subunit (FcR-?), and transfected them with DNA vectors coding for FcR-? of the wild-type or mutants in which T22 was substituted for nonpolar alanine (T22A mutant) or polar serine (T22S mutant). Analysis of the transfectants showed that

Název v anglickém jazyce

Fc receptor-? subunits with both polar or non-polar amino acids at position of T22 are capable of restoring surface expression of the high-affinity IgE receptor and degranulation in ? subunit-deficient rat basophilic leukemia cells

Popis výsledku anglicky

The high-affinity IgE receptor (Fc?RI) is formed by the IgE-binding ? subunit, ? subunit and ? subunits homodimer. All three subunits are required for proper expression of the receptor on the plasma membrane of mast cells and basophils. However, the exact molecular mechanism of inter-subunit interactions required for correct expression and function of the Fc?RI complex remains to be identified. A recent study suggested that polar aspartate at position 194 within the transmembrane domain of the ? subunitcould interact by hydrogen bonding with polar threonine at position 22 in the transmembrane domains of the ? subunits. To verify this, we used previously isolated rat basophilic leukemia (RBL)-2H3 variant cells deficient in the expression of the Fc?RI-?subunit (FcR-?), and transfected them with DNA vectors coding for FcR-? of the wild-type or mutants in which T22 was substituted for nonpolar alanine (T22A mutant) or polar serine (T22S mutant). Analysis of the transfectants showed that

Druh

J_x - Nezařazeno - Článek v odborném periodiku (Jimp, Jsc a Jost)

CEP obor

EB - Genetika a molekulární biologie

OECD FORD obor

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Projekt

Výsledek vznikl pri realizaci vícero projektů. Více informací v záložce Projekty.

Návaznosti

Z - Vyzkumny zamer (s odkazem do CEZ)

Rok uplatnění

2013

Kód důvěrnosti údajů

S - Úplné a pravdivé údaje o projektu nepodléhají ochraně podle zvláštních právních předpisů

Název periodika

Molecular Immunology

ISSN

0161-5890

e-ISSN

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Svazek periodika

53

Číslo periodika v rámci svazku

3

Stát vydavatele periodika

GB - Spojené království Velké Británie a Severního Irska

Počet stran výsledku

4

Strana od-do

270-273

Kód UT WoS článku

000310822500013

EID výsledku v databázi Scopus

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