Главная Назад


Авторизация
Идентификатор пользователя / читателя
Пароль (для удалённых пользователей)
 

Вид поиска

Область поиска
Найдено в других БД
Формат представления найденных документов:
библиографическое описаниекраткийполный
Поисковый запрос: (<.>S=АНТИГЕННЫЙ ЛИГАНД<.>)
Общее количество найденных документов : 1
1.
РЖ ВИНИТИ 34 (BI39) 96.04-04К1.174

   

    Identification of the ligand-binding domains of CD22, a member of the immunoglobulin superfamily that uniquely binds a sialic acid-dependent ligand [Text] / Pablo Engel [et al.] // J. Exp. Med. - 1995. - Vol. 181, N 4. - P1581-1586 . - ISSN 0022-1007
Перевод заглавия: Выявление связанного с лигандом домена CD22, члена суперсемейства иммуноглобулинов, который уникально присоединяет зависимый от сиаловой кислоты лиганд
Аннотация: CD22 is a B cell-restricted member of the immunoglobulin (Ig) superfamily that functions as an adhesion receptor for leukocytes and erythrocytes. CD22 is unique among members of the Ig superfamily in that it has been suggested to bind a series of sialic acid-dependent ligands, potentially through different functional domains expressed by different splice variants of CD22. In this study, the epitopes identified by a large panel of function-blocking and non-function-blocking CD22 monoclonal antibodies were localized to specific Ig-like domains, revealing that all function-blocking monoclonal antibodies bound to the first and/or second Ig-like domains. Consistent with a single ligand-binding region, the two amino-terminal domains were the functional unit that mediated CD22 adhesion with lymphocytes, neutrophils, monocytes, and erythrocytes. The predominant cell surface species of CD22 was a full length 140,000 relative molecular mass seven Ig-like domain glycoprotein and a minor 130,000 relative molecular mass form lacking the fourth domain. While the two amino-terminal Ig-like domains of CD22 are structurally similar to those found in other members of the Ig superfamily involved in cell adhesion and containing an amino acid sequence motif associated with integrin recognition, site-directed mutagenesis of critical residues surrounding this motif did not disrupt CD22-mediated adhesion. These results demonstrate that the unique ligand-binding properties of CD22 are distinct from those of other members of the Ig superfamily involved in integrin-mediated cell adhesion. США, Dep. Immunol., Duke Univ. Med. Ctr., Durham, NC 27710. Библ. 21
ГРНТИ  
ВИНИТИ 341.43.29.07
Рубрики: ЛИМФОЦИТЫ B
МАРКЕР CD22

АНТИГЕННЫЙ ЛИГАНД

ОБРАЗОВАНИЕ КОМПЛЕКСА

ВЫЯВЛЕНИЕ

МОНОКЛОНАЛЬНЫЕ АНТИТЕЛА


Доп.точки доступа:
Engel, Pablo; Wagner, Norbert; Miller, Ann S.; Tedder, Thomas F.


 




© Международная Ассоциация пользователей и разработчиков электронных библиотек и новых информационных технологий
(Ассоциация ЭБНИТ)