The interaction of L-glutamic acid with human T lymphocytes

I. A. Kostanyan; E. V. Navolotskaya; R. I. Nurieva; V. P. Zav'yalov; V. M. Lipkin

The interaction of L-glutamic acid with human T lymphocytes

I. A. Kostanyan
, E. V. Navolotskaya
, R. I. Nurieva
, V. P. Zav'yalov
, V. M. Lipkin

Research output: Contribution to journal › Article › peer-review

Abstract

A specific interaction of [³H]Glu with T lymphocytes from the blood of healthy donors (K_d = 0.236 μM) was revealed and described. It was found that unlabeled quisqualate, a structural analogue of L-glutamic acid, and unlabeled dipeptides Ala-Glu, Glu-Ala, and Glu-Glu competitively inhibit the specific binding of [³H]Glu to T lymphocytes (with K_i 0.19, 2.4, 3.4, and 1.2 μM, respectively). Binding experiments with conjugates of labeled and unlabeled glutamic acid with dextran showed that the receptors of [³H]Glu are localized on the outer surface of the plasma membrane of T lymphocytes.

Original language	English (US)
Pages (from-to)	727-729
Number of pages	3
Journal	Russian Journal of Bioorganic Chemistry
Volume	23
Issue number	10
State	Published - Oct 1997
Externally published	Yes

Keywords

Glutamate receptors
Immune system
L-glutamic acid
T lymphocyte

ASJC Scopus subject areas

Biochemistry
Organic Chemistry

Cite this

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title = "The interaction of L-glutamic acid with human T lymphocytes",

abstract = "A specific interaction of [3H]Glu with T lymphocytes from the blood of healthy donors (Kd = 0.236 μM) was revealed and described. It was found that unlabeled quisqualate, a structural analogue of L-glutamic acid, and unlabeled dipeptides Ala-Glu, Glu-Ala, and Glu-Glu competitively inhibit the specific binding of [3H]Glu to T lymphocytes (with Ki 0.19, 2.4, 3.4, and 1.2 μM, respectively). Binding experiments with conjugates of labeled and unlabeled glutamic acid with dextran showed that the receptors of [3H]Glu are localized on the outer surface of the plasma membrane of T lymphocytes.",

keywords = "Glutamate receptors, Immune system, L-glutamic acid, T lymphocyte",

author = "Kostanyan, \{I. A.\} and Navolotskaya, \{E. V.\} and Nurieva, \{R. I.\} and Zav'yalov, \{V. P.\} and Lipkin, \{V. M.\}",

year = "1997",

month = oct,

language = "English (US)",

volume = "23",

pages = "727--729",

journal = "Russian Journal of Bioorganic Chemistry",

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T1 - The interaction of L-glutamic acid with human T lymphocytes

AU - Kostanyan, I. A.

AU - Navolotskaya, E. V.

AU - Nurieva, R. I.

AU - Zav'yalov, V. P.

AU - Lipkin, V. M.

PY - 1997/10

Y1 - 1997/10

N2 - A specific interaction of [3H]Glu with T lymphocytes from the blood of healthy donors (Kd = 0.236 μM) was revealed and described. It was found that unlabeled quisqualate, a structural analogue of L-glutamic acid, and unlabeled dipeptides Ala-Glu, Glu-Ala, and Glu-Glu competitively inhibit the specific binding of [3H]Glu to T lymphocytes (with Ki 0.19, 2.4, 3.4, and 1.2 μM, respectively). Binding experiments with conjugates of labeled and unlabeled glutamic acid with dextran showed that the receptors of [3H]Glu are localized on the outer surface of the plasma membrane of T lymphocytes.

AB - A specific interaction of [3H]Glu with T lymphocytes from the blood of healthy donors (Kd = 0.236 μM) was revealed and described. It was found that unlabeled quisqualate, a structural analogue of L-glutamic acid, and unlabeled dipeptides Ala-Glu, Glu-Ala, and Glu-Glu competitively inhibit the specific binding of [3H]Glu to T lymphocytes (with Ki 0.19, 2.4, 3.4, and 1.2 μM, respectively). Binding experiments with conjugates of labeled and unlabeled glutamic acid with dextran showed that the receptors of [3H]Glu are localized on the outer surface of the plasma membrane of T lymphocytes.

KW - Glutamate receptors

KW - Immune system

KW - L-glutamic acid

KW - T lymphocyte

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M3 - Article

AN - SCOPUS:27544449484

SN - 1068-1620

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EP - 729

JO - Russian Journal of Bioorganic Chemistry

JF - Russian Journal of Bioorganic Chemistry

IS - 10

ER -

The interaction of L-glutamic acid with human T lymphocytes

Abstract

Keywords

ASJC Scopus subject areas

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