Analysis of cDNA clones specific for human T cells and the α and β chains of the T-cell receptor heterodimer from a human T-cell line

Y. Yanagi, A. Chan, B. Chin, M. Minden, T. W. Mak

Research output: Contribution to journalArticle

172 Citations (Scopus)

Abstract

We report the isolation and characterization of 19 classes of nonrearranging T cell-specific cDNA clones and two cDNA clones encoding the α and β chains of the T-cell antigen receptor from a human T-cell line, Jurkat. Results indicate that the human α-chain gene, like its β-chain counterpart, undergoes somatic rearrangement in T cells. In addition, it shows sequence homology to its β-chain counterpart and immunoglobulin, indicating that the human α chain is also a member of the immunoglobulin supergene family. Sequence comparison suggests that the α chain also may be composed of variable (V), diversity (D), joining (J), and constant (C) region gene segments. The protein deduced from the cDNA sequence has a molecular weight of 29,995 and possesses six potential N-glycosylation sites. The availability of α- and β-chain genes of the T-cell receptor from the same T-cell line provides tools to study their possible roles in recognition of antigens and major histocompatibility complex products by the human T-cell receptor.

Original languageEnglish
Pages (from-to)3430-3434
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume82
Issue number10
DOIs
Publication statusPublished - Sep 25 1985
Externally publishedYes

Fingerprint

T-Cell Antigen Receptor
Complementary DNA
Clone Cells
T-Lymphocytes
Cell Line
Immunoglobulin Subunits
T-Cell Receptor Genes
Sequence Homology
Major Histocompatibility Complex
Glycosylation
Genes
Immunoglobulins
Molecular Weight
Antigens
Proteins

All Science Journal Classification (ASJC) codes

  • General

Cite this

@article{274f2c7b1b954c31953f672f91e28023,
title = "Analysis of cDNA clones specific for human T cells and the α and β chains of the T-cell receptor heterodimer from a human T-cell line",
abstract = "We report the isolation and characterization of 19 classes of nonrearranging T cell-specific cDNA clones and two cDNA clones encoding the α and β chains of the T-cell antigen receptor from a human T-cell line, Jurkat. Results indicate that the human α-chain gene, like its β-chain counterpart, undergoes somatic rearrangement in T cells. In addition, it shows sequence homology to its β-chain counterpart and immunoglobulin, indicating that the human α chain is also a member of the immunoglobulin supergene family. Sequence comparison suggests that the α chain also may be composed of variable (V), diversity (D), joining (J), and constant (C) region gene segments. The protein deduced from the cDNA sequence has a molecular weight of 29,995 and possesses six potential N-glycosylation sites. The availability of α- and β-chain genes of the T-cell receptor from the same T-cell line provides tools to study their possible roles in recognition of antigens and major histocompatibility complex products by the human T-cell receptor.",
author = "Y. Yanagi and A. Chan and B. Chin and M. Minden and Mak, {T. W.}",
year = "1985",
month = "9",
day = "25",
doi = "10.1073/pnas.82.10.3430",
language = "English",
volume = "82",
pages = "3430--3434",
journal = "Proceedings of the National Academy of Sciences of the United States of America",
issn = "0027-8424",
number = "10",

}

TY - JOUR

T1 - Analysis of cDNA clones specific for human T cells and the α and β chains of the T-cell receptor heterodimer from a human T-cell line

AU - Yanagi, Y.

AU - Chan, A.

AU - Chin, B.

AU - Minden, M.

AU - Mak, T. W.

PY - 1985/9/25

Y1 - 1985/9/25

N2 - We report the isolation and characterization of 19 classes of nonrearranging T cell-specific cDNA clones and two cDNA clones encoding the α and β chains of the T-cell antigen receptor from a human T-cell line, Jurkat. Results indicate that the human α-chain gene, like its β-chain counterpart, undergoes somatic rearrangement in T cells. In addition, it shows sequence homology to its β-chain counterpart and immunoglobulin, indicating that the human α chain is also a member of the immunoglobulin supergene family. Sequence comparison suggests that the α chain also may be composed of variable (V), diversity (D), joining (J), and constant (C) region gene segments. The protein deduced from the cDNA sequence has a molecular weight of 29,995 and possesses six potential N-glycosylation sites. The availability of α- and β-chain genes of the T-cell receptor from the same T-cell line provides tools to study their possible roles in recognition of antigens and major histocompatibility complex products by the human T-cell receptor.

AB - We report the isolation and characterization of 19 classes of nonrearranging T cell-specific cDNA clones and two cDNA clones encoding the α and β chains of the T-cell antigen receptor from a human T-cell line, Jurkat. Results indicate that the human α-chain gene, like its β-chain counterpart, undergoes somatic rearrangement in T cells. In addition, it shows sequence homology to its β-chain counterpart and immunoglobulin, indicating that the human α chain is also a member of the immunoglobulin supergene family. Sequence comparison suggests that the α chain also may be composed of variable (V), diversity (D), joining (J), and constant (C) region gene segments. The protein deduced from the cDNA sequence has a molecular weight of 29,995 and possesses six potential N-glycosylation sites. The availability of α- and β-chain genes of the T-cell receptor from the same T-cell line provides tools to study their possible roles in recognition of antigens and major histocompatibility complex products by the human T-cell receptor.

UR - http://www.scopus.com/inward/record.url?scp=0347393051&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0347393051&partnerID=8YFLogxK

U2 - 10.1073/pnas.82.10.3430

DO - 10.1073/pnas.82.10.3430

M3 - Article

C2 - 3873654

AN - SCOPUS:0347393051

VL - 82

SP - 3430

EP - 3434

JO - Proceedings of the National Academy of Sciences of the United States of America

JF - Proceedings of the National Academy of Sciences of the United States of America

SN - 0027-8424

IS - 10

ER -