Skip to main content

Expression of human T cell receptor-gamma delta structural forms.

Publication ,  Journal Article
Band, H; Hochstenbach, F; Parker, CM; McLean, J; Krangel, MS; Brenner, MB
Published in: J Immunol
May 15, 1989

The human TCR-gamma delta occurs in three biochemically distinct forms (forms 1, 2bc, and 2abc). A 40-kDa TCR gamma-chain is disulfide-linked to the TCR delta-chain in form 1, whereas 40-kDa or 55-kDa TCR-gamma polypeptides are noncovalently associated with the TCR delta-chain in forms 2bc and 2abc, respectively. Sequence analysis of TCR-gamma cDNA clones indicates that form 1 utilizes the C gamma 1 gene segment, whereas forms 2bc and 2abc appear to use allelic C gamma 2 gene segments containing either two copies (b and c) or three copies (a, b, and c) of the CII exon, respectively. We transfected TCR-gamma cDNA encoding form 1 or form 2abc into the MOLT-13 cell line that expresses form 2bc. The transfected TCR gamma-chains associate with the resident MOLT-13 TCR-delta, normally part of form 2bc, to yield CD3-associated TCR-gamma delta heterodimers identical to those seen on the donor cell lines (form 1 or 2abc). These transfection experiments show directly that, 1) when a single TCR-delta subunit is available, the presence or absence of disulfide linkage between TCR gamma- and TCR delta-chains is controlled by the TCR gamma-chain, and 2) the difference in the amount of N-linked carbohydrate attached to the transfected TCR-gamma proteins of form 2bc vs form 2abc is influenced by the presence or absence of CII exon copy "a" which appears to alter the secondary and/or tertiary structure of these TCR gamma-chain constant regions, thereby affecting the attachment of N-linked glycans. In contrast to the similar structure and usage of C beta 1 and C beta 2, TCR-gamma delta forms show striking differences in structure and are not equally represented in peripheral blood. Although the role of each form is unknown, it is possible that variable or joining-gene segment selection events or functional differences account for their unequal usage.

Duke Scholars

Published In

J Immunol

ISSN

0022-1767

Publication Date

May 15, 1989

Volume

142

Issue

10

Start / End Page

3627 / 3633

Location

United States

Related Subject Headings

  • Transfection
  • T-Lymphocytes
  • Structure-Activity Relationship
  • Receptors, Antigen, T-Cell
  • Peptides
  • Molecular Weight
  • Leukemia, T-Cell
  • Immunology
  • Immunoglobulin Constant Regions
  • Humans
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Band, H., Hochstenbach, F., Parker, C. M., McLean, J., Krangel, M. S., & Brenner, M. B. (1989). Expression of human T cell receptor-gamma delta structural forms. J Immunol, 142(10), 3627–3633.
Band, H., F. Hochstenbach, C. M. Parker, J. McLean, M. S. Krangel, and M. B. Brenner. “Expression of human T cell receptor-gamma delta structural forms.J Immunol 142, no. 10 (May 15, 1989): 3627–33.
Band H, Hochstenbach F, Parker CM, McLean J, Krangel MS, Brenner MB. Expression of human T cell receptor-gamma delta structural forms. J Immunol. 1989 May 15;142(10):3627–33.
Band, H., et al. “Expression of human T cell receptor-gamma delta structural forms.J Immunol, vol. 142, no. 10, May 1989, pp. 3627–33.
Band H, Hochstenbach F, Parker CM, McLean J, Krangel MS, Brenner MB. Expression of human T cell receptor-gamma delta structural forms. J Immunol. 1989 May 15;142(10):3627–3633.

Published In

J Immunol

ISSN

0022-1767

Publication Date

May 15, 1989

Volume

142

Issue

10

Start / End Page

3627 / 3633

Location

United States

Related Subject Headings

  • Transfection
  • T-Lymphocytes
  • Structure-Activity Relationship
  • Receptors, Antigen, T-Cell
  • Peptides
  • Molecular Weight
  • Leukemia, T-Cell
  • Immunology
  • Immunoglobulin Constant Regions
  • Humans