Thy-1 cDNA sequence suggests a novel regulatory mechanism

Moriuchi, Tetsuya; Chang, Hsui-Ching; Denome, Roger; Silver, Jack

doi:10.1038/301080a0

Cited by 58 publications

(39 citation statements)

References 23 publications

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“…In this context, how can the cross-linking of Thy-1 transduce a signal to the cell interior? The Thy-1 protein has been sequenced [20] and corresponding cDNA cloned [21,22]. The amino acid sequence has homology with both variable region sequences and β 2 microglobulin (β 2 m).…”

Section: The Thy-1 Molecule As An Activation Site On T Cellsmentioning

confidence: 99%

A synaptic basis for T-lymphocyte activation

Norcross

1984

Annales de l'Institut Pasteur / Immunologie

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SummaryT lymphocytes respond to foreign antigen by forming specialized junctions with antigen-presenting cells (APC) or target cells. A hypothesis is presented, illustrating the similarity between the T-cell recognition-activation process and the cell communication processes found in other organ systems, especially the nervous system. Based on data showing that a major neuronal protein, Thy-1, is also a mitogenic site on T cells, and based on predictions for the structures of the T-cell receptor (TcR) and Ia proteins, an activation model is presented as follows. 1) The T-cell receptor initiates cell-cell contact with the APC by interacting with Ia and antigen, forming an antigen-binding site. 2) Sets of adhesion molecules then bind, focusing the interacting proteins to the junctional site. One binding protein, L3/T4, binds Ia and concentrates the Ia molecules to the contact site.3) The two-chain TcR then links together the TcR-Ia-antigen complexes, forming a linear chain of receptors which will self-associate once reaching a critical length, forming a cluster. This cluster juxtaposes associated channel subunits, the T3 membrane molecules, creating an ion channel, stimulating the T cell. 4) The MHC molecule is structurally a part of this activation complex, and therefore also forms a cluster on the APC surface, possibly activating the presenting cell. 5) Secretory products are then released into the synaptic site allowing for efficient and directed cell-cell communication. Cytolytic class-Irestricted cells use a similar pathway to focus the effect of cytolytic proteins.This analogy views neuronal communication and lymphoid recognition as evolutionary descendents of a primordial lymphocytic type of cell interaction.

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Section: The Thy-1 Molecule As An Activation Site On T Cellsmentioning

confidence: 99%

A synaptic basis for T-lymphocyte activation

Norcross

1984

Annales de l'Institut Pasteur / Immunologie

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“…Preparation of cDNA Library. The cDNA library was constructed as described (35). Briefly, poly(A)-containing RNA was isolated from ISK cells and cDNA was synthesized by reverse transcription using an oligo(dT) primer followed by second-strand synthesis using DNA polymerase I.…”

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confidence: 99%

Nucleotide sequence of an HLA-DQ alpha chain derived from a DRw9 cell line: genetic and evolutionary implications.

Moriuchi¹,

Moriuchi²,

Silver³

1985

Proc. Natl. Acad. Sci. U.S.A.

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Three families of human Ia molecules, DP, DQ, and DR, have previously been defined. A cDNA clone, pDSH-9.1, encoding the a chain of a DQ molecule derived from an HLA-DRw9 homozygous cell line has been isolated and sequenced. Comparison of the nucleotide and predicted protein sequence to those of other DQ a subunits reveals that DQ a subunits derived from DR4, -7, and -9 cells are very similar to each other but quite different from a DQ a subunit derived from a DRw6 cell line. These studies suggest that certain Ia haplotypes have a common evolutionary history. Furthermore, in the context of current serologic and biochemical knowledge, they suggest that the gene encoding the DQ a subunit is in strong linkage disequilibrium with the DR locus.The Ia region of the major histocompatibility complex (MHC) consists of a series of closely linked loci encoding cell surface molecules that regulate the immune response. These Ia molecules may be divided into three groups, DP (formerly known as SB) (1), DQ (formerly known as DS) (2), and DR (3), that are structurally distinct. Ia molecules consist of two subunits, a and ,3, with molecular weights of approximately 28,000 and 33,000. Within each group, DP, DQ, and DR, multiple a-and /8-chain gene loci have been described; at present seven P3 chain (two DP, two DQ, and three DR) and five a chain (two DP, two DQ, and one DR) gene loci have been identified (4-9). Although their precise genetic order is not yet known, the DP locus is known to be centromeric to both DQ and DR, which in turn are centromeric to the class I loci, HLA-A, -B, and -C (10). Recombinational analysis indicates that both DP and the class I loci are approximately 1 centimorgan from the DQ and DR loci (10,11). No recombinational event between DQ and DR has yet been confirmed, suggesting a relatively low frequency of recombination. Biochemical studies (2,(12)(13)(14)(15)(16)(17)(18) and analysis of cDNA clones (19)(20)(21)(22)(23)(24)(25)(26) indicate that a majority of the Ia genes are expressed as products. Ia gene products belonging to the same group are highly related (greater than 95% protein homology) while those belonging to different groups are only approximately 60% related.The Ia system is highly polymorphic. At least 11 alleles at the DR locus (designated numerically-i.e., DR1-DR11) have been defined serologically (27). Similarly, at least 6 alleles at the DQ locus and 6 at the DP locus have been defined biochemically and by cellular assays, respectively (27,28 (29). Similarly, cells typing as DR1, -2, and -6 frequently display the MB1 antigenic determinant (30).Although the molecular basis for these antigenic determinants is not known, in some instances, the gene products expressing them have been identified. Thus, MB1, which is expressed on Drl, -2, and -6 cells, and MB3, which is expressed on DR4 and DR5 cells, are both present on different allelic forms of DQ molecules (28,31,32). In other instances, the molecular assignment has been more controversial; MT3 has been localized to DR-like mol...

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“…We have previously isolated a rat Thy-l cDNA clone pT64, which prematurely ends at amino acid 103 due to a polyadenylation signal within the coding sequence [7]. pT64 was used to screen a new rat thymocyte cDNA library and a new Thy-l cDNA clone pT86 was isolated from approx.…”

Section: Resultsmentioning

confidence: 99%

“…The cDNA library was constructed using mRNA from W/Fu rat thymocytes as in [7]. Plasmid pT86 was identified by colony hybridization with a nicktranslated probe derived from first Thy-l clone pT64.…”

Section: Clandva Synthesis and Clone Identi~icaiio~mentioning

confidence: 99%

Rat Thy‐1 antigen has a hydrophobic segment at the carboxyl terminus

Moriuchi

Silver

1984

FEBS Letters

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We have isolated a cDNA clone coding for rat Thy-l antigen from a rat thymocyte cDNA library. The 549 base pairs insert includes the complete coding region of a mature Thy-l polypeptide of 142 amino acids, 31 amino acids longer than the previously reported glycoprotein sequence. These 31 amino acids contain an extremely hydrophobic region of 26 uncharged amino acids which apparently represent the transmembrane segment that allows for integration within the membrane. The presence of this additional protein segment will solve most of the enigmas regarding the properties of the C-terminal region of Thy-1 antigen.

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Thy-1 cDNA sequence suggests a novel regulatory mechanism

Cited by 58 publications

References 23 publications

A synaptic basis for T-lymphocyte activation

A synaptic basis for T-lymphocyte activation

Nucleotide sequence of an HLA-DQ alpha chain derived from a DRw9 cell line: genetic and evolutionary implications.

Rat Thy‐1 antigen has a hydrophobic segment at the carboxyl terminus

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