Discordance between surface and cytoplasmic expression of the Leu-4 (T3) antigen in thymocytes and in blast cells from childhood T lymphoblastic malignancies.

Link, Michael P.; Stewart, Stanford J.; Warnke, Roger A.; Levy, Ronald

doi:10.1172/jci111954

Cited by 49 publications

(17 citation statements)

References 42 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…'7213' In keeping with the fact that it is initially an internal cell constituent its demonstration in leukaemias and lymphomas of thymic phenotype requires a technique which shows intracellular antigen, such as staining of cytospin preparations or tissue sections. 32 In the present study this phenomenon is probably epitomised by the lymphoblastic lymphoma (case 9) which was CD3 negative when tested in cell suspension, but strongly positive when stained in paraffin sections.…”

Section: Non-neoplastic Tissuesupporting

confidence: 46%

Antisera against epitopes resistant to denaturation on T3 (CD3) antigen can detect reactive and neoplastic T cells in paraffin embedded tissue biopsy specimens.

et al. 1988

View full text Add to dashboard Cite

SUMMARY Polyclonal rat antisera, raised against affinity purified CD3 antigen, gave strong immunoenzymatic labelling of T cells in routine paraffin embedded sections, with negligible background staining. The specificity of these reactions was confirmed by staining biopsy specimens from 21 previously phenotyped non-Hodgkin's lymphomas (including 14 of T cell origin and six of B cell origin). It is suggested that the ability of the polyclonal anti-CD3 antisera to detect T cells in paraffin sections is due to the presence in these sera of antibodies against fixation resistant epitopes on CD3 antigen, and that immunisation with purified denatured preparations of other white cell associated antigens may broaden the range of antibodies suitable for the phenotypic analysis of leucocytes in routine histological samples.

show abstract

Section: Non-neoplastic Tissuesupporting

confidence: 46%

Antisera against epitopes resistant to denaturation on T3 (CD3) antigen can detect reactive and neoplastic T cells in paraffin embedded tissue biopsy specimens.

et al. 1988

View full text Add to dashboard Cite

show abstract

“…This is explained by our work that demonstrates that assembly with a-, is required for survival of the complex. Studies using MOLT-4 T-cell leukemia cells reveal the presence of intracellular 8, y, and E chains but no cell surface expression (23,24). These cells have P-chain transcripts but lack mRNA for the a chain (25).…”

Section: Resultsmentioning

confidence: 97%

Building a multichain receptor: synthesis, degradation, and assembly of the T-cell antigen receptor.

Minami¹,

Weissman²,

Samelson³

et al. 1987

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

223

154

View full text Add to dashboard Cite

The murine T-cell antigen receptor consists of at least seven chains and six different proteins. The two clonotypic chains a and fi are glycoproteins of 40-45 kDa present as a disulfide-linked heterodimer. Four clonally invariant chains include 8 (a 26-kDa glycoprotein), y (a 21-kDa glycoprotein), e (a 25-kDa protein), and C (a 16-kDa protein).{is found in the complex as a disulfide-linked homodimer. The clonotypic chains and the invariant chains form a noncovalent complex on the cell surface. We have developed antibodies against each of the chains and used them to examine the assembly of the mature complex in the murine antigen-specific T-cell hybridoma 2B4. Pulse-chase studies of metabolically labeled cells demonstrate that many of the chains are synthesized in great excess over the amount assembled into the mature complex. These excess chains, either as free components or as partially assembled complexes, are rapidly degraded. This degradation most likely takes place in the lysosomes. The complete complex is quite stable with a long half-life. A specific hierarchy of partially assembled complexes can be discerned.Numerous cell surface receptors are multisubunit complexes including the acetylcholine receptor, the IgE Fc receptor, and the T-cell antigen receptor. The complete and precise assembly ofthese components is a formidable problem, but one that has been solved by the cell to ensure proper function of these critical cellular elements. In studies of the acetylcholine receptor (1, 2), it was established that only about 30o of the newly synthesized a chain is assembled into mature receptor. The unassembled a chains are rapidly degraded (1, 2). A similar set of observations about the B-cell antigen receptor (surface IgM) has correlated assembly of multisubunit complexes with dramatic stabilization of the components of the complexes (3). Studies of the assembly of erythrocyte cytoskeletal proteins, a and , spectrin, revealed that unassembled chains were rapidly degraded, in contrast to the fully assembled complex (4). The selective stabilization imparted by complex assembly may be critical to the mechanism whereby the cell ensures the existence of only stoichiometrically assembled protein complexes.Because selective catabolism may be fundamental to the selective survival of properly assembled complexes, the cell must possess mechanisms whereby unassembled, partially assembled, or incorrectly assembled complexes can be recognized. The following two major systems for intracellular proteolysis have been extensively studied: lysosomes and cytosolic ATP-dependent proteolytic pathways. Degradation by each of these is selective. Lysosomes are generally regarded as the major site of degradation of membrane proteins but they can also be responsible for the catabolism of cytosolic proteins and the content of other intracellular organelles (5). ATP-dependent, cytosolic, neutral protease systems have been implicated in the selective degradation of cytosolic proteins (6). Denatured proteins when microinjected into...

show abstract

“…1, lane 6). MOLT 4 cells do not express detectable levels of CD3 on the cell surface (47,48). Thus, although the Ti/CD3 complex may interact with the CD4.p561ck complex, its presence on the cell surface does not appear to be required for the formation of the CD4.,56 ck complex.…”

Section: Discussionmentioning

confidence: 96%

The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase (p56lck) that phosphorylates the CD3 complex.

Barber

Dasgupta

Schlossman

et al. 1989

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

395

235

View full text Add to dashboard Cite

Many mammalian receptors have been found to regulate cell growth by virtue of a protein-tyrosine kinase domain in their cytoplasmic tail. We recently described an association of the CD4 antigen with a T-cell-specific proteintyrosine kinase (p56"c"; formerly termed pp58lck; EC 2.7.1.112). This interaction represents a potential mechanism by which T-cell growth may be regulated and offers a model by which other members of the src family (products of c-src, c-yes, c-fgr, etc.) may interact with mammalian growth factor receptors. As in the case ofthe CD4 antigen, the CD8 antigen appears to serve as a receptor for nonpolymorphic regions of products of the major histocompatibility complex and has been implicated in the regulation of T-cell growth. In this study, we reveal that the human CD8 antigen is also associated with the T-cell-specific protein-tyrosine kinase (p56""k).

show abstract

Discordance between surface and cytoplasmic expression of the Leu-4 (T3) antigen in thymocytes and in blast cells from childhood T lymphoblastic malignancies.

Abstract: We have examined the expression of the Leu-4 (T3) antigen on the cell surface and in the cytoplasm of blast cells from 23 patients with T cell acute lymphoblastic leukemia and T cell lymphoblastic lymphoma. In the majority of cases (17)

Cited by 49 publications

References 42 publications

Antisera against epitopes resistant to denaturation on T3 (CD3) antigen can detect reactive and neoplastic T cells in paraffin embedded tissue biopsy specimens.

Antisera against epitopes resistant to denaturation on T3 (CD3) antigen can detect reactive and neoplastic T cells in paraffin embedded tissue biopsy specimens.

Building a multichain receptor: synthesis, degradation, and assembly of the T-cell antigen receptor.

The CD4 and CD8 antigens are coupled to a protein-tyrosine kinase (p56lck) that phosphorylates the CD3 complex.

Contact Info

Product

Resources

About