Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1

Jones, Nicholas; Clabby, Martha L.; Dialynas, Deno P.; Huang, Huei-Jen Su; Herzenberg, Leonard A.; Strominger, Jack L.

doi:10.1038/323346a0

Cited by 194 publications

(119 citation statements)

References 30 publications

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“…Additionally, we immunoprecipitated an extra 56-kDa band ( Fig. 2A) which has been previously intcrpreted either as a partial proteolytic fragment lacking the cytoplasmic tail [12] or as a metabolic precursor [l]. The exact nature of this band is unknown, but the fact that it was not seen on "P-labeled immunoprecipitates support the former possibility.…”

Section: P M a Induces The Appearance Of Hyperphosphorylated Cd5 Formsupporting

confidence: 52%

“…Recently, the molecular cloning of the human [12] and Abbreviations. Con A, concanavalin A; IL-1, interleukin-1 ; mAb, monoclonal antibody; PAP, potato acid phosphatase; PBMC, peripheral blood mononuclear cells; PDBU, phorbol 12,13-dibutyrate; PGE2, prostaglandin Ez; PI, isoelectric point; PHA-P, phytohaemagglutinin; PKC, protein kinase C; PMA, phorbol 12-myristate 13-acetate; TPA, tumor promoter agent/s; H-7, 1-(5-isoquinolylsulfonyl)-2-methylpiperazine.…”

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confidence: 99%

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Phosphorylation‐mediated changes in the electrophoretic mobility of CD5 molecules

Lozano

Alberola‐Ila

Places

et al. 1990

European Journal of Biochemistry

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This work shows that tumor promoter agents (TPA) induce the post-translational modification of the human lymphocyte surface CD5 antigen (Tp67) in several cellular types. Treatment of [32P]orthophosphate-and [35S]cysteine-labeled normal and lymphoblastoid T and B cells with active tumor promoters induced the rapid, transitory and dose-dependent appearance of hyperphosphorylated CD5 forms with higher apparent molecular masses. These changes in the electrophoretic mobility of CD5 molecules were independent of RNA and protein synthesis, as well as of differences in neuraminic acid content. The inhibition of the TPA-mediated changes by protein kinase C inhibitors (staurosporine and 1 -(5-isoquinolylsulfonyl)-2-methylpiperazine) indicated its proteinkinase-C-mediated nature. Phosphatase digestion of CD5 immunoprecipitates reverted the TPA-mediated mobility changes showing its dependence on phosphorylation. Neuraminidase digestion of intact cells revealed that the target of the TPA effects are surface-expressed CD5 molecules. In conclusion, we suggest that the heterogeneity in the electrophoretic mobility induced by TPA could reflect some structural and/or functional differences within CD5 molecules.The CD5 (Tl, Leu-1, Tp67 in human; Ly-1 in mouse) molecule is a 67 kDa surface differentiation glycoprotein present on most peripheral T lymphocytes and thymocytes, as well as on a subset of normal peripheral B lymphocytes [l, 21. Although both the function and the natural ligand of the CD5 antigen still remain unknown, there are functional studies showing that this antigen provides accessory signals necessary for human T lymphocyte activation and proliferation [3]. Perturbation of CD5 by monoclonal antibodies (mAb) has not been observed to activate T cells, however they can increase the CD3iantigen receptor-mediated production of interleukin-2, cell proliferation [4, 51, Ca2+ influx [6] and hydrolysis of inositol phospholipids [7]. Importantly, it has been also shown that although CD5 is not the interleukin-1 (IL-1) receptor itself [8], its expression may regulate responsiveness and binding of 1L-1 [9]. In this respect, IL-1 and CD5-specific mAb had an additive effect on the enhancement of T cell activation, suggesting that the CD5 molecule and the IL-1 receptor are complementary and act through distinct pathways to increase T cell activation [5, 101. However, little is known about the nature of the intracellular mechanism mediating the functional effects of CD5.Protein phosphorylation is the most common form of posttranslational modification used to regulate cellular functions [ll]. Recently, the molecular cloning of the human [12] and Abbreviations. Con A, concanavalin A; IL-1, interleukin-1 ; mAb, monoclonal antibody; PAP, potato acid phosphatase; PBMC, peripheral blood mononuclear cells; PDBU, phorbol 12,13-dibutyrate; PGE2, prostaglandin Ez; PI, isoelectric point; PHA-P, phytohaemagglutinin; PKC, protein kinase C; PMA, phorbol 12-myristate 13-acetate; TPA, tumor promoter agent/s; H-7, 1-(5-isoquinolylsulfonyl)-2-meth...

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Section: P M a Induces The Appearance Of Hyperphosphorylated Cd5 Formsupporting

confidence: 52%

mentioning

confidence: 99%

Phosphorylation‐mediated changes in the electrophoretic mobility of CD5 molecules

Lozano

Alberola‐Ila

Places

et al. 1990

European Journal of Biochemistry

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“…Although the function of the SRCR domains is not clear, they are likely to be involved with binding to other cell surface or extracellular molecules. The SRCR domains form most of the extracellular sequence of CD5 (21), which binds to its ligand, CD72 (23). Furthermore, the membrane-proximal SRCR domains in CD6 are necessary for binding of CD6 to its ligand (24).…”

Section: Resultsmentioning

confidence: 99%

Regulation of a Novel Gene Encoding a Lysyl Oxidase-related Protein in Cellular Adhesion and Senescence

Saitō

Papaconstantinou

Sato

et al. 1997

Journal of Biological Chemistry

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We report here a novel cDNA clone with a predicted protein sequence similar to lysyl oxidase. This fulllength cDNA clone of 3432 base pairs (WS9-14) was isolated from human fibroblasts on the basis of its overexpression in senescent cells. It encodes an 87-kDa polypeptide, whose protein is a member of the scavenger receptor cysteine-rich family, because it contains four scavenger receptor cysteine-rich domains that are found in several secreted or cell surface proteins. The WS9-14 protein has a 48% identity with both lysyl oxidase and lysyl oxidase-like protein at a region corresponding to exons 2-6, implying the existence of a lysyl oxidase gene family. The pattern of WS9-14 gene expression by fibroblasts parallels pro-collagen I-␣1 expression. Its mRNA level is induced by transforming growth factor ␤-1 and indomethacin and inhibited by phorbol ester and retinoic acid. WS9-14 is abundantly expressed in all tumor cell lines examined that attach to culture dishes but not in cell lines that grow in suspension and is also up-regulated in senescent fibroblasts. These results suggest that WS9-14 gene encodes an extracellular protein that may be specifically involved in cell adhesion and senescence.

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“…We have reported [3-61 that the character of a protein is also related to its amino acid composition and this varies with location (inside or outside of the cell), function (enzyme or non-enzyme) and folding type. The amino acid composition of an extracellular protein, which is characterized as having a signal peptide at the N-terminus, is different from that of intracellular proteins [4].…”

Section: Introductionmentioning

confidence: 99%

The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins

Nakashima

Nishikawa

1992

FEBS Letters

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The amino acid composition of transmemhrane proteins was analyzed for their three separate portions: the transmembrane apolar, cytoplasmic and extracellular regions. The composition was different between cytoplasmic and extracellular peptides; alanine and argininc residues were preferentially sited on the cytoplasmic side, while the threonine and cysteinc/cysdne were preferentially sited on the extracellular side, The composition ofcytoplasmic and extracellular peptides of membrane protcinscorresponded to those of intracellular and extracellular types ofsoluble proteins, respectively. This difference in composition was independent of the peptidc orientation against the membrane. Peptide chains could he correctly assigned as either cytoplasmic or cxtraccllular, solely from an analysis of sequence composition. For single-spanning membrane proteins the predictive accuracy was 9046, whereas for multi-spanning proteins this was 85%.

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Isolation of complementary DNA clones encoding the human lymphocyte glycoprotein T1/Leu-1

Cited by 194 publications

References 30 publications

Phosphorylation‐mediated changes in the electrophoretic mobility of CD5 molecules

Phosphorylation‐mediated changes in the electrophoretic mobility of CD5 molecules

Regulation of a Novel Gene Encoding a Lysyl Oxidase-related Protein in Cellular Adhesion and Senescence

The amino acid composition is different between the cytoplasmic and extracellular sides in membrane proteins

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