Modulation of T leukaemic cell phenotype with phorbol ester

Delia, Domenico; Greaves, Melvyn F.; Newman, Roland; Sutherland, D. Robert; Minowada, Jun; Kung, Patrick; Goldstein, Gideon

doi:10.1002/ijc.2910290106

Cited by 94 publications

(24 citation statements)

References 58 publications

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“…The nature, pace, and extent of the phenotypic changes induced by this potent activator of protein kinase C depended on the characteristics of the native line (Table I and [26][27][28][29]. As previously reported (30,31), all lines showed clonal rearrangements of the alpha and beta T cell receptor genes (data not shown).…”

Section: Resultssupporting

confidence: 71%

“…DMSO alone had no effect on the growth, viability, or affinity for HEV. PMA treatment slowed growth in several cell lines and gradually reduced cell viability as reported previously (55,27,28 binding assays were conducted at 1 or 5 X 106 cells/ml (i.e., 1 At each time point, affinity for the HEV of rat lymph nodes and for PPME beads were determined and normalized to concurrently run PBMC as described in Methods. The ratio of the normalized binding activities measured for the PMA-and DMSO-treated cultures are plotted for both attachment to the HEV (relative HEV binding) and PPME beads (relative PPME binding).…”

Section: Resultsmentioning

confidence: 99%

“…Perturbation of the membrane by this lipophilic compound is cited as a potential non-specific action; however, such effects are unlikely at < 50 nM (50, 51) while upregulation of the endothelial-binding lectin occurs at 1 nM. PKC appears to function in both lymphocyte differentiation (27)(28)(29) and activation (39,40). In conjunction with rapid mobilization of calcium, this enzyme provides a transmembrane signaling pathway for surface structures linked to phosphoinositol (52).…”

Section: Discussionmentioning

confidence: 99%

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Adhesion molecules of cultured hematopoietic malignancies. A calcium-dependent lectin is the principle mediator of binding to the high endothelial venule of lymph nodes.

Stoolman¹,

Ebling²

1989

J. Clin. Invest.

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This study documents that a calcium-dependent phosphomannosyl-binding site on human lymphoid malignancies mediates attachment to the peripheral node high endothelial venule (PNHEV). The phorbol ester PMA coordinately upregulates lectin activity and binding to the PNHEV in the human T-lymphoblastic cell line Jurkat but not in the less phenotypically mature lines HSB2, Molt4, CEM, and HPB-ALL. In contrast, expression of CD18, CD2, and several common epitopes of the putative adhesion receptor gp90fIerme (CD44) did not correlate with attachment to PNHEV in this series of cell lines. Insensitivity to inhibition by the CD18 MAb TS 1.18, temperature and divalent cation requirements further distinguish the Jurkat-PNHEV adhesive interaction from CD11a/18-and CD2-mediated adhesion. The PMA-induced phenotypic changes in the Jurkat line parallel late thymocyte differentiation as well as lymphocyte activation, suggesting that expression of the endothelial-binding lectin may be linked to one or both of these processes. The lectin-like activity on Jurkat cells is functionally indistinguishable from those previously linked to PNHEV recognition in normal human lymphocytes, normal rat lymphocytes and both normal and malignant murine lymphoid cells. In the mouse, this activity is either contained in or functionally linked to a member of the LEC-CAM family gp9OMeIl4, suggesting that Jurkat cells express the human homologue of the murine nodal homing receptor. Thus cultured T lymphoblastic malignancies express a variety of potential endothelial adhesion molecules but use primarily a highly conserved surface lectin to interact with PNHEV.

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Section: Resultssupporting

confidence: 71%

Section: Resultsmentioning

confidence: 99%

Section: Discussionmentioning

confidence: 99%

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Adhesion molecules of cultured hematopoietic malignancies. A calcium-dependent lectin is the principle mediator of binding to the high endothelial venule of lymph nodes.

Stoolman¹,

Ebling²

1989

J. Clin. Invest.

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“…However, despite its apparent critical role in regulating Tlymphocyte responses, the molecular basis of the regulation of the surface expression of T3 and Ti is poorly defined. Recent results suggest that phorbol esters can modulate the expression of various T-cell surface determinants (including T3), induce antigen unresponsiveness in specific T-cell clones, and stimulate some of the biochemical steps leading to T-cell activation (19)(20)(21). Because such reagents activate the Ca2l-dependent, phospholipid-dependent protein kinase C, this enzyme has been promoted as an intracellular signaling system in T-lymphocyte activation (22,23 (27).…”

mentioning

confidence: 99%

Activators of protein kinase C down-regulate and phosphorylate the T3/T-cell antigen receptor complex of human T lymphocytes.

Cantrell¹,

Davies²,

Crumpton³

1985

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

241

109

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As judged by indirect immunofluorescence, phorbol 12,13-dibutyrate and 1.oleoyl-2-acetylglycerol induced a rapid, concentration-dependent decrease of about 50% in the surface expression of the T3 antigen on human T lymphoblasts, and of T3 and the T-cell antigen receptor on HPB-ALL cells. Direct binding experiments using 'MI labeled antibody indicated that the reduction in T3 expression corresponded to a decrease in the number of antigen molecules rather than a change in their affinity. (5), and mutant cell lines selected for lack of expression of T3 also showed loss of Ti and vice versa (16). Down-regulation of the T3/Ti complex induced by specific antigen has been correlated with an inhibition of antigen recognition and related immune functions (2, 17, 18). However, despite its apparent critical role in regulating Tlymphocyte responses, the molecular basis of the regulation of the surface expression of T3 and Ti is poorly defined. Recent results suggest that phorbol esters can modulate the expression of various T-cell surface determinants (including T3), induce antigen unresponsiveness in specific T-cell clones, and stimulate some of the biochemical steps leading to T-cell activation (19-21 (27). The UCHT1, W6/32, and RFT11 antibodies were purified from ascitic fluid by ammonium sulfate precipitation and staphylococcal protein A-Sepharose affinity chromatography. The H1-2D4 antibody was used as ascitic fluid. 125I-labeled UCHT1 (1.4 x 108 cpm/nmol) was prepared by using the Enzymobead (Bio-Rad) modification of the lactoperoxidase-catalyzed iodination technique. Fluorescein-labeled and unlabeled rabbit antibodies against mouse immunoglobulin were purchased from Dakopatts (Mercia Brocades, Weybridge, Surrey, England). Endo-/3-N-acetylglycosaminidase F (Endo-F) was purchased from New England Nuclear. Purified recombinant human interleukin 2 was donated by K. A. Smith (Dartmouth Medical School, New Hampshire). Human peripheral blood mononuclear cells were separated from fresh blood by Ficoll-Hypaque discontinuous gradient centrifugation.Cell Cultures. The human T leukemia cell line HPB-ALL was cultured in RPMI 1640 medium containing penicillin (100 units/ml), streptomycin (50 ug/ml), and 10o (vol/vol) fetal calf serum (Flow Laboratories). Human T lymphoblasts were prepared by stimulating peripheral blood mononuclear cells (106 cells per ml of RPMI 1640/10% fetal calf serum) with UCHT1 antibody (250 ng/ml) for 72 hr. The cells were washed to remove UCHT1 and growth was maintained at concentrations of 105_106 cells per ml for up to 10 days by supplementing every 2 days with 0.1 nM interleukin 2. For modulation studies, cells were washed three times in RPMI Abbreviations: Ti, T-cell antigen receptor; PBt2, phorbol 12,13-dibutyrate; OleAcGro, 1-oleoyl-2-acetylglycerol; Endo-F, endo-3-N-acetylglycosaminidase F. 8158The publication costs of this article were defrayed in part by page charge payment. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. §1734 solely to indica...

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“…Since many of the above leukaemia/lymphoma cell lines are being increasingly used in the study of growth, differentiation and other studies (Koeffler & Golde, 1980;Koeffler et al, 1981;Delia et al, 1982;Gallo & Ruscetti, 1981;Westin et al, 1982;Srivastava, 1978), the cytochemical characterization and comparison of these cell lines which represent various levels of maturation could be very useful. In addition, this study also offers the possibility of finding deviations of pattern due to in vitro culture environment and for detecting additional heterogeneity in leukaemia/lymphoma cell lines.…”

mentioning

confidence: 99%

Cytochemical comparison of immunologically characterized human leukaemia/lymphoma cell lines representing different levels of maturation

Srivastava¹,

Rossowski²,

Minowada³

1983

Br J Cancer

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Summary Forty-seven human leukaemia/lymphoma cell lines belonging to myelocytic, monocytic, non-T/non-B, T-, and B-lineage and representing different levels of maturation as well as fresh cells from normal and leukaemic subjects were examined for immunological markers and cytochemically for acid phosphatase, alkaline phosphatase, a-naphthyl acetate esterase (pH 5.8 and 8.0), a-naphthyl butyrate esterase (pH 5.8 and 8.0), non-specific esterase, chloroacetate esterase, chymotrypsin-like protease, deoxyribonuclease II, fglucuronidase, sudan black, and periodic acid Schiff's staining.Strong sudan black, nonspecific esterase, and chloroacetate esterase reaction was obtained only for myelocytic and monocytic cell lines with the reaction intensity increasing progressively in more mature cells. Focal acid phosphatase reaction like T-ALL was found in all T-ALL cell lines, whereas myeloid/monocytoid lines had semicircular distribution and B-cell lines cytoplasmic distribution of activity. Acid phosphatase activity appeared to decline with maturation along both myeloid and T-cell lineage. High activity of anaphthyl acetate esterase and a-naphthyl butyrate esterase both at pH 5.8 and 8.0 and of ,B-glucuronidase was found in myeloid/monocytoid lines although both B-and T-cell lines in contrast to peripheral blood B-cells also had significant esterase activity. a-Naphthyl butyrate esterase activity declined with increasing cell maturation along myeloid lineage. Except for weak activity in two B-cell lines alkaline phosphatase was not detected in any cell lines. Monocyte elterase activity was inhibited by sodium fluoride whereas acid phosphatase, only from hairy cell leukaemia line, was resistant to L-tartarate. Although periodic acid Schiff's staining could not distinguish myeloid, T-, B-, or non-T/non-B cell lines it gave characteristic reaction (large number of coarse granules against a clear background forming a ring around the nucleus) with erythroblastic leukaemia cell line and along myeloid series its intensity increased in more mature cells. Deoxyribonuclease II and chymotrypsin-like protease staining were not discriminatory.The results of this study show that cytochemical staining characteristics of various leukaemia/lymphoma cell lines are comparable to those of corresponding cells from patients and that the intensity and pattern of expression of these activities are related to cell type and degree of cell maturation. These studies give further credence to the use of these cell lines in cell differentiation, differential drug cytotoxicity, and many other studies.

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Modulation of T leukaemic cell phenotype with phorbol ester

Cited by 94 publications

References 58 publications

Adhesion molecules of cultured hematopoietic malignancies. A calcium-dependent lectin is the principle mediator of binding to the high endothelial venule of lymph nodes.

Adhesion molecules of cultured hematopoietic malignancies. A calcium-dependent lectin is the principle mediator of binding to the high endothelial venule of lymph nodes.

Activators of protein kinase C down-regulate and phosphorylate the T3/T-cell antigen receptor complex of human T lymphocytes.

Cytochemical comparison of immunologically characterized human leukaemia/lymphoma cell lines representing different levels of maturation

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