Plasminogen activator and its enhancement in differentiating mouse friend erythroleukemia cells

Amici, Carla; Benedetto, A.; Saksela, Olli; Salonen, Eeva‐Marjatta; Vaheri, Antti

doi:10.1002/ijc.2910430131

Cited by 6 publications

(2 citation statements)

References 24 publications

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“…For Rous sarcoma virus-transformed chicken embryo fibroblasts and mesangial epithelial cells, treatment with antiuPA directed against the catalytic uPA domain promotes adhesion and prevents the morphological effects induced by PMA or cyclic-AMP mediated pathways (46,47). Moreover, in maturing Friend erythroleukemia cells, where evidence exists for a role ofATF in inducing differentiation, monoclonal antibodies directed against the catalytic domain promote adhesion on fibronectin coated surfaces presumably by interfering with metabolism of the matrix (48).…”

Section: Methodsmentioning

confidence: 99%

An autocrine role for urokinase in phorbol ester-mediated differentiation of myeloid cell lines.

Nusrat¹,

Chapman²

1991

J. Clin. Invest.

131

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The human myeloid cell line HL60 secretes urokinase-type plasminogen activator (uPA) and expresses its receptor. When stimulated with phorbol myristate acetate (PMA), both secretion of uPA and the expression of its receptor are up-regulated, and these cells differentiate to an adherent phenotype. This adhesive response is markedly reduced in the presence of uPA antibodies. The PMA response is restored by the addition of native uPA, an amino-terminal fragment of uPA (residues 1-143) devoid of proteolytic activity, or a synthetic peptide (residues 12-32) from the uPA growth factor domain known to mediate receptor binding. In contrast, the addition of catalytically active low molecular weight uPA, which is missing the growth factor domain, or a peptide from the catalytic domain (residues 247-266) is ineffective. The influence ofuPA antibodies on a second marker of macrophage differentiation, cysteine proteinase activity, was also examined. Cysteine proteinase activity of HL60 cells is increased in PMA-treated cells after 24 h but it fails to increase in the presence of anti-uPA. This increase in cathepsin B-like activity is also restored by exogenous uPA. These experiments indicate that an autocrine interaction of the growth factor domain of uPA with its receptor mediates an essential step in PMA-mediated myeloid cell differentiation. (J. Clin.

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Section: Methodsmentioning

confidence: 99%

An autocrine role for urokinase in phorbol ester-mediated differentiation of myeloid cell lines.

Nusrat¹,

Chapman²

1991

J. Clin. Invest.

131

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“…This signal transduction can lead to a change in the adhesive (9,10), chemotactic (11,12), and mitogenic (13)(14)(15)(16)(17) response of various cell types. In a number of studies the mitogenic response depends on both u-PA activity and interaction with a cell surface receptor mediated by the ATF domain (16, 18 -20).…”

mentioning

confidence: 99%

Mitogenic Effects of Urokinase on Melanoma Cells Are Independent of High Affinity Binding to the Urokinase Receptor

Koopman¹,

Slomp²,

Bart³

et al. 1998

Journal of Biological Chemistry

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The structural and functional properties of the urokinase-type plasminogen activator (u-PA) that are involved in the mitogenic effect of this proteolytic enzyme on human melanoma cells M14 and IF6 and the role of the u-PA receptor (u-PAR) in transducing this signal were analyzed. Native u-PA purified from urine induced a mitogenic response in quiescent IF6 and M14 cells that ranged from 25 to 40% of the mitogenic response obtained by fetal calf serum. The half-maximum response in M14 and IF6 cells was reached at u-PA concentrations of approximately 35 and 60 nM, respectively. Blocking the proteolytic activity of u-PA resulted in a 30% decrease of the mitogenic effect, whereas inhibition of plasmin activity did not alter the mitogenic effect. No mitogenic response was elicited by low molecular weight u-PA, lacking the growth factor domain and the kringle domain. The ATF domain of u-PA induced a mitogenic response that was similar to complete u-PA. Defucosylated ATF and recombinant u-PA purified from Escherichia coli lacking all post-translational modifications did not induce a mitogenic response. Blocking the interaction of u-PA with u-PAR, using a specific monoclonal antibody, did not alter the mitogenic effect induced by u-PA. The binding of radiolabeled u-PA to M14 and IF6 cells was characterized by high affinity binding mediated by u-PAR and low affinity binding to an unknown binding site. These results demonstrate that proteolytically inactive u-PA is able to induce a mitogenic response in quiescent melanoma cells in vitro by a mechanism that involves the ATF domain but is independent of high affinity binding to u-PAR. Furthermore, it suggests that u-PA is able to bind with low affinity to a hitherto unidentified membrane associated protein that could be involved in u-PA-induced signal transduction.

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A role for urokinase in mediating phorbol ester induced macrophagelike maturation and adhesion of u937 and other myeloid cells

et al. 1992

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Plasminogen activator and its enhancement in differentiating mouse friend erythroleukemia cells

Cited by 6 publications

References 24 publications

An autocrine role for urokinase in phorbol ester-mediated differentiation of myeloid cell lines.

An autocrine role for urokinase in phorbol ester-mediated differentiation of myeloid cell lines.

Mitogenic Effects of Urokinase on Melanoma Cells Are Independent of High Affinity Binding to the Urokinase Receptor

A role for urokinase in mediating phorbol ester induced macrophagelike maturation and adhesion of u937 and other myeloid cells

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