The topology of plasminogen binding and activation on the surface of human breast cancer cells

Andronicos, Nicholas M.; Ranson, Marie

doi:10.1054/bjoc.2001.2022

Cited by 33 publications

(41 citation statements)

References 19 publications

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“…Cell surface actin has been shown previously to be a plasminogen binding site (34,39,40). Actin was associated with the cell membrane fractions of PC-3, MDA-MB231, and HT1080 cells as determined by Western blot (Fig.…”

Section: Resultsmentioning

confidence: 58%

“…One or more actin isoform was found by several independent groups of researchers on the surface of lymphocytes (44,45), brain capillary endothelial cells (46), and bovine pulmonary endothelial cells (47)(48)(49)(50). Actin was also discovered as a cell surface binding site for plasminogen on endothelial cells (39), monocytoid cells, blood monocytes (34), and breast cancer cells (40). The mechanism of actin trafficking and binding to the cell surface is not well understood.…”

Section: Discussionmentioning

confidence: 99%

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Cell Surface-Dependent Generation of Angiostatin4.5

et al. 2004

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Angiostatin4.5 (AS4.5) is a naturally occurring human angiostatin isoform, consisting of plasminogen kringles 1-4 plus 85% of kringle 5 (amino acids Lys78 to Arg529). Prior studies indicate that plasminogen is converted to AS4.5 in a two-step reaction. First, plasminogen is activated to plasmin. Then plasmin undergoes autoproteolysis within the inner loop of kringle 5, which can be induced by a free sulfhydryl donor or an alkaline pH. We now demonstrate that plasminogen can be converted to AS4.5 in a cell membrane-dependent reaction. Actin was shown previously to be a surface receptor for plasmin(ogen). We now show that ␤-actin is present on the extracellular membranes of cancer cells (PC-3, HT1080, and MDA-MB231), and ␤-actin can mediate plasmin binding to the cell surface and autoproteolysis to AS4.5. In the presence of ␤-actin, no small moleculefree sulfhydryl donor is needed for generation of AS4.5. Antibodies to actin reduced membrane-dependent generation of AS4.5 by 70%. In a cell-free system, addition of actin to in vitro-generated plasmin resulted in stoichiometric conversion to AS4.5. Annexin II and ␣-enolase have been reported to be plasminogen receptors, but we did not demonstrate a role for these proteins in conversion of plasminogen to AS4.5. Our data indicate that membrane-associated ␤-actin, documented previously as a plasminogen receptor, is a key cell membrane receptor capable of mediating conversion of plasmin to AS4.5. This conversion may serve an important role in regulating tumor angiogenesis, invasion, and metastasis, and surface ␤-actin may also serve as a prognostic marker to predict tumor behavior.

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Section: Resultsmentioning

confidence: 58%

Section: Discussionmentioning

confidence: 99%

Cell Surface-Dependent Generation of Angiostatin4.5

et al. 2004

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“…However, under stimulatory conditions, ENO-1 can be translocated to the cell surface, where it acts as a PLG receptor (13). Accumulation of PLG on the cell surface and its subsequent conversion to plasmin contribute to the modulation of pericellular proteolytic activity and thus to the regulation of migratory properties of numerous cell types including cancer cells (14,40). Although increased abundance of ENO-1 was described on the cell surface of cancer cells, the contribution of cell surface-bound ENO-1 to the increased migratory and the invasive properties of tumor cells, as well as the mechanism underlying ENO-1 exteriorization, have not yet been reported.…”

Section: Discussionmentioning

confidence: 99%

STIM1/ORAI1-mediated Ca2+ Influx Regulates Enolase-1 Exteriorization

Didiášová

Zakrzewicz

Magdolen

et al. 2015

Journal of Biological Chemistry

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Background: Cell surface-associated enolase-1 regulates plasmin formation and thus pericellular proteolysis. Results: STIM1/ORAI1-mediated Ca 2ϩ influx controls enolase-1 exteriorization in cancer cells. Conclusion: Extracellular enolase-1 regulates migratory and invasive properties of cancer cells. Significance: Enhanced exteriorization of enolase-1 may aggravate the malignant behavior of cancer cells and thus contribute to metastasis formation.

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“…As an independent approach, we demonstrated the presence of actin on the catecholaminergic cell surface using FACS analyses. Several reports suggest the presence of a cell-surface form of actin on other cell types (Owen et al, 1978;Bachvaroff et al, 1980;Sanders and Craig, 1983;Moroianu et al, 1993;Dudani and Ganz, 1996;Andronicos and Ranson, 2001;Dudani et al, 2005). Actin mediates autoproteolysis of plasminogen to angiostatin on cancer cells (H. Wang et al, , 2006.…”

Section: Discussionmentioning

confidence: 99%

Cell-Surface Actin Binds Plasminogen and Modulates Neurotransmitter Release from Catecholaminergic Cells

Miles¹,

Andronicos²,

Baik³

et al. 2006

J. Neurosci.

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An emerging area of research has documented a novel role for the plasminogen activation system in the regulation of neurotransmitter release. Prohormones, secreted by cells within the sympathoadrenal system, are processed by plasmin to bioactive peptides that feed back to inhibit secretagogue-stimulated release. Catecholaminergic cells of the sympathoadrenal system are prototypic prohormone-secreting cells. Processing of prohormones by plasmin is enhanced in the presence of catecholaminergic cells, and the enhancement requires binding of plasmin(ogen) to cellular receptors. Consequently, modulation of the local cellular fibrinolytic system of catecholaminergic cells results in substantial changes in catecholamine release. However, mechanisms for enhancing prohormone processing and cellsurface molecules mediating the enhancement on catecholaminergic cells have not been investigated. Here we show that plasminogen activation was enhanced Ͼ6.5-fold on catecholaminergic cells. Carboxypeptidase B treatment decreased cell-dependent plasminogen activation by ϳ90%, suggesting that the binding of plasminogen to proteins exposing C-terminal lysines on the cell surface is required to promote plasminogen activation. We identified catecholaminergic plasminogen receptors required for enhancing plasminogen activation, using a novel strategy combining targeted specific proteolysis using carboxypeptidase B with a proteomics approach using twodimensional gel electrophoresis, radioligand blotting, and tandem mass spectrometry. Two major plasminogen-binding proteins that exposed C-terminal lysines on the cell surface contained amino acid sequences corresponding to ␤/␥-actin. An anti-actin monoclonal antibody inhibited cell-dependent plasminogen activation and also enhanced nicotine-dependent catecholamine release. Our results suggest that cell-surface-expressed forms of actin bind plasminogen, thereby promoting plasminogen activation and increased prohormone processing leading to inhibition of neurotransmitter release.

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The topology of plasminogen binding and activation on the surface of human breast cancer cells

Cited by 33 publications

References 19 publications

Cell Surface-Dependent Generation of Angiostatin4.5

Cell Surface-Dependent Generation of Angiostatin4.5

STIM1/ORAI1-mediated Ca2+ Influx Regulates Enolase-1 Exteriorization

Cell-Surface Actin Binds Plasminogen and Modulates Neurotransmitter Release from Catecholaminergic Cells

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