The Lipoxygenase Metabolite, 12(S)-HETE, Induces a Protein Kinase C-Dependent Cytoskeletal Rearrangement and Retraction of Microvascular Endothelial Cells

Tang, Dean G.; Tı́már, József; Grossi, Irma M.; Renaud, Colette; Kimler, Victoria A.; Diglio, Clement A.; Taylor, John D.; Honn, Kenneth V.

doi:10.1006/excr.1993.1203

Cited by 55 publications

(41 citation statements)

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“…These include functioning as the cytoplasmic organizer, a supracellular mechanical scaffold, intercellular transporter, and signal transducer (Tang et al, 1993;Asaga et al, 1998). Several groups have reported that, in endothelial cells, vimentin controls directly or indirectly the cell-cell contact area and stabilizes cell-matrix adhesion (Tsuruta and Jones, 2003).…”

Section: Discussionmentioning

confidence: 99%

Role of Vimentin in the Inhibitory Effects of Low-Molecular-Weight Heparin on PC-3M Cell Adhesion to, and Migration through, Endothelium

Pan¹,

Lei²,

Teng³

et al. 2011

J Pharmacol Exp Ther

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Low-molecular-weight heparin (LMWH) has been used in cancer patients with venous thromboembolic complications, resulting in a higher survival rate and an inhibitory action on experimental metastasis. In the present study, human umbilical vein endothelial cells (HUVECs) were treated with LMWH for 24 h. We found that the resulting HUVECs could significantly inhibit the highly metastatic human prostate cancer cell line (PC-3M) in terms of its adhesion to the endothelium and migration across the endothelium, according to scanning electron microscopy. We also determined the elevated levels of endothelial intercellular Ca 2ϩ concentration after the adhesion of PC-3M cells to HUVECs was greatly reduced by incubation with LMWH. Using proteomics, we surveyed the global protein changes in HUVECs after LMWH treatment and identified four down-regulated proteins that were possible isoforms of cytoskeletal vimentin intermediate filaments, cartilage-derived Ctype lectin, and serine/threonine protein phosphatase 1␤ (PP-1B). LMWH affected the morphology of vimentin and the expression levels of ␣ v integrin and PP-1B in HUVECs bound to PC-3M cells. Vimentin assists in the adhesion of PC-3M cells, which was confirmed by short interfering RNA experiments. Furthermore, the direct binding of purified vimentin protein with LMWH was detected with surface plasmon resonance methods. However, when we used fluorescence-labeled heparin for 24 h to identify whether this binding occurred within cells, heparin was distributed principally around endothelial cells. Taken together, these findings suggest that the monoincubation of LMWH with HUVECs could inhibit PC-3M cell adhesion to, and migration through, endothelium. LMWH's regulation of vimentin plays a role in the antimetastatic action.

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Section: Discussionmentioning

confidence: 99%

Role of Vimentin in the Inhibitory Effects of Low-Molecular-Weight Heparin on PC-3M Cell Adhesion to, and Migration through, Endothelium

Pan¹,

Lei²,

Teng³

et al. 2011

J Pharmacol Exp Ther

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“…Integrins function as integrative elements in cytoskeletal arrangements and are involved in signalling events . Disruption of several cytoskeletal proteins, including actin and intermediate filaments, interferes with integrin-mediated phosphorylation of intracellular proteins (Tang et al, 1993). Furthermore, cytoskeletal arrangements and integrin surface expression seem to be related.…”

Section: Discussionmentioning

confidence: 99%

Different adhesion properties of highly and poorly metastatic HT-29 colon carcinoma cells with extracellular matrix components: role of integrin expression and cytoskeletal components

1999

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Summary Integrin-mediated tumour cell adhesion to extracellular matrix (ECM) components is an important step in the development of metastatic lesions. Thus, integrin expression and integrin-mediated adhesion of colon carcinoma cells to various ECM components was examined. Poorly (HT-29P) and highly (HT-29LMM) liver-metastatic colon carcinoma cells were used to study the rates of adhesion to collagen I (C I), collagen IV (C IV), laminin (LN), fibronectin (FN), or vitronectin (VN) in a static adhesion assay (10-120 min). Cells were untreated or treated with oligopeptides (RGD, GRGDS, YIGSR, RGES), anti-integrin antibodies, or colchicine, nocodazole, cycloheximide, acrylamide or cytochalasin D (to disrupt cytoskeletal structures). Both cell lines expressed similar patterns of integrin expression (α 2 , α 3 , α 6 , α v , β 1 , β 4 and β 5 ) by immunocytochemistry and immunoprecipitation. HT-29LMM cells showed significantly higher rates of adhesion to LN (P < 0.001) and FN (P < 0.001), but significantly poorer rates of adhesion to C I (P < 0.05) and C IV (P < 0.001) than HT-29P cells, respectively, adhesion to VN was insignificant. RGD and GRGDS inhibited HT-29LMM cell adhesion to FN only. Pretreatment with anti-β 1 or anti-α 2 integrin subunits suppressed adhesion to C I and C IV, and adhesion to LN was inhibited with anti-β 1 or anti-α 6 integrin. Anti-β 1 or anti-α v blocked adhesion to FN. Pretreatment of cells with cytochalasin D, cycloheximide or acrylamide inhibited adhesive interactions of both cell lines to the ECM components. In contrast, colchicine and nocodazole had no effect. The results demonstrate that adhesion of HT-29 cells to ECM is mediated, in part, by different integrins, depending on the substrate. Poorly and highly metastatic HT-29 cells possessed different patterns of adhesion to the various ECM substrates, but these differences were not due to different expression of integrin subunits. The results also suggested that the initial adhesion of poorly or highly metastatic HT-29 cells to ECM components requires, in part, the presence of native action and intermediate filaments, but not of microtubules. Thus the adhesion of tumour cells to ECM components may be dependent on signal transduction and assembly of microfilaments.

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“…It has been reported that cancer cells induce morphological changes of mesothelial cells by releasing some unknown substances (Kimura et al, 1985;Uchiyama et al, 1992) and may damage the mesothelial cells by attachment onto the mesothelial surface (Kiyasu et al, 1981). In cultured endothelial cells, several substances, including thrombin (Laposata et al, 1983), active oxygen (Shasby et al, 1985), 12(S)-HETE (Tang et al, 1993), tumour necrosis factor, interferon-y, interleukin 1 (Molony and Armstrong, 1991), histamine (Carson et al, 1989) and tyrosine phosphatase inhibitor (Staddon et al, 1995), are confirmed to increase permeability. We did not find any noticeable signs of mesothelial cell damage by cancer cells in this study, but found that the medium conditioned by SST-2 cells rapidly and reversibly reduced TER across the mesothelial monolayer and caused the disappearance of 7H6 antigen from the cell border (data not shown).…”

Section: Ter Measurementsmentioning

confidence: 99%

Enhanced paracellular barrier function of rat mesothelial cells partially protects against cancer cell penetration

Tobioka

Sawada²,

Zhong³

et al. 1996

Br J Cancer

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The Lipoxygenase Metabolite, 12(S)-HETE, Induces a Protein Kinase C-Dependent Cytoskeletal Rearrangement and Retraction of Microvascular Endothelial Cells

Cited by 55 publications

References 0 publications

Role of Vimentin in the Inhibitory Effects of Low-Molecular-Weight Heparin on PC-3M Cell Adhesion to, and Migration through, Endothelium

Role of Vimentin in the Inhibitory Effects of Low-Molecular-Weight Heparin on PC-3M Cell Adhesion to, and Migration through, Endothelium

Different adhesion properties of highly and poorly metastatic HT-29 colon carcinoma cells with extracellular matrix components: role of integrin expression and cytoskeletal components

Enhanced paracellular barrier function of rat mesothelial cells partially protects against cancer cell penetration

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