Association of intermediate filaments with vinculin‐containing adhesion plaques of fibroblasts

Bershadsky, Alexander D.; Tint, I.S.; Svitkina, T.M.

doi:10.1002/cm.970080308

Cited by 71 publications

(38 citation statements)

References 26 publications

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“…For the latter reason we suggest the term vimentinassociated matrix adhesions (VMAs) for these adhesion sites. These may be comparable to the vimentin-associated focal contacts demonstrated by Bershadsky et al (1987) in quail embryo fibroblasts. We assume that plectin mediates the interaction of vimentin with these focal contact-like devices, based on its known vimentin-binding properties, its localization, and its function in linking other types of intermediate filaments to the cell surface (Wiche et al, 1982;Steinbö ck and Wiche, 1999).…”

Section: Discussionsupporting

confidence: 77%

Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

Gonzales

Weksler

Tsuruta

et al. 2001

MBoC

148

134

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The ␣4 laminin subunit is a component of endothelial cell basement membranes. An antibody (2A3) against the ␣4 laminin G domain stains focal contact-like structures in transformed and primary microvascular endothelial cells (TrHBMECs and HMVECs, respectively), provided the latter cells are activated with growth factors. The 2A3 antibody staining colocalizes with that generated by ␣v and ␤3 integrin antibodies and, consistent with this localization, TrHBMECs and HMVECs adhere to the ␣4 laminin subunit G domain in an ␣v␤3-integrin-dependent manner. The ␣v␤3 integrin/2A3 antibody positively stained focal contacts are recognized by vinculin antibodies as well as by antibodies against plectin. Unusually, vimentin intermediate filaments, in addition to microfilament bundles, interact with many of the ␣v␤3 integrin-positive focal contacts. We have investigated the function of ␣4-laminin and ␣v␤3-integrin, which are at the core of these focal contacts, in cultured endothelial cells. Antibodies against these proteins inhibit branching morphogenesis of TrHBMECs and HMVECs in vitro, as well as their ability to repopulate in vitro wounds. Thus, we have characterized an endothelial cell matrix adhesion, which shows complex cytoskeletal interactions and whose assembly is regulated by growth factors. Our data indicate that this adhesion structure may play a role in angiogenesis.

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Section: Discussionsupporting

confidence: 77%

Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

Gonzales

Weksler

Tsuruta

et al. 2001

MBoC

148

134

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“…Yet, a number of studies have indicated that in certain cells FCs show interaction with the vimentin cytoskeleton (Bershadsky et al, 1987;Gonzales et al, 2001). We have extended these observations.…”

Section: Discussionsupporting

confidence: 61%

“…fibroblasts vimentin IFs are connected to FCs (Bershadsky et al, 1987). Moreover, the idea that vimentin IFs are involved in modulating either the structure or function of FCs is also supported by observations of the organization of FCs along regions of cell-matrix interaction in vimentin-deficient fibroblasts (Eckes et al, 1998).…”

mentioning

confidence: 88%

The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress

Tsuruta

Jones

2003

Journal of Cell Science

216

196

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Recently, we reported that vimentin-type intermediate filaments, in addition to microfilaments, associate with αvβ3 integrin-positive focal contacts in endothelial cells. To gain insight into intermediate filament-focal contact interaction, we induced expression of yellow fluorescent protein (YFP)-integrin β3 and cyan fluorescent protein (CFP)-vimentin protein in endothelial cells. At least 50% of the YFP-β3 integrin-labeled focal contacts associated with CFP-labeled vimentin intermediate filaments in live cells. Moreover, focal contacts and intermediate filaments moved in concert in the plane of the membrane and assembling focal contacts were sites of vimentin filament assembly. When endothelial cells were subjected to flow, large focal contacts assembled and associated with thick vimentin bundles. These large focal contacts showed minimal dynamic activity. Cells in which vimentin expression had been inhibited by RNA interference assembled smaller than normal focal contacts. More dramatically, such cells showed decreased adhesion to the substratum. These data provide evidence that the vimentin cytoskeleton regulates focal contact size and helps stabilize cell-matrix adhesions in endothelial cells.

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“…It has been reported that vimentin colocalizes with adhesion plaques to stabilize the plaque. Adhesion plaque formation therefore influences cell-cell adhesion (Bershadsky et al, 1987;Burridge et al, 1988). In our present experiment, the structural organization of vimentin in endothelial cells by LMWH could therefore play an important role in the antiadhesion and antitransendothelial migration functions of LMWH.…”

Section: Discussionmentioning

confidence: 50%

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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Association of intermediate filaments with vinculin‐containing adhesion plaques of fibroblasts

Cited by 71 publications

References 26 publications

Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

Structure and Function of a Vimentin-associated Matrix Adhesion in Endothelial Cells

The vimentin cytoskeleton regulates focal contact size and adhesion of endothelial cells subjected to shear stress

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

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