Release of an invasion promoter E-cadherin fragment by matrilysin and stromelysin-1

2001 ◽  
Vol 114 (1) ◽  
pp. 111-118 ◽  
Author(s):  
V. Noe ◽  
B. Fingleton ◽  
K. Jacobs ◽  
H.C. Crawford ◽  
S. Vermeulen ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Collagen Type ◽  
Cell Aggregation ◽  
Collagen Type I ◽  
Type I ◽  
Tissue Inhibitor Of Metalloproteinases ◽  
Dependent Cell ◽  
Mcf 7 ◽  
E Cadherin

The function of many transmembrane molecules can be altered by cleavage and subsequent release of their ectodomains. We have investigated ectodomain cleavage of the cell-cell adhesion and signal-transducing molecule E-cadherin. The E-cadherin ectodomain is constitutively shed from the surface of MCF-7 and MDCKts.srcC12 cells in culture. Release of the 80 kDa soluble E-cadherin fragment is stimulated by phorbol-12-myristate-13-acetate and is inhibited by overexpression of the tissue inhibitor of metalloproteinases-2. The metalloproteinases matrilysin and stromelysin-1 both cleave E-cadherin at the cell surface and release sE-CAD into the medium. The soluble E-cadherin fragment thus released inhibits E-cadherin functions in a paracrine way, as indicated by induction of invasion into collagen type I and inhibition of E-cadherin-dependent cell aggregation. Our results, therefore, suggest a novel mechanism by which metalloproteinases can influence invasion.

scholarly journals Stimulation of beta1 integrins on fibroblasts induces PDGF independent tyrosine phosphorylation of PDGF beta-receptors.

1996 ◽  
Vol 132 (4) ◽  
pp. 741-752 ◽  
Author(s):  
C Sundberg ◽  
K Rubin
Keyword(s):  
Cell Adhesion ◽  
Tyrosine Phosphorylation ◽  
Collagen Type ◽  
Collagen Gel ◽  
Collagen Type I ◽  
Receptor Activation ◽  
Type I ◽  
Integrin Subunit ◽  
Beta Receptor ◽  
Beta Receptors

We report that integrin-mediated signaling induces a rapid and transient tyrosine phosphorylation of platelet-derived growth factor (PDGF) beta-receptors in human diploid foreskin AG 1518 fibroblasts. A transient tyrosine phosphorylation of PDGF beta-receptors was evident one and two hours after cells had been plated on collagen type I and fibronectin, as well as on immobilized anti-integrin subunit IgG, but not on poly-L-lysine. In contrast EGF or PDGF alpha-receptors were not phosphorylated on tyrosine residues under these conditions. Tyrosine phosphorylation of PDGF beta-receptors induced by plating on collagen type I was inhibited by cytochalasin D and herbimycin A, unaffected by cycloheximide and enhanced by orthovanadate. Furthermore, a transient phosphorylation of PDGF beta-receptors occurred when AG 518 fibroblasts were cultured in three-dimensional collagen lattices or exposed to external strain exerted through centrifugation. The latter effect was evident already after two minutes. Clustering of cell surface beta1 integrins led to PDGF beta-receptor phosphorylation both in suspended and firmly attached AG 1518 fibroblasts. Plating of cells on collagen type I, fibronectin, and anti-beta1-integrin IgG resulted in the formation of PDGF beta-receptor aggregates as detected by immunofluorescence. Suramin or anti-PDGF-BB IgG had no effect on the plating-induced tyrosine phosphorylation of PDGF beta-receptors. PDGF-B chain mRNA, or protein, were not detected in AG 1518 fibroblasts. Our data suggest that a ligand-independent PDGF beta-receptor activation during cell adhesion and early phases of cell spreading is involved in integrin-mediated signaling in fibroblasts, and constitutes parts of a mechanism for cells to respond during the dynamic phases of externally applied tension as well as fibroblast-mediated tension during cell adhesion and collagen gel contraction.

scholarly journals Collagen type I-induced Smad-interacting protein 1 expression downregulates E-cadherin in pancreatic cancer

Oncogene ◽  
2006 ◽  
Vol 26 (16) ◽  
pp. 2381-2385 ◽  
Author(s):  
Y Imamichi ◽  
A König ◽  
T Gress ◽  
A Menke
Keyword(s):  
Pancreatic Cancer ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Interacting Protein ◽  
E Cadherin

A comparative study on collagen type I and hyaluronic acid dependent cell behavior for osteochondral tissue bioprinting

2014 ◽  
Vol 6 (3) ◽  
pp. 035004 ◽  
Author(s):  
Ju Young Park ◽  
Jong-Cheol Choi ◽  
Jin-Hyung Shim ◽  
Jung-Seob Lee ◽  
Hyoungjun Park ◽  
...  
Keyword(s):  
Hyaluronic Acid ◽  
Comparative Study ◽  
Collagen Type ◽  
Collagen Type I ◽  
Cell Behavior ◽  
Type I ◽  
Dependent Cell ◽  
Osteochondral Tissue

Oncostatin M-induced effects on EMT in human proximal tubular cells: differential role of ERK signaling

2007 ◽  
Vol 293 (5) ◽  
pp. F1714-F1726 ◽  
Author(s):  
Verena Pollack ◽  
Rita Sarközi ◽  
Zoltan Banki ◽  
Elisabeth Feifel ◽  
Swantje Wehn ◽  
...  
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Oncostatin M ◽  
Type I ◽  
Proximal Tubular Cells ◽  
Strong Concentration ◽  
Tubular Cells ◽  
Cell Scattering ◽  
Proximal Tubular ◽  
E Cadherin

Growing evidence suggests that a proportion of interstitial myofibroblasts detected during renal tubulointerstitial fibrosis originates from tubular epithelial cells by a process called epithelial-mesenchymal transition (EMT). The IL-6-type cytokine oncostatin M (OSM) has been recently implicated in the induction of EMT. We investigated OSM effects on the expression of both cell-cell contact proteins and mesenchymal markers and studied OSM-induced intracellular signaling mechanisms associated with these events in human proximal tubular cells. Human recombinant OSM attenuated the expression of N-cadherin, E-cadherin, and claudin-2 in human kidney-2 (HK-2) cells associated with the induction of HK-2 cell scattering in 3D collagen matrices. Conversely, expression of collagen type I, vimentin, and S100A4 was induced by OSM. OSM-stimulated cell scattering was inhibited by antibodies against gp130. Besides inducing phosphorylation of Stat1 and Stat3, OSM led to a strong concentration- and time-dependent phosphorylation of the mitogen-activated protein kinases ERK1, ERK2, and ERK5. MEK1/2 inhibitor U0126 (10 μM) blocked basal and OSM-induced ERK1/2 phosphorylation but not phosphorylation of either ERK5 or Stat1/3. Both synthetic MEK1/2 inhibitors U0126 and Cl-1040, when used at concentrations which inhibit ERK1/2 phosphorylation but not ERK5 phosphorylation, restored N-cadherin expression in the presence of OSM, inhibited basal claudin-2 expression, but did not affect either basal or OSM-inhibited E-cadherin expression or OSM-induced expression of collagen type I and vimentin. These results suggest that in human proximal tubular cells ERK1/2 signaling represents an important component of OSM's inhibitory effect on N-cadherin expression. Furthermore, functional ERK1/2 signaling is necessary for basal claudin-2 expression.

scholarly journals Plakoglobin, or an 83-kD homologue distinct from beta-catenin, interacts with E-cadherin and N-cadherin.

1992 ◽  
Vol 118 (3) ◽  
pp. 671-679 ◽  
Author(s):  
K A Knudsen ◽  
M J Wheelock
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Molecular Mass ◽  
Beta Catenin ◽  
Calcium Dependent ◽  
Intracellular Proteins ◽  
Dependent Cell ◽  
Cell Surface Glycoproteins ◽  
E Cadherin ◽  
Cell Cell

E- and N-cadherin are members of a family of calcium-dependent, cell surface glycoproteins involved in cell-cell adhesion. Extracellularly, the transmembrane cadherins self-associate, while, intracellularly, they interact with the actin-based cytoskeleton. Several intracellular proteins, collectively termed catenins, have been noted to co-immunoprecipitate with E- and N-cadherin and are thought to be involved in linking the cadherins to the cytoskeleton. Two catenins have been identified recently: a 102-kD vinculin-like protein (alpha-catenin) and a 92-kD Drosophila armadillo/plakoglobin-like protein (beta-catenin). Here, we show that plakoglobin, or an 83-kD plakoglobin-like protein, co-immunoprecipitates and colocalizes with both E- and N-cadherin. The 83-kD protein is immunologically distinct from the 92-kD beta-catenin and, because of its molecular mass, likely represents the cadherin-associated protein called gamma-catenin. Thus, two different members of a plakoglobin family associate with N- and E-cadherin and, together with the 102-kD alpha-catenin, appear to participate in linking the cadherins to the actin-based cytoskeleton.

scholarly journals Correlation between cell substrate attachment in vitro and cell surface heparan sulfate affinity for fibronectin and collagen.

1983 ◽  
Vol 96 (6) ◽  
pp. 1820-1823 ◽  
Author(s):  
S C Stamatoglou ◽  
J M Keller
Keyword(s):  
Cell Adhesion ◽  
Cell Surface ◽  
Heparan Sulfate ◽  
Cell Attachment ◽  
Myeloma Cell ◽  
Collagen Type I ◽  
Type I ◽  
Heparan Sulfates ◽  
Sepharose 4B

Heparan sulfate glycosaminoglycan, isolated from the cell surface of nonadhering murine myeloma cells (P3X63-Ag8653), does not bind to plasma fibronectin, but binds partially to collagen type I, as assayed by affinity chromatography with proteins immobilized on cyanogen bromide-activated Sepharose 4B. Identical results were obtained when myeloma heparan sulfate was cochromatographed, on the same fibronectin and collagen columns, with cell surface heparan sulfates collagen columns, with cell surface heparan sulfates from adhering Swiss mouse 3T3 and SV3T3 cells. These latter heparan sulfates do, however, bind to both fibronectin and collagen, as reported earlier (Stamatoglou, S.C., and J.M. Keller, 1981, Biochim. Biophys. Acta., 719:90-97). Cell adhesion assays established that hydrated collagen substrata can support myeloma cell attachment, but fibronectin cannot. Saturation of the heparan sulfate binding sites on the collagen substrata with heparan sulfate or heparin, prior to cell inoculation, abolished the ability to support cell adhesion, whereas chondroitin 4 sulfate, chondroitin 6 sulfate, and hyaluronic acid had no effect.

scholarly journals Fibrillar Collagen Type I Participates in the Survival and Aggregation of Primary Hepatocytes Cultured on Soft Hydrogels

Biomimetics ◽  
2020 ◽  
Vol 5 (2) ◽  
pp. 30
Author(s):  
Nathalia Serna-Márquez ◽  
Adriana Rodríguez-Hernández ◽  
Marisol Ayala-Reyes ◽  
Lorena Omega Martínez-Hernández ◽  
Miguel Ángel Peña-Rico ◽  
...  
Keyword(s):  
Actin Cytoskeleton ◽  
Cell Biology ◽  
Collagen Type ◽  
Cell Aggregation ◽  
Collagen Type I ◽  
Type I ◽  
Primary Hepatocytes ◽  
Cortical Actin ◽  
Fibrillar Collagens

Liver is an essential organ that carries out multiple functions such as glycogen storage, the synthesis of plasma proteins, and the detoxification of xenobiotics. Hepatocytes are the parenchyma that sustain almost all the functions supported by this organ. Hepatocytes and non-parenchymal cells respond to the mechanical alterations that occur in the extracellular matrix (ECM) caused by organogenesis and regenerating processes. Rearrangements of the ECM modify the composition and mechanical properties that result in specific dedifferentiation programs inside the hepatic cells. Quiescent hepatocytes are embedded in the soft ECM, which contains an important concentration of fibrillar collagens in combination with a basement membrane-associated matrix (BM). This work aims to evaluate the role of fibrillar collagens and BM on actin cytoskeleton organization and the function of rat primary hepatocytes cultured on soft elastic polyacrylamide hydrogels (PAA HGs). We used rat tail collagen type I and Matrigel® as references of fibrillar collagens and BM respectively and mixed different percentages of collagen type I in combination with BM. We also used peptides obtained from decellularized liver matrices (dECM). Remarkably, hepatocytes showed a poor adhesion in the absence of collagen on soft PAA HGs. We demonstrated that collagen type I inhibited apoptosis and activated extracellular signal-regulated kinases 1/2 (ERK1/2) in primary hepatocytes cultured on soft hydrogels. Epidermal growth factor (EGF) was not able to rescue cell viability in conjugated BM but affected cell aggregation in soft PAA HGs conjugated with combinations of different proportions of collagen and BM. Interestingly, actin cytoskeleton was localized and preserved close to plasma membrane (cortical actin) and proximal to intercellular ducts (canaliculi-like structures) in soft conditions; however, albumin protein expression was not preserved, even though primary hepatocytes did not remodel their actin cytoskeleton significantly in soft conditions. This investigation highlights the important role of fibrillar collagens on soft hydrogels for the maintenance of survival and aggregation of the hepatocytes. Data suggest evaluating the conditions that allow the establishment of optimal biomimetic environments for physiology and cell biology studies, where the phenotype of primary cells may be preserved for longer periods of time.

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