Formation of hemidesmosomes in vitro by a transformed rat bladder cell line.

Riddelle, Kathryn S.; Green, Kathleen J.; Jones, Jonathan

doi:10.1083/jcb.112.1.159

Cited by 78 publications

(79 citation statements)

References 40 publications

(45 reference statements)

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“…804G cells were maintained as previously detailed (Riddelle et al, 1991). MCF-10A cells were obtained from American Type Culture Collection (Rockville, MD) and were maintained in a 1:1 mix of Dulbecco's modified Eagle medium and Ham's F-12 medium supplemented with 5% equine serum, 0.01 mg/ml insulin, 20 ng/ml epidermal growth factor (EGF), 100 ng/ml cholera toxin, and 500 ng/ml hydrocortisone.…”

Section: Cell Culturementioning

confidence: 99%

A Cell Signal Pathway Involving Laminin-5, α3β1 Integrin, and Mitogen-activated Protein Kinase Can Regulate Epithelial Cell Proliferation

Gonzales¹,

Haan²,

Baker³

et al. 1999

MBoC

148

105

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Laminin-5 (LN5) is a matrix component of epithelial tissue basement membranes and plays an important role in the initiation and maintenance of epithelial cell anchorage to the underlying connective tissue. Here we show that two distinct LN5 function-inhibitory antibodies, both of which bind the globular domain of the ␣3 subunit, inhibit proliferation of epithelial cells. These same antibodies also induce a decrease in mitogenactivated protein kinase activity. Inhibition of proliferation by the function-perturbing LN5 antibodies is reversed upon removal of the antibodies and can be overcome by providing the antibody-treated cells with exogenous LN5 and rat tail collagen. Because epithelial cells use the integrin receptor ␣3␤1 to interact with both LN5 and rat tail collagen, we next investigated the possibility that integrin ␣3␤1 is involved in mediating the proliferative impact of LN5. Proliferation of human epithelial cells is significantly inhibited by a function-perturbing ␣3 integrin antibody. In addition, antibody activation of ␤1 integrin restores the proliferation of epithelial cells treated with LN5 functionperturbing antibodies. These data indicate that a complex comprising LN5 and ␣3␤1 integrin is multifunctional and contributes not only to epithelial cell adhesion but also to the regulation of cell growth via a signaling pathway involving mitogen-activated protein kinase. We discuss our study in light of recent evidence that LN5 expression is up-regulated at the leading tips of tumors, where it may play a role in tumor cell proliferation. INTRODUCTIONCell interaction with elements of the extracellular matrix impacts their adherence, motility, as well as protein and gene expression (for example, see Adams and Watt, 1993;Roskelly et al., 1995). In intact normal tissue epithelial cells bind to extracellular matrix molecules, which are organized into a complex multiprotein structure called the basement membrane. The major components of the latter include type IV collagen, proteoglycans, and laminins. One laminin isoform, laminin-5 (LN5), 1 in particular plays an important role in establishing firm adherence of epithelial cells to the basement membrane, because it is necessary for the assembly and maintenance of stable anchorage devices between epithelial cells and matrix called hemidesmosomes (Baker et al., 1996;Green and Jones, 1996). However, recent reports also indicate that LN5 is expressed at the budding tips of invading tumor cells, i.e., at sites where cancer cells are undergoing cell division but where there are most likely no hemidesmosomes (Pyke et al., 1994(Pyke et al., , 1995. This provides an indication § Corresponding author. E-mail address: j-jones3@nwu.edu. 1 Abbreviations used: BrdU, bromodeoxyuridine; DAPI, 4,6-diamidino-2-phenylindole; EGF, epidermal growth factor; FN, fibronectin; hLN5, human laminin-5; Ig, immunoglobulin; LN, laminin; MAP, mitogen-activated protein; MAPK, MAP kinase; RTC, rat tail collagen; rtLN5, rat laminin-5.© 1999 by The American Society for Cell Biology 259 that L...

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Section: Cell Culturementioning

confidence: 99%

A Cell Signal Pathway Involving Laminin-5, α3β1 Integrin, and Mitogen-activated Protein Kinase Can Regulate Epithelial Cell Proliferation

Gonzales¹,

Haan²,

Baker³

et al. 1999

MBoC

148

105

View full text Add to dashboard Cite

show abstract

“…Single-and double-label immunofluorescence was performed as detailed previously (Riddelle et al, 1991). After mounting, coverslips were viewed on a Zeiss (Thornwood, NY) LSM510 confocal microscope fitted with appropriate filters for visualization of GFP as well as fluorescein-and rhodamine-conjugated probes (Zeiss).…”

Section: Immunofluorescence Microscopymentioning

confidence: 99%

“…For these studies, we used 804G cells because these cells express all of the known hemidesmosome proteins and assemble bona fide hemidesmosomes in vitro (Riddelle et al, 1991). 804G cells were grown to ϳ60% confluence and then transfected according to standard procedures (see Hopkinson et al, 1995).…”

Section: Transfection Analysesmentioning

confidence: 99%

“…A mouse IgM mAb preparation (1804b) against the N-terminal domain of BP180 was described by Hopkinson et al (1992) and Riddelle et al (1991). J17 rabbit antiserum was generated against the same BP180 domain (Hopkinson et al, 1992).…”

Section: Antibodiesmentioning

confidence: 99%

“…804G cells were cultured as detailed by Riddelle et al (1991). 804G cells were maintained for 72 h on 22-mm glass coverslips.…”

Section: Cell Culture and Transfection Proceduresmentioning

confidence: 99%

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The N Terminus of the Transmembrane Protein BP180 Interacts with the N-terminal Domain of BP230, Thereby Mediating Keratin Cytoskeleton Anchorage to the Cell Surface at the Site of the Hemidesmosome

Hopkinson

Jones

2000

MBoC

106

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In epidermal cells, the keratin cytoskeleton interacts with the elements in the basement membrane via a multimolecular junction called the hemidesmosome. A major component of the hemidesmosome plaque is the 230-kDa bullous pemphigoid autoantigen (BP230/BPAG1), which connects directly to the keratin-containing intermediate filaments of the cytoskeleton via its C terminus. A second bullous pemphigoid antigen of 180 kDa (BP180/BPAG2) is a type II transmembrane component of the hemidesmosome. Using yeast two-hybrid technology and recombinant proteins, we show that an N-terminal fragment of BP230 can bind directly to an N-terminal fragment of BP180. We have also explored the consequences of expression of the BP230 N terminus in 804G cells that assemble hemidesmosomes in vitro. Unexpectedly, this fragment disrupts the distribution of BP180 in transfected cells but has no apparent impact on the organization of endogenous BP230 and ␣6␤4 integrin. We propose that the BP230 N terminus competes with endogenous BP230 protein for BP180 binding and inhibits incorporation of BP180 into the cell surface at the site of the hemidesmosome. These data provide new insight into those interactions of the molecules of the hemidesmosome that are necessary for its function in integrating epithelial and connective tissue types.

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Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: Involvement of IFAP300 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of α6A integrin

Baker

Skalli

Goldman

et al. 1997

Cell Motil. Cytoskeleton

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Formation of hemidesmosomes in vitro by a transformed rat bladder cell line.

Cited by 78 publications

References 40 publications

A Cell Signal Pathway Involving Laminin-5, α3β1 Integrin, and Mitogen-activated Protein Kinase Can Regulate Epithelial Cell Proliferation

A Cell Signal Pathway Involving Laminin-5, α3β1 Integrin, and Mitogen-activated Protein Kinase Can Regulate Epithelial Cell Proliferation

The N Terminus of the Transmembrane Protein BP180 Interacts with the N-terminal Domain of BP230, Thereby Mediating Keratin Cytoskeleton Anchorage to the Cell Surface at the Site of the Hemidesmosome

Laminin-5 and modulation of keratin cytoskeleton arrangement in FG pancreatic carcinoma cells: Involvement of IFAP300 and evidence that laminin-5/cell interactions correlate with a dephosphorylation of α6A integrin

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