Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes.

Carter, W G; Kaur, Pritinder; Gil, Susana G.; Gahr, Pamaia J.; Wayner, Elizabeth A.

doi:10.1083/jcb.111.6.3141

Cited by 426 publications

(305 citation statements)

References 56 publications

(86 reference statements)

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“…Integrin b4 is another cellular attachment receptor which forms a a6b4 heterodimer in many epithelia (Stepp et al, 1990;Sonnenberg et al, 1991) and is required for cell adhesion on basal lamina via laminins (Kajiji et al 1989;Carter et al, 1990), forming hemidesmosomes (Jones et al, 1991; A B CE, columner epithelium; S, stroma Sonnenberg et al, 1991;Dowling et al, 1996). Considering previous cell kinetic analyses that stem cells divide only rarely under normal steady-state conditions (Potten and Morris, 1988;Cotsarelis et al, 1990;Lavker et al, 1991;Loe er and Potten, 1997), our present observations lead us to propose that the p75 NGFR -expressing cells are a speci®c basal cell subset, such as precursor cells, of the regenerating human epithelial tissues (Loe er and Potten, 1997).…”

Section: Discussionmentioning

confidence: 99%

Telomerase activity in a specific cell subset co-expressing integrinβ1/EGFR but not p75NGFR/bcl2/integrin β4 in normal human epithelial cells

Kikuchi

Ahmed

et al. 1998

Oncogene

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Telomerase activity is correlated with the immortality of various cultured cells and cancer cells. The activity, however, is also demonstrated in various normal regenerating cells which normally have a ®nite life span in vivo and in vitro, though its biological implication remains unclear. Using cultured normal human epithelial cells, we show that telomerase activity is associated with epithelial cell subsets which actively proliferate in vitro. Unlike in most cancer cell lines, telomerase activity was evidently up-regulated when the cells entered into S phase in primary human epithelial cells. To characterize the cells which have telomerase activity, the primary human epithelial cell population of uterine cervix was dissociated into several distinctive cellular subsets by means of immunocytochemical cell fractionation. Telomerase activity was found to be closely associated with the subset which expressed predominantly integrin b1 and epidermal growth factor receptor. We further identi®ed the telomerase-negative subpopulation which contained a small subset that strongly coexpresses p75 NGFR low a nity nerve growth factor receptor, integrin b4 and bcl-2 protein. The location of the p75 NGFR -expressing cells contrasts to that of the Ki-67 positive cells in vivo and is distinctive of telomerase positive cycling cells, indicating that these cells remain at the G0 phase. The present study supports the notion that telomerase activity is linked to cell cycle regulation, implying that telomerase is activated upon cell proliferation in regenerating normal human epithelial cells.

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Section: Discussionmentioning

confidence: 99%

Telomerase activity in a specific cell subset co-expressing integrinβ1/EGFR but not p75NGFR/bcl2/integrin β4 in normal human epithelial cells

Kikuchi

Ahmed

et al. 1998

Oncogene

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“…This result gave us a clue as to the nature of the receptor involved in LN5 regulation of cell growth, because cell interaction with both of these particular matrix molecules can be mediated by the ␣3␤1 integrin heterodimer (Carter et al, 1990;Elices et al, 1991;Hynes, 1992). The use of human cells enabled us to further this aspect of our study, because we could assess whether a well-characterized ␤1 integrin antibody that activates its human antigen in the absence of ligand could rescue the proliferation of MCF-10A cells treated with an inhibitory LN5 antibody (van de Wiel-van Kemenade et al, 1992).…”

Section: Discussionmentioning

confidence: 99%

“…Comparable studies using 804G cells were not possible because of lack of availability of an appropriate set of inhibitory and activating anti-rat integrin antibodies. LN5 has two known integrin receptors, ␣3␤1 and ␣6␤4 (Carter et al, 1990). Thus we made use of antibodies (P1B5 and GoH3) that perturb ␣3 and ␣6 integrin function, respectively.…”

Section: Antibodies Against the Human ␣3 Ln Subunit Inhibit Proliferamentioning

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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“…Laminin-332 interacts with two major epithelial integrin a3b1 and a6b4, and promotes the formation of two separate types of attachment structure, focal adhesion and stable anchoring contacts (Carter et al, 1990). In several types of carcinomas, laminin-332 has been reported to be highly expressed and to correlate well with poor patient prognosis (Pyke et al, 1995;Soini et al, 1996;Koshikawa et al, 1999;Matta et al, 1999;Ono et al, 1999;Yamamoto et al, 2001;Fukai et al, 2005).…”

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confidence: 99%

Laminin-332 promotes the invasion of oesophageal squamous cell carcinoma via PI3K activation

et al. 2008

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Laminin-332 is major component of epithelial basement membrane, and has an important role in cell migration and tumour invasion. Recently, the phosphatidylinositol 3-kinase (PI3K) activation induced by laminin-332 during carcinogenesis or tumour invasion has been highlighted in skin squamous cell carcinoma. The expression of laminin-332 in 126 resected oesophageal squamous cell carcinoma (ESCC) specimens was immunohistochemically examined to determine its associations with the clinicopathological characteristics, and the effect of laminin-332 on the invasiveness and the PI3K activation was assessed by in vitro experiments using ESCC cell lines (ESCCs). Sections with immunostaining signals in 430% cancer cells, which were observed in 55 of 126 cases, were judged to be positive for laminin-332. The positivity was significantly correlated with pTNM stage and poor prognosis. Inactivation of the PI3K pathway by laminin-332 blocking antibody suppressed the invasiveness of TE8 cell line, which secreted laminin-332 at high level and had high PI3K activity. The addition of the purified laminin-332 activated the PI3K pathway and increased the invasiveness of TE11 cell line, which secreted laminin-332 at lower level and had low PI3K activity. The deactivation of PI3K pathway using the PI3K inhibitor decreased the invasiveness of ESCCs and the secretion of laminin-332 in vitro. The expression of laminin-332 was one of the prognostic factors of ESCC. Laminin-332 could provide the autocrine positive-feedback loop through PI3K activation, contributing the invasive ability. Therefore, the inhibitor of PI3K pathway might be useful as the anticancer therapies for ESCC.

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Distinct functions for integrins alpha 3 beta 1 in focal adhesions and alpha 6 beta 4/bullous pemphigoid antigen in a new stable anchoring contact (SAC) of keratinocytes: relation to hemidesmosomes.

Cited by 426 publications

References 56 publications

Telomerase activity in a specific cell subset co-expressing integrinβ1/EGFR but not p75NGFR/bcl2/integrin β4 in normal human epithelial cells

Telomerase activity in a specific cell subset co-expressing integrinβ1/EGFR but not p75NGFR/bcl2/integrin β4 in normal human epithelial cells

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

Laminin-332 promotes the invasion of oesophageal squamous cell carcinoma via PI3K activation

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