Domains of laminin with growth-factor activity

Panayotou, George; End, Peter; Aumailley, Monique; Timpl, Rupert; Engel, Jürgen

doi:10.1016/0092-8674(89)90987-2

Cited by 324 publications

(122 citation statements)

References 48 publications

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“…The idea that LN5, together with its ␣3␤1 cell surface receptor, has an impact on cell proliferation is consistent with studies on LN1, which indicate that it also may impact cell growth (Panayotou et al, 1989;Mortarini et al, 1995). For example, LN and ␤1 integrins exert a mitogenic effect on human melanoma cells (Ocalan et al, 1988).…”

Section: Discussionsupporting

confidence: 75%

“…In this regard, there has been a recent report that suggests that epithelial cells in mice carrying a ␤4 cytoplasmic deletion have some cell cycle defects (Murgia et al, 1998). Because the epithelial tissues in the mutant mice appear relatively normal, we hypothesize that ␣3␤1 integrin may well compensate for the functionally impaired ␣6␤4 integrin heterodimer.The idea that LN5, together with its ␣3␤1 cell surface receptor, has an impact on cell proliferation is consistent with studies on LN1, which indicate that it also may impact cell growth (Panayotou et al, 1989; M. Gonzales et al Mortarini et al, 1995). For example, LN and ␤1 integrins exert a mitogenic effect on human melanoma cells (Ocalan et al, 1988).…”

supporting

confidence: 72%

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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: Discussionsupporting

confidence: 75%

supporting

confidence: 72%

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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“…The interaction with matrix molecules also appears to be required for ciliary neurotrophic factor to induce certain types of astrocyte differentiation (Lillien et al, 1990), and in experiments similar to those reported here, it was shown that a laminin substratum is required for the response of Schwann cells to an undefined mitogen (Porter et al, 1987) . Extracellular matrix proteins such as laminin contain many EGF precursor repeats that Schubert and Kimura Substratum Regulation of Growth Factor Mitogenicity have been implicated in developmental processes as well as the stimulation of cell division (Panayotou et al ., 1989;Davis, 1990) . The P19 response to activin A and bFGF in the presence oflaminin does not, however, appear to be simply related to EGF receptoroccupancy, for EGF is not synergistic with bFGF or activin A when P19 cells are grown on tissue culture plastic .…”

Section: Resultsmentioning

confidence: 99%

Substratum-growth factor collaborations are required for the mitogenic activities of activin and FGF on embryonal carcinoma cells.

Schubert

Kimura

1991

The Journal of Cell Biology

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“…This activity appears to originate in domain 1 of the moleculer which is rich in EGF-like repeats, and it has been suggested that this part of the molecule may be accessible to cells only during early stages of tissue development or following injury, where the basement membrane is either not intact or has been damaged (Panayotou et al, 1989). Thus the co-injection of cells with purified laminin may imitate this situation, causing increasing cell growth, although the situation is a complex one and other factors such as interaction with host proteins could be involved.…”

Section: Resultsmentioning

confidence: 99%

Effect of reconstituted basement membrane components on the growth of a panel of human tumour cell lines in nude mice

Topley

Jenkins²,

Jessup³

et al. 1993

Br J Cancer

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Sunmmary Previous reports have indicated that reconstituted basement membrane (matrigel), when co-injected with either established or primary human tumour cells, can improve the growth of subcutaneous xenografts in nude mice. The human adenocarcinoma cell lines A549, SW480, and WiDr, and the human fibrosarcoma cell line HT1080scc2 exhibit varying degrees of tumourigenicity in nude mice. All these lines showed increased tumourigenicity and/or growth rate, together with a change towards a more differentiated tissue morphology, when co-injected with matrigel into nude mice. Experiments using A549 cell line have indicated that the effect of matrigel is concentration-dependent and that increased growth rate is not maintained when xenografts grown with matrigel are passaged into further mice. These results strongly suggest that increased tumour growth results from the improved growth conditions afforded by matrigel, rather than from the selection of subpopulations of the most tumourigenic cells. Increased growth of intracaecal tumours arising from the co-injection of SW480 cells with matrigel, indicate a possible use for matrigel in the development of more relevant animal models using the orthotopic site. Purified laminin significantly increased the growth of sc tumours resultant from co-injection with either WiDr or A549 cells, whereas collagen IV or laminin with entactin showed no such effect. A role for free laminin in the stimulation of cell growth in the absence of an intact basement membrane is discussed.

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Domains of laminin with growth-factor activity

Cited by 324 publications

References 48 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

Substratum-growth factor collaborations are required for the mitogenic activities of activin and FGF on embryonal carcinoma cells.

Effect of reconstituted basement membrane components on the growth of a panel of human tumour cell lines in nude mice

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