Signal transduction by cell adhesion receptors

Rosales, Carlos; O'Brien, Vincent; Kornberg, Lori; Juliano, R. L.

doi:10.1016/0304-419x(95)00005-z

Cited by 138 publications

(110 citation statements)

References 252 publications

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“…In fact, PBMCs spontaneously adhered to SaOS-2 cells partly through j32-integrin. Cell adhesion receptors including integrins function in the signal transduction process leading to the regulation of cell growth and differentiation [28]. Another possibility is that soluble factors released from PBMCs and/or SaOS-2 cells might bind to their specific receptors on PBMCs to induce the signal transduction process, finally leading to the differentiation of PBMCs into osteoclasts.…”

Section: Il-1~3 Stimulates the Formation Of Trap Positive Mncs From Pmentioning

confidence: 99%

Interleukin-1.BETA. Stimulates Transendothelial Mobilization of Human Peripheral Blood Mononuclear Cells with a Potential to Differentiate into Osteoclasts in the Presence of Osteoblasts.

et al. 2001

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Abstract.There is accumulating evidence that interleukin-1 (IL-1) levels are increased locally at the site of active bone resorption in a variety of diseases including osteoporosis, periodontal disease and rheumatoid arthritis. However, the pathogenic role of IL-1 in bone loss remains to be fully elucidated.We present here additional evidence that IL-19 enhances endothelial activation and thereby stimulates mobilization of peripheral blood mononuclear cells (PBMCs) from luminal to abluminal spaces across the endothelium. Furthermore, IL-l jl stimulates the differentiation of PBMCs into osteoclast-like cells with bone-resorbing activity in the presence of human osteoblastic SaOS-2 cells without systemic hormones.These findings provide circumstantial evidence for the hypothesis that IL-19 generated in the bone microenviroment plays a stimulatory role in PBMC mobilization from the peripheral circulation and their subsequent differentiation into osteoclast-like cells in the bone tissue. In addition, the present study supports the notion that osteoclast progenitor cells might be derived from the peripheral circulating blood mononuclear cells in human.

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Section: Il-1~3 Stimulates the Formation Of Trap Positive Mncs From Pmentioning

confidence: 99%

Interleukin-1.BETA. Stimulates Transendothelial Mobilization of Human Peripheral Blood Mononuclear Cells with a Potential to Differentiate into Osteoclasts in the Presence of Osteoblasts.

et al. 2001

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“…Based on data that suggest that MAP kinase mediates the regulatory effects of extracellular matrix and integrin receptors on cell cycle progression, we evaluated the degree of MAP kinase activation in both 804G and MCF-10A cells after various treatments (Rosales et al, 1995;Howe et al, 1998;Schlaepfer and Hunter, 1998). For these studies we used an antibody (anti-ACTIVE MAPK p42/p44), specific for phosphorylated, activated p42/p44 in combination with an antibody (antip42/p44) that recognizes p42/p44 irrespective of its activation state.…”

Section: Is Map Kinase Involved?mentioning

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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“…In addition to providing a structural link between cells and the extracellular matrix, focal adhesions represent important sites for signal transduction (reviewed in [3][4][5]). Notably, several known signalling enzymes, including protein kinase C (PKC) [6,7], c-Src [8][9][10] and the non-receptor tyrosine kinase, focal adhesion kinase (FAK) [11][12][13][14][15][16], are localized to these sites.…”

Section: Introductionmentioning

confidence: 99%

Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin

Bellis

Perrotta

Curtis

et al. 1997

Biochemical Journal

110

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Tyrosine phosphorylation of paxillin by the focal adhesion kinase (FAK) has been implicated as a signal transduction mechanism associated with cell adhesion and cytoskeletal reorganization. The potential role of serine phosphorylation of paxillin in these events has not been well characterized. In this study we have examined the phosphorylation profile of paxillin both invitro and invivo. By using glutathione S-transferase–paxillin fusion proteins in precipitation-kinase assays invitro we observed that a fusion protein spanning amino acid residues 54–313 of paxillin, and containing a FAK-binding site, precipitated substantial serine kinase activity as well as FAK activity from a smooth-muscle lysate. Together these kinases phosphorylated paxillin on tyrosine residue 118, a site that has been identified previously as a target for FAK phosphorylation, and on serine residues 188 and/or 190. The binding site for the serine kinase, the identity of which is currently unknown, was further mapped to residues 168–191 of paxillin. To assess the physiological relevance of these sites phosphorylated invitro, the profile of paxillin phosphorylation invivo stimulated by seeding fibroblasts on fibronectin was characterized. As expected, plating cells on fibronectin enhanced the tyrosine phosphorylation of paxillin. However, 96% of the phosphorylation of paxillin occurred on serine residues. Comparison by two-dimensional phosphopeptide analyses indicated that the major sites of tyrosine and serine phosphorylation detected in the assays invitro co-migrate with phosphopeptides derived from paxillin phosphorylated invivo in response to plating cells on fibronectin. These findings support a role for both tyrosine and serine kinases in the signal transduction pathway linking integrin activation to paxillin phosphorylation.

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Signal transduction by cell adhesion receptors

Cited by 138 publications

References 252 publications

Interleukin-1.BETA. Stimulates Transendothelial Mobilization of Human Peripheral Blood Mononuclear Cells with a Potential to Differentiate into Osteoclasts in the Presence of Osteoblasts.

Interleukin-1.BETA. Stimulates Transendothelial Mobilization of Human Peripheral Blood Mononuclear Cells with a Potential to Differentiate into Osteoclasts in the Presence of Osteoblasts.

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

Adhesion of fibroblasts to fibronectin stimulates both serine and tyrosine phosphorylation of paxillin

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