Function and regulation of melanoma–stromal fibroblast interactions: when seeds meet soil

Li, Gang; Satyamoorthy, Kapaettu; Meier, Friedegund; Berking, Carola; Bogenrieder, Thomas; Herlyn, Meenhard

doi:10.1038/sj.onc.1206455

Cited by 167 publications

(140 citation statements)

References 100 publications

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“…Similar circuitries have been shown for growth factors, such as HGF, interleukin-8 and PDGF-AA, to support the proliferation, survival and migration of melanoma cells [124].…”

Section: Taddei Et Alsupporting

confidence: 59%

Anoikis: an emerging hallmark in health and diseases

Taddei

Giannoni

Fiaschi

et al. 2011

The Journal of Pathology

466

401

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Anoikis is a programmed cell death occurring upon cell detachment from the correct extracellular matrix, thus disrupting integrin ligation. It is a critical mechanism in preventing dysplastic cell growth or attachment to an inappropriate matrix. Anoikis prevents detached epithelial cells from colonizing elsewhere and is thus essential for tissue homeostasis and development. As anchorage-independent growth and epithelial-mesenchymal transition, two features associated with anoikis resistance, are crucial steps during tumour progression and metastatic spreading of cancer cells, anoikis deregulation has now evoked particular attention from the scientific community. The aim of this review is to analyse the molecular mechanisms governing both anoikis and anoikis resistance, focusing on their regulation in physiological processes, as well as in several diseases, including metastatic cancers, cardiovascular diseases and diabetes.

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“…Similar circuitries have been shown for growth factors, such as HGF, interleukin-8 and PDGF-AA, to support the proliferation, survival and migration of melanoma cells [124].…”

Section: Taddei Et Alsupporting

confidence: 59%

Anoikis: an emerging hallmark in health and diseases

Taddei

Giannoni

Fiaschi

et al. 2011

The Journal of Pathology

466

401

View full text Add to dashboard Cite

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“…To analyze expression of CK1α during melanoma progression, we first evaluated expression of CK1α and its target β-catenin in several well-defined human melanoma cell lines derived either from primary melanomas or from melanoma metastases (18)(19)(20). We found RNA and protein expression of CK1α to be significantly reduced in metastatic compared with nonmetastatic melanoma cells, whereas β-catenin expression is strongly increased and the protein preferentially localized in the nucleus in metastatic melanoma cells (Fig.…”

Section: Resultsmentioning

confidence: 99%

Suppression of Casein Kinase 1α in Melanoma Cells Induces a Switch in β-Catenin Signaling to Promote Metastasis

et al. 2010

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Casein kinase 1 α (CK1α) is a multifunctional Ser/Thr kinase that phosphorylates several substrates. Among those is β-catenin, an important player in cell adhesion and Wnt signaling. Phosphorylation of β-catenin by CK1α at Ser45 is the priming reaction for the proteasomal degradation of β-catenin. Interestingly, aside from this role in β-catenin degradation, very little is known about the expression and functional role of CK1α in tumor cells. Here, we show that CK1α expression in different tumor types is either strongly suppressed or completely lost during tumor progression and that CK1α is a key factor determining β-catenin stability and transcriptional activity in tumor cells. CK1α reexpression in metastatic melanoma cells reduces growth in vitro and metastasis formation in vivo, and induces cell cycle arrest and apoptosis, whereas suppression of CK1α in primary melanoma cells induces invasive tumor growth. Inactivation of CK1α promotes tumor progression by regulating a switch in β-catenin-mediated signaling. These results show that melanoma cells developed an efficient new mechanism to activate the β-catenin signaling pathway and define CK1α as a novel tumor suppressor. Cancer Res; 70(17); 6999-7009. ©2010 AACR.

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“…This will allow for the examination of cooperativity between the ␣ 2 ␤ 1 integrin and CD44/CSPG. In addition, peptide amphiphiles can be used to probe receptor-mediated events in co-culture systems, further defining the stimuli for cross-talk within the melanoma microenvironment (101)(102)(103)(104). Peptide amphiphile ligands ultimately provide a general approach for monitoring receptor-mediated regulation of proteolysis in cellular systems.…”

Section: Discussionmentioning

confidence: 99%

Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by α2β1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen

Baronas-Lowell

Lauer‐Fields

Borgia³

et al. 2004

Journal of Biological Chemistry

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Tumor cell binding to components of the basement membrane is well known to trigger intracellular signaling pathways. Signaling ultimately results in the modulation of gene expression, facilitating metastasis. Type IV collagen is the major structural component of the basement membrane and is known to be a polyvalent ligand, possessing sequences bound by the ␣ 1 ␤ 1 , ␣ 2 ␤ 1 , and ␣ 3 ␤ 1 integrins, as well as cell surface proteoglycan receptors, such as CD44/chondroitin sulfate proteoglycan (CSPG). The role of ␣ 2 ␤ 1 integrin and CD44/CSPG receptor binding on human melanoma cell activation has been evaluated herein using triple-helical peptide ligands incorporating the ␣1(IV)382-393 and ␣1(IV)1263-1277 sequences, respectively. Gene expression and protein production of matrix metalloproteinases-1 (MMP-1), -2, -3, -13, and -14 were modulated with the ␣ 2 ␤ 1 -specific sequence, whereas the CD44-specific sequence yielded significant stimulation of MMP-8 and lower levels of modulation of MMP-1, -2, -13, and -14. Analysis of enzyme activity confirmed different melanoma cell proteolytic potentials based on engagement of either the ␣ 2 ␤ 1 integrin or CD44/CSPG. These results are indicative of specific activation events that tumor cells undergo upon binding to select regions of basement membrane collagen. Based on the present study, triple-helical peptide ligands provide a general approach for monitoring the regulation of proteolysis in cellular systems.Melanoma is one of the most rapidly increasing malignancies in the world in both young and old patients, with over 50,000 newly diagnosed patients each year (1). 1 Mortality from cancer is frequently due to metastasis, given that surgical excision of the primary tumor considerably enhances the prognosis of a patient and prolongs survival (2). Metastasis is a complex series of finely coordinated events that results in cancer cells circulating in lymph and blood vascular systems to invade remote tissues and establish secondary sites of tumor growth (3). Extravasation of the tumor cell into secondary tissues requires alterations in cellular behaviors, resulting from specific adhesion to components of the basement membrane. Tumor cells respond to each of the various components of the ECM, 2 including the collagens; noncollagenous glycoproteins, such as fibronectin and laminin; and proteoglycans, such as decorin and syndecan (4). These interactions are known to occur through several families of cell surface receptors, including the integrins and cell surface proteoglycans.Integrins are heterodimeric proteins composed of one ␣ and one ␤ subunit and are the best described of the cell surface adhesion molecules. To date, there are 18 different ␣ subunits and 8 distinct ␤ subunits identified that combine to form at least 24 heterodimers (5-7). Although the specific integrin expression profile can fluctuate with tumor type and stage of progression, highly metastatic melanoma cells are known to up-regulate expression of, and ␣ 6 ␤ 4 integrins while down-regulating the expression ...

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Function and regulation of melanoma–stromal fibroblast interactions: when seeds meet soil

Cited by 167 publications

References 100 publications

Anoikis: an emerging hallmark in health and diseases

Anoikis: an emerging hallmark in health and diseases

Suppression of Casein Kinase 1α in Melanoma Cells Induces a Switch in β-Catenin Signaling to Promote Metastasis

Differential Modulation of Human Melanoma Cell Metalloproteinase Expression by α2β1 Integrin and CD44 Triple-helical Ligands Derived from Type IV Collagen

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