Culture Conditions Affect Expression of the α6β4 Integrin Associated with Aggressive Behavior in Head and Neck Cancer

Carey, Thomas E.; Laurikainen, Leena; Ptok, A.; Reinke, Timothy; Linder, Keith E.; Nair, Thankam S.; Marcelo, Cynthia L.

doi:10.1007/978-1-4615-3468-6_10

Cited by 3 publications

(3 citation statements)

References 15 publications

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“…In view of the reported association of malignant phenotype and /34 integrin subunit [9,12,13,29,30], the expression of this adhesion molecule in treated and untreated cells was evaluated by immunofiuorescence, immunoprecipitation and Northern blot analyses. We focused our attention on this adhesion molecule, because the evidence that R A may regulate the expression of other molecules (integrins and non-integrins) will not clarify the relationship between metastatic phenotype and /34 expression.…”

Section: Discussionmentioning

confidence: 99%

“…8]. /34 heterodimers do not have clearly defined ligands and functions, but seem involved in tumor progression, being associated with poor prognosis in the case of head and neck tumors [9]. Moreover, the /34 subunit, expressed primarily on epithelial cells and on their oncogenically transformed derivatives, is particularly abundant in lung [10] and colon carcinomas [11] (R. Falcioni, manuscript in preparation).…”

Section: Introductionmentioning

confidence: 98%

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Retinoic acid negatively regulates β4 integrin expression and suppresses the malignant phenotype in a Lewis lung carcinoma cell line

Gaetano¹,

Melchiori²,

Albini³

et al. 1994

Clin Exp Metast

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Retinoic acid (RA) is a potent inhibitor of the malignant phenotype and of tumour cell growth. We observed that in vitro RA treatment of a highly metastatic lung carcinoma cell line (C87) induced a marked reduction in the amount of the beta 4 integrin subunit. The downregulation of this adhesion molecule was assessed by immunofluorescence, immunoprecipitation, and northern analysis. In order to investigate the effects of RA on the malignant phenotype in C87 cells we performed morphological and functional analysis after RA treatment. We found that RA was able to produce marked changes in C87 cell shape, increasing the number of flat cells (90% of the total cell population), and significantly inhibiting the malignant and invasive phenotype of C87 cells. RA treatment suppressed their clonogenic potential in soft agar (control, 20 +/- 5; RA, 0), and strongly reduced their chemotactic and chemoinvasive capacity (chemotaxis: control, 231 +/- 5; RA, 28 +/- 0; chemoinvasion: control, 132 +/- 11; RA = 2 +/- 1). FACS analysis and cell count, however, indicated that RA reduced the growth of C87 cells only partially. After 72 h of treatment we observed only a 10% reduction in the S phase fraction of the cell population. Finally, the reduced lung colony-forming ability, observed after i.v. injection of RA-treated cells (lung foci/animal: RA-treated cells, 1 +/- 0.1; untreated, 8.5 +/- 0.8), further supports the conclusion that in this murine lung carcinoma cell line a marked reduction in the expression of the beta 4 integrin subunit is associated with a marked inhibition of the malignant phenotype.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 98%

Retinoic acid negatively regulates β4 integrin expression and suppresses the malignant phenotype in a Lewis lung carcinoma cell line

Gaetano¹,

Melchiori²,

Albini³

et al. 1994

Clin Exp Metast

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“…The primary ligands for integrins are proteins of the ECM that consist of Type I and IV collagens, fibronectin, laminins, heparin sulfate proteoglycan and other non-collagenous glycoproteins (13). The integrins α6β1, α6β4 and α3β1 are laminin receptors, (14,15) and these integrin pairs are associated with the progression of many epithelial tumors (16)(17)(18). In particular, the α6 subunit is continually expressed during prostate cancer progression and found in micrometastases (8,16,19).…”

Section: Introductionmentioning

confidence: 99%

Synthetic D-amino acid peptide inhibits tumor cell motility on laminin-5

2006

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Cell motility is partially dependent on interactions between the integrins and the extracellular matrix. Our previous studies have identified synthetic D-amino acid cell adhesion peptides using a combinatorial screening approach. In this study, we demonstrate that HYD1 (kikmviswkg) completely blocks random haptotactic migration and inhibits invasion of prostate carcinoma cells on laminin-5. This effect is adhesion independent and reversible. The inhibition of migration by HYD1 involves a dramatic remodeling of the actin cytoskeleton resulting in increased stress fiber formation and actin colocalization with cortactin at the cell membrane. HYD1 interacts with alpha6beta1 (not alpha6beta4) and alpha3beta1 integrins and surprisingly elevates laminin-5-dependent intracellular signals including focal adhesion kinase, mitogen-activated protein kinase kinase and extracellular signal-regulated kinase. HYD1 does not contain a previously characterized binding sequence for integrins. A scrambled derivative of HYD1, called HYDS (wiksmkivkg), does not interact with the alpha6 or alpha3 integrin subunits and is not biologically active. Taken together, these results indicate that HYD1 is a biologically active integrin-targeting peptide that reversibly inhibits tumor cell migration on laminin-5 and uncouples phosphotyrosine signaling from cytoskeletal-dependent migration.

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The minimum element of a synthetic peptide required to block prostate tumor cell migration

Sroka¹,

Mařı́k²,

Pennington³

et al. 2006

Cancer Biology & Therapy

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ABBREVIATIONS Research PaperThe Minimum Element of a Synthetic Peptide Required to Block Prostate Tumor Cell Migration ABSTRACTHuman prostate tumor cell invasion and metastasis are dependent in part on cell adhesion to extracellular matrix proteins and cell migration. We previously identified a synthetic D-amino acid tumor cell adhesion peptide called HYD1 (kikmviswkg) that supported adhesion of tumor cells derived from breast, prostate, ovary and pancreas tissue. Alanine substitution analysis and a peptide deletion strategy were used to determine the minimal element of HYD1 necessary for bioactivity in a prostate cancer cell line called PC3N. Bioactivity was measured by assays of cell adhesion, migration and ERK signaling. The most potent element of HYD1 necessary to support cell adhesion was kmvixw, the block to migration required xkmviswxx and activation of ERK signaling required ikmviswxx. The shortest sequence active in all three assays was iswkg. The HYD1 peptide contains overlapping elements required for adhesion, blocking migration and the activation of ERK signaling. These linear peptide sequences provide the starting point for development of novel compounds to target cancer cell adhesion and migration.

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Culture Conditions Affect Expression of the α6β4 Integrin Associated with Aggressive Behavior in Head and Neck Cancer

Cited by 3 publications

References 15 publications

Retinoic acid negatively regulates β4 integrin expression and suppresses the malignant phenotype in a Lewis lung carcinoma cell line

Retinoic acid negatively regulates β4 integrin expression and suppresses the malignant phenotype in a Lewis lung carcinoma cell line

Synthetic D-amino acid peptide inhibits tumor cell motility on laminin-5

The minimum element of a synthetic peptide required to block prostate tumor cell migration

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