The effect of sub-lethal ALA-PDT on the cytoskeleton and adhesion of cultured human cancer cells

Uzdensky, Anatoly B.; Kolpakova, Elona; Juzeniene, Asta; Juzenas, Petras; Moan, Johan Emelian

doi:10.1016/j.bbagen.2004.11.011

Cited by 44 publications

(36 citation statements)

References 34 publications

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“…In addition, this reduced metastatic potential is also linked to the direct impairment of adhesion molecules at the plasma membrane [15,30] or indirect deterioration of cell adhesion [16,31]. In fact, following ALA-PDT, all the cancer cells used in this study also showed transient morphological alterations and increased adherence as previously found in NIH3T3 cells [17].…”

Section: Discussionsupporting

confidence: 60%

ALA‐PDT results in phenotypic changes and decreased cellular invasion in surviving cancer cells

Tsai

Chiang

et al. 2009

Lasers Surg Med

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Section: Discussionsupporting

confidence: 60%

ALA‐PDT results in phenotypic changes and decreased cellular invasion in surviving cancer cells

Tsai

Chiang

et al. 2009

Lasers Surg Med

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“…Cell adhesion to the extracellular matrix was determined as previously described (30,56,59). Briefly, cells were plated at a density of 50,000 cells per well in a 12-well plate.…”

Section: Methodsmentioning

confidence: 99%

Gastrin-releasing peptide mediates its morphogenic properties in human colon cancer by upregulating intracellular adhesion protein-1 (ICAM-1) via focal adhesion kinase

Taglia

Matusiak²,

Benya³

2007

American Journal of Physiology-Gastrointestinal and Liver Physi

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Gastrin-releasing peptide (GRP) and its receptor (GRPR) act as morphogens when expressed in colorectal cancer (CRC), promoting the assumption of a better differentiated phenotype by regulating cell motility in the context of remodeling and retarding tumor cell metastasis by enhancing cell-matrix attachment. Although we have shown that these processes are mediated by focal adhesion kinase (FAK), the downstream target(s) of GRP-induced FAK activation are not known. Since osteoblast differentiation is mediated by FAK-initiated upregulation of ICAM-1 (Nakayamada S, Okada Y, Saito K, Tamura M, Tanaka Y. J Biol Chem 278: 45368-45374, 2003), we determined whether GRP-induced activation of FAK alters ICAM-1 expression in CRC and, if so, determined the contribution of ICAM-1 to mediating GRP's morphogenic properties. Caco-2 and HT-29 cells variably express GRP/GRPR. These cells only express ICAM-1 when GRPR are present. In human CRC, GRPR and ICAM-1 are only expressed by better differentiated tumor cells, with ICAM-1 located at the basolateral membrane. ICAM-1 expression was only observed subsequent to GRPR signaling via FAK. To study the effect of ICAM-1 expression on tumor cell motility, CRC cells expressing GRP, GRPR, and ICAM-1 were cultured in the presence and absence of GRPR antagonist or monoclonal antibody to ICAM-1. CRC cells engaged in directed motility in the context of remodeling and were highly adherent to the extracellular matrix, only in the absence of antagonist or ICAM-1 antibody. These data indicate that GRP upregulation of ICAM-1 via FAK promotes tumor cell motility and attachment to the extracellular matrix.

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“…The strength of cell to culture dish attachment was quantified by the "cell detachment assay" (28,29). Total number of viable cells was evaluated by Cell Counting Kit-8 (Dojindo) before and after incubation with a dissociation solution containing 5 mmol/L EDTA in PBS (−) for 10 min.…”

Section: Cellmentioning

confidence: 99%

Critical Roles of Mucin 1 Glycosylation by Transactivated PolypeptideN-Acetylgalactosaminyltransferase 6 in Mammary Carcinogenesis

et al. 2010

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The structure of O-glycosylated proteins is altered in breast cancer cells, but the mechanisms of such an aberrant modification have been largely unknown. We here report critical roles of a novel druggable target, polypeptide N-acetylgalactosaminyltransferase 6 (GALNT6), which is upregulated in a great majority of breast cancers and encodes a glycosyltransferase responsible for initiating mucin-type O-glycosylation. Knockdown of GALNT6 by small interfering RNA significantly enhanced cell adhesion function and suppressed the growth of breast cancer cells. Western blot and immunostaining analyses indicated that wild-type GALNT6 protein could glycosylate and stabilize an oncoprotein mucin 1 (MUC1), which was upregulated with GALNT6 in breast cancer specimens. Furthermore, knockdown of GALNT6 or MUC1 led to similar morphologic changes of cancer cells accompanied by the increase of cell adhesion molecules β-catenin and E-cadherin. Our findings implied that overexpression of GALNT6 might contribute to mammary carcinogenesis through aberrant glycosylation and stabilization of MUC1 and that screening of GALNT6 inhibitors would be valuable for the development of novel therapeutic modalities against breast cancer. Cancer Res; 70(7); 2759-69. ©2010 AACR.

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The effect of sub-lethal ALA-PDT on the cytoskeleton and adhesion of cultured human cancer cells

Cited by 44 publications

References 34 publications

ALA‐PDT results in phenotypic changes and decreased cellular invasion in surviving cancer cells

ALA‐PDT results in phenotypic changes and decreased cellular invasion in surviving cancer cells

Gastrin-releasing peptide mediates its morphogenic properties in human colon cancer by upregulating intracellular adhesion protein-1 (ICAM-1) via focal adhesion kinase

Critical Roles of Mucin 1 Glycosylation by Transactivated PolypeptideN-Acetylgalactosaminyltransferase 6 in Mammary Carcinogenesis

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