Expression of intercellular adhesion molecule-1 and prognosis in colorectal cancer

Maeda, Kiyoshi; Kang, Soon-Myoung; Sawada, Tetsuji; Nishiguchi, Yukio; Yashiro, Masakazu; Ogawa, Yoshinari; Ohira, Masaichi; Ishikawa, Tetsuro; Chung, Kyukwang

doi:10.3892/or.9.3.511

Cited by 68 publications

(86 citation statements)

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“…In this study, we investigated whether ICAM-3 increased cell migration and invasion because it has been shown that ICAM family proteins activate several proteins such as integrin molecules and IKK proteins involved in cancer invasion (15,17,18). As ICAM-3 over-expressing stable transfectant displayed elevated migration and invasion ability, we attempted to identify the molecule driving migration and invasion.…”

Section: Icam-3 Enhances the Migratory And Invasive Potential Of Humamentioning

confidence: 99%

“…Interestingly, the ICAM proteins appear to have a dual role in cancer. ICAM molecules may target and block tumor progression by stimulation of an immune response such as leukocyte activation (15,16). Conversely, other investigations have shown that ICAM molecules are involved in cancer malignancy because their increased expressions are associated with a poor diagnosis, lower survival rates and metastasis in some cancers including melanoma, breast cancer and leukemia (17)(18)(19)(20)(21)(22)(23)(24).…”

Section: Introductionmentioning

confidence: 99%

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ICAM-3 enhances the migratory and invasive potential of human non-small cell lung cancer cells by inducing MMP-2 and MMP-9 via Akt and CREB

Park

et al. 2009

Int J Oncol

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Abstract.We have previously reported that intercellular adhesion molecule-3 (ICAM-3) is associated with an increase of cellular radio-resistance and cancer cell proliferation. In this study, we hypothesized that ICAM-3 has an additional effect on cancer cell migration and invasion because molecules induced by ICAM-3 are known as regulators of cell migration and invasion. To examine this hypothesis, we used NCI-H1299 non-small cell lung cancer (NSCLC) cell line (p53 and PTEN null cell) and constructed an ICAM-3-over-expressing stable transfectant, which exhibited increased cell migration and invasion. The increased migration and invasion resulted from up-regulation of expression and activities of MMP-2 and MMP-9. ICAM-3 also increased Akt phosphorylation, which caused an increase in cellular migration/invasion and MMP activities. Activity of several transcriptional factors located downstream in the Akt pathway was also tested, and constitutive activation of adenosine 3', 5'-monophosphate response element-binding protein (CREB) by ICAM-3 was detected. Blockage of the Akt pathway attenuated CREB activation, and a decrease in CREB expression reduced cellular migration/invasion and activity of MMPs. This result indicates that CREB functions in the signaling pathway between Akt and MMP. We also showed ICAM-3-induced cell migration and invasion in NCI-H460 NSCLC cells (wild-type p53 and PTEN cell) through the same signaling pathway. Taken together, our findings suggest that ICAM-3 stimulates cancer cell migration/ invasion via ICAM-3/Akt/CREB/MMP pathway regardless of p53 and PTEN status, and this reflects the possibility that ICAM-3 could be considered as a candidate for anti-cancer drug development and as a cancer diagnostic marker.

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Section: Icam-3 Enhances the Migratory And Invasive Potential Of Humamentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

ICAM-3 enhances the migratory and invasive potential of human non-small cell lung cancer cells by inducing MMP-2 and MMP-9 via Akt and CREB

Park

et al. 2009

Int J Oncol

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“…Tumor progression and the development of metastasis appear to be influenced by 2,3,6,7,8,9,12,14). In 3 of the pairs, the differences were statistically significant ( * p<0.05, ** p<0.01).…”

Section: Discussionmentioning

confidence: 85%

“…Interestingly, the impact of ICAM-1 depends on whether the protein is expressed in a membrane-bound or a soluble form (13). Immunohistochemical staining of CRC revealed a lower incidence of lymph node and liver metastases in primary tumors expressing membrane-bound ICAM-1, whereas a lower number of ICAM-1-positive cells are noted in primary tumors that metastasize (14,16,17). Taglia et al (16) showed that membrane-bound ICAM-1 mediates tumor cell attachment to the extracellular matrix.…”

Section: Introductionmentioning

confidence: 99%

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Tumor-associated fibroblasts isolated from colorectal cancer tissues exhibit increased ICAM-1 expression and affinity for monocytes

Schellerer¹,

Langheinrich²,

Hohenberger³

et al. 2013

Oncology Reports

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Abstract. Progression of colorectal cancer (CRC) is strongly associated with inflammation and other desmoplastic reactions in the tumor cell-surrounding tissue. We successfully isolated fibroblasts from the desmoplastic stroma of human CRC specimens and uninvolved colon tissue of patients treated surgically for CRC and investigated potential functional capacities. All of the isolated fibroblasts were vimentin-positive and CK-20/CD45-negative confirming the fibroblast phenotype. Differential expression patterns were detected between tumor-associated fibroblasts (TAFs) and normal tissue-associated fibroblasts (NAFs) regarding intercellular adhesion molecule-1 (ICAM-1) expression. In 11 of 12 TAF cultures, basal ICAM-1 expression was increased as compared to corresponding NAF cultures (p= 0.001). After stimulation of the cultures with interleukin-1β, 8 of the 12 TAF cultures presented higher ICAM-1 levels when compared with the level in the corresponding NAF cultures (p= 0.001). Moreover, the adhesive capacity of these cultures for U937 was increased in 8 out of 10 unstimulated and in 10 out of 10 stimulated cultures when TAFs and NAFs were compared. In corresponding tumor tissue sections from the same patients, the amount of ICAM-1-positive fibroblasts was significantly higher than that in the corresponding normal colon mucosa, indicating a tumor-specific effect that was maintained in the isolated cultures. These results indicate that fibroblasts from CRC tissue exhibit an increased affinity for monocytic cells. This increased intercellular interaction may contribute to elongated residence times of monocytes in CRC tissue. Therefore, these isolated fibroblasts are a useful tool for further functional investigation of desmoplastic tissue reactions in CRC.

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Expression, regulation and function of autotaxin in thyroid carcinomas

Kehlen

Englert

Seifert

et al. 2004

Intl Journal of Cancer

111

102

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Key words: autotaxin; lysophospholipase D; thyroid carcinoma; motilityAutotaxin (ATX) is a 125 kDa glycoprotein that was originally isolated from the conditioned medium of human melanoma A2058 cells. ATX stimulates random and directed motility in a variety of tumor cell lines, including those from prostate and breast carcinomas, melanomas, neuroblastomas and renal-cell carcinoma. [1][2][3][4] Sequence analysis of ATX revealed significant homology to a family of cell surface type I phosphodiesterases, 5 and ATX has recently been newly classified as a member of the ecto-nucleotide pyrophosphate/phosphodiesterase family (E-NPP). Three structurally related mammalian E-NPPs are known, NPP1 (PC-1), NPP2 (ATX, PD-I␣) and NPP3 (gp130 RB 13-6 , PD-I␤, B10). Members of the E-NPP family are capable of hydrolyzing phosphodiester bonds of nucleotides and nucleic acids and pyrophosphate bonds of nucleotides and nucleotide sugars. In addition, they can hydrolyze 3Ј,5Ј-cAMP to AMP, nucleoside 5Ј-triphosphates, such as ATP, to AMP and 2xP i , nucleoside 5Ј-diphosphates, such as ADP, to AMP and P i , or NAD ϩ to AMP and nicotinamide mononucleotide. 6 Recently, ATX (NPP-2) was also shown to hydrolyze lysophosphatidyl choline (LPC) to lysophosphatidic acid (LPA). 7,8 Active phosphodiesterase, lyso-phospholipase D (lyso-PLD) and migration-stimulating activity of ATX depends on the presence of 4 defined amino acid residues, threonine 210 and histidines 316, 360 and 475, within the ATX molecule. 9 When comparing the substrate specificity of ATX with that of the related family members NPP1 and NPP3, only NPP2 displayed a lyso-PLD activity, whereas NPP1 and NPP3 had a much higher nucleotide pyrophosphatase activity. 10

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Expression of intercellular adhesion molecule-1 and prognosis in colorectal cancer

Cited by 68 publications

References 0 publications

ICAM-3 enhances the migratory and invasive potential of human non-small cell lung cancer cells by inducing MMP-2 and MMP-9 via Akt and CREB

ICAM-3 enhances the migratory and invasive potential of human non-small cell lung cancer cells by inducing MMP-2 and MMP-9 via Akt and CREB

Tumor-associated fibroblasts isolated from colorectal cancer tissues exhibit increased ICAM-1 expression and affinity for monocytes

Expression, regulation and function of autotaxin in thyroid carcinomas

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