βig-h3 triggers signaling pathways mediating adhesion and migration of vascular smooth muscle cells through αvβ5 integrin

Lee, Byung Heon; Bae, Jong Sup; Park, Rang Woon; Kim, Jung Eun; Park, Jae Yong; Kim, In San

doi:10.1038/emm.2006.19

Cited by 54 publications

(45 citation statements)

References 31 publications

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“…28 In addition to the upregulation of K Ca 3.1 current and K Ca 3.1 expression by AGEs, the recent studies reported that K Ca 3.1 channels were activated by PI(3)P, which is produced by PI3K from phosphatidylinositol. [29][30][31] Decreasing intracellular level of PI(3)P can reduce K Ca 3.1 channel activity. 32 Besides, recombinant human K Ca 3.1 channels induce HEK293 cell proliferation by a direct interaction with ERK1/2 pathways 33 and downregulating ERK reduces K Ca 3.1 channel expression.…”

Section: Discussionmentioning

confidence: 99%

KCa3.1 channels mediate the increase of cell migration and proliferation by advanced glycation endproducts in cultured rat vascular smooth muscle cells

Zhao

Wang

et al. 2013

Laboratory Investigation

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The mechanisms underlying the involvement of advanced glycation endproducts (AGEs) in diabetic atherosclerosis are not fully understood. The present study was designed to investigate whether intermediate-conductance Ca 2 þ -activated K þ channels (K Ca 3.1 channels) are involved in migration and proliferation induced by AGEs in cultured rat vascular smooth muscle cells (VSMCs) using approaches of whole-cell patch voltage-clamp, cell proliferation and migration assay, and western blot analysis. It was found that the current density and protein level of K Ca 3.1 channels were enhanced in cells incubated with AGE-BSA (bovine serum albumin), and the effects were reversed by co-incubation of AGE-BSA with anti-RAGE (anti-receptors of AGEs) antibody. The ERK1/2 inhibitors PD98059 and U0126, the P38-MAPK inhibitors SB203580 and SB202190, or the PI3K inhibitors LY294002 and wortmannin countered the K Ca 3.1 channel expression by AGE-BSA. In addition, AGE-BAS increased cell migration and proliferation, and the effects were fully reversed with anti-RAGE antibody, the K Ca 3.1 channel blocker TRAM-34, or K Ca 3.1 small interfering RNA. These results demonstrate for the first time that AGEs-induced increase of migration and proliferation is related to the upregulation of K Ca 3.1 channels in rat VMSCs, and the intracellular signals ERK1/2, P38-MAPK and PI3K are involved in the regulation of K Ca 3.1 channel expression.

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Section: Discussionmentioning

confidence: 99%

KCa3.1 channels mediate the increase of cell migration and proliferation by advanced glycation endproducts in cultured rat vascular smooth muscle cells

Zhao

Wang

et al. 2013

Laboratory Investigation

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“…BigH3 has been immunohistochemically found in human tissues such as corneal, skin, lung, bone, bladder, and kidney (26). In addition, BigH3 is involved in certain human diseases such as corneal dystrophies (27,28), melorheostosis, osteogenesis (29), diabetic angiopathy, atherothrombosis and restenosis (30).…”

Section: Introductionmentioning

confidence: 99%

BigH3 protein expression as a marker for breast cancer

Calaf

Echiburú-Chau²,

Zhao³

et al. 2008

Int J Mol Med

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Abstract. The current hypothesis of tumorigenesis in humans suggests that cancer cells acquire their hallmarks of malignancy through the accumulation of advantageous gene activation and inactivation events over long periods of time. For breast cancer development, this multistep process may manifest itself as a sequence of pathologically defined stages. It is widely held that breast cancer originates at the premalignant stage of atypical ductal hyperplasia, progresses to the preinvasive stage of ductal carcinoma in situ, and culminates in the potentially lethal stage of invasive ductal carcinoma. Tumor grade has been a highly valuable prognostic factor for breast cancer, and high-grade ductal carcinoma in situ lesions are associated with poor clinical outcome. The aim of this work was to investigate the BigH3 protein expression changes associated with various stages of breast cancer progression in comparison to benign specimens using tissue microarray technology. Pathological characteristics of breast tissues ranged from benign lesions to breast cancers either of lobular or ductal carcinomas in origin, and included in situ ductal carcinomas, lobular carcinomas, infiltrating ductal carcinomas, carcinomas, scirrhous carcinomas, adenocarcinomas and infiltrating colloid carcinomas. BigH3 protein expression was analyzed by immunohistochemistry in 192 cases of breast tumors. Results indicated a decrease in BigH3 protein expression from benign tissues to in situ ductal carcinoma, lobular carcinoma, infiltrating ductal carcinomas, carcinomas, scirrhous carcinoma, adenocarcinomas to infiltrating colloid carcinomas. We observed that the benign tissue had a 23-fold increase in BigH3 protein expression compared to the infiltrating colloid carcinoma which was the most malignant tissue analyzed. In summary, these studies confirmed the suppressor effect of the BigH3 gene expressed as protein expression in those processes related to the progression of breast tumorigenesis. We conclude that this protein can be used as a marker for breast cancer progression.

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“…The FAS1 domains have been identified in the secretory and membrane proteins of many organisms including mammals, insect, sea urchins, plants, yeast and bacteria . The FAS1 domain mediates cell adhesion and migration via interactions with different integrins (Kim et al, 2000a;Park et al, 2004;Lee et al, 2005;Thapa et al, 2007). Currently, only four FAS1 domain-containing human proteins have been identified (βig-h3, periostin, stabilin-1 and stabilin-2) and investigation of physiological and/or pathological source of fastatin and its regulatory mechanism has been the topic of intense investigation .…”

Section: Introductionmentioning

confidence: 99%

“…Thus, T-CAM represents the fusion protein of cell adhesion domains from two prominent and distinct ECM proteins, βig-h3 and FN. The known-cell adhesion motifs present in fastatin are Glu-Pro-Asp-Ile-Met (EPDIM) and Try-His (YH), and are recognized by α3β1 (Kim et al, 2000a) and αvβ3/αvβ5 integrins (Kim et al, 2002a;Park et al, 2004;Lee et al, 2005;Thapa et al, 2005), respectively. The known-cell adhesion motifs present in the 9 th and the 10 th type III fibronectin domains are Pro-His-Ser-Arg-Asn (PHSRN) and Arg-Gly-Asp (RGD), respectively, and are known to interact with various integrins including α5β1 and αvβ3 (Grant et al, 1997).…”

Section: Introductionmentioning

confidence: 99%

T-CAM, a fastatin-FIII 9-10 fusion protein, potently enhances anti-angiogenic and anti-tumor activity αvβ3 and α5β1 integrins

et al. 2008

Self Cite

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We made fusion protein of fastatin and FIII 9-10, termed tetra-cell adhesion molecule (T-CAM) that can interact simultaneously with α vβ 3 and α 5β 1 integrins, both playing important roles in tumor angiogenesis. T-CAM can serve as a cell adhesion substrate mediating adhesion and migration of endothelial cells in α vβ 3 and α 5β 1 integrin-dependent manner. T-CAM showed pronounced anti-angiogenic activities such as inhibition of endothelial cell tube formation, endothelial cell proliferation, and induction of endothelial cell apoptosis. T-CAM also inhibited angiogenesis and tumor growth in mouse xenograft model. The anti-angiogenic and anti-tumoral activity of molecule like fastatin could be improved by fusing it with integrin-recognizing cell adhesion domain from other distinct proteins. The strategy of combining two distinct anti-angiogenic molecules or cell adhesion domains could facilitate designing improved anticancer agent of therapeutic value.

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βig-h3 triggers signaling pathways mediating adhesion and migration of vascular smooth muscle cells through αvβ5 integrin

Cited by 54 publications

References 31 publications

KCa3.1 channels mediate the increase of cell migration and proliferation by advanced glycation endproducts in cultured rat vascular smooth muscle cells

KCa3.1 channels mediate the increase of cell migration and proliferation by advanced glycation endproducts in cultured rat vascular smooth muscle cells

BigH3 protein expression as a marker for breast cancer

T-CAM, a fastatin-FIII 9-10 fusion protein, potently enhances anti-angiogenic and anti-tumor activity αvβ3 and α5β1 integrins

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