Search results for: Mouse Anti-Human Tenascin Antibodies
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2014/08/08
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Tumor-α9β1 integrin-mediated signaling induces breast cancer growth and lymphatic metastasis via the recruitment of cancer-associated fibroblasts.
Tumor-derived matricellular proteins such as osteopontin (OPN) and tenascin-C (TN-C) have been implicated in tumor growth and metastasis. However, the molecular basis of how these proteins contribute to tumor progression remains to be elucidated. Importantly, these matricellular proteins are known to interact with α9β1 integrin. Therefore, we hypothesized that tumor-derived α9β1 integrin may contribute to tumor progression. To clarify the roles of α9β1 integrin in tumor growth and lymphatic metastasis, we used an inhibitory anti-human α9β1 integrin antibody (anti-hα9β1 antibody) and a α9β1 integrin-positive human breast cancer cell line, MDA-MB-231 luc-D3H2LN (D3H2LN), in vitro functional assays, and an in vivo orthotopic xenotransplantation model. In this study, we demonstrated that tumor, but not host α9β1 integrin, contributes to tumor growth, lymphatic metastasis, recruitment of cancer-associated fibroblasts (CAFs), and host-derived OPN production. We also found that CAFs contributed to tumor growth, lymphatic metastasis, and host-derived OPN levels. Consistent with those findings, tumor volume was well-correlated with numbers of CAFs and levels of host-derived OPN. Furthermore, it was shown that the inoculation of D3H2LN cells into mammary fat pads with mouse embryonic fibroblasts (MEFs), obtained from wild type, but not OPN knock-out mice, resulted in enhancement of tumor growth, thus indicating that CAF-derived OPN enhanced tumor growth. These results suggested that tumor α9β1-mediated signaling plays a pivotal role in generating unique primary tumor tissue microenvironments, which favor lymphatic metastasis and tumor growth.Daichi Ota, Masashi Kanayama, Yutaka Matsui, Koyu Ito, Naoyoshi Maeda, Goro Kutomi, Koichi Hirata, Toshihiko Torigoe, Noriyuki Sato, Akinori Takaoka, Ann F Chambers, Junko Morimoto, Toshimitsu Uede
1885 related Products with: Tumor-α9β1 integrin-mediated signaling induces breast cancer growth and lymphatic metastasis via the recruitment of cancer-associated fibroblasts.
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#21208610 2011/01/03
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Immunohistochemical expression of Tenascin in embryogenesis, tumorigenesis and inflammatory oral mucosa.
Tenascin is a large extracellular matrix glycoprotein that plays specific role in cell matrix interaction. This protein is mainly attracted because of its oncofetal predominance expression at epithelial-mesenchymal interaction and also been associated with inflammatory response. Thus the aim was to study the expression of Tenascin within the oral cavity in a developing tooth, normal oral mucosa, squamous cell carcinoma and inflammatory mucosa and further to compare its expression in inflammatory mucosa with that of squamous cell carcinoma.Deepa R Mane, Alka D Kale, Veena V Naik
2350 related Products with: Immunohistochemical expression of Tenascin in embryogenesis, tumorigenesis and inflammatory oral mucosa.
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Tenascin expression in intraepithelial neoplasia and invasive carcinoma of the uterine cervix.
To determine whether the expression of the matrix protein tenascin (TN) is of diagnostic or prognostic value in cervical intraepithelial neoplasia (CIN).B F Iskaros, L G Koss
1712 related Products with: Tenascin expression in intraepithelial neoplasia and invasive carcinoma of the uterine cervix.
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Epimorphin expression during human foetal hair follicle development.
Epimorphin is a mesenchymal protein expressed in several organs and known to have an essential role in epithelial tissue organization, including hair follicle morphogenesis, in mice. Although about 90% homology has been reported between human and mouse epimorphin exon sequences, there is no information about expression and function of epimorphin in hair follicle development in humans. In order to elucidate the expression pattern of epimorphin in human hair follicle morphogenesis and to compare it with the distribution of tenascin and neural cell adhesion molecule (NCAM), skin samples from human foetuses of a series of estimated gestational ages (EGAs) (46-168 days EGA) were studied using monoclonal anti-epimorphin antibody MC-1, anti-tenascin antibody and anti-human NCAM antibody. Epimorphin was detected in the mesenchymal cell condensation at the pregerm stage (< 75 days EGA), and there was strong expression of epimorphin in the perifollicular mesenchymal cells around the hair germ (75-84 days EGA). At the hair peg stage (85-104 days EGA), epimorphin was around the hair peg with the strongest staining in the neck portion. This sequence of staining patterns was similar to that of tenascin. In the bulbous hair peg (105-134 days EGA), the perifollicular dermal mesenchymal cells were evenly positive for epimorphin. Mesenchymal cells underneath the follicle bulb prior to formation of the dermal papilla were also positive for epimorphin. In the lanugo hair follicle (> 134 days EGA), dermal papilla cells expressed epimorphin as well as tenascin and NCAM. These results indicate that epimorphin expression is closely linked to developing hair follicles in human foetuses. This suggests that epimorphin may have an important part in induction of morphogenesis during human foetal hair follicle development.M Akiyama, M Amagai, L T Smith, K Hashimoto, H Shimizu, T Nishikawa
2507 related Products with: Epimorphin expression during human foetal hair follicle development.
1 kit(96 Wells)2x 100ug1 mg300 units 100ul5 mLOne 96-Well Strip Micropl500 100μl1mg100.00 ug1.00 flask
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Similarities of an autoantigen in aneurysmal disease of the human abdominal aorta to a 36-kDa microfibril-associated bovine aortic glycoprotein.
Immunoglobulin G (IgG) from human aneurysmal aorta was used to partially purify an aortic protein with an apparent MW approximately 80 kDa. Amino acid sequencing of a tryptic digest revealed two sequences with homology to mouse tenascin-X. The autoimmune IgG was then shown to react with purified human tenascin, and a rabbit polyclonal anti-human tenascin antibody was found to react with the purified autoantigen. These observations suggest that the autoantigen of abdominal aortic aneurysm disease may be homologous to a calcium-binding member of the tenascin superfamily that has been identified by others in pig and cow.M D Tilson