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  • 1
    Online Resource
    Online Resource
    Elevated Coexpression of KITENIN and the ErbB4 CYT-2 Isoform Promotes the Transition from Colon Adenoma to Carcinoma Following APC loss
    American Association for Cancer Research (AACR) ; 2016
    In:  Clinical Cancer Research Vol. 22, No. 5 ( 2016-03-01), p. 1284-1294
    Details
    In: Clinical Cancer Research, American Association for Cancer Research (AACR), Vol. 22, No. 5 ( 2016-03-01), p. 1284-1294
    Abstract: Purpose and Experimental Design: The molecular events in the malignant progression of colon adenoma after loss of adenomatous polyposis coli (APC) are not fully understood. KITENIN (KAI1 C-terminal interacting tetraspanin) increases the invasiveness of colorectal cancer cells, and we identified a novel EGFR-independent oncogenic signal of EGF that works under coexpressed KITENIN and ErbB4. Here we tested whether elevated KITENIN and ErbB4 contribute to further progression of intestinal adenoma following APC loss. Results: The intestinal tissues of villin-KITENIN transgenic mice in which villin-driven KITENIN expression induces increased c-Jun expression exhibit mild epithelial cell proliferation but no epithelial lineage changes compared with those of nontransgenic mice. Among the four ErbB4 isoforms, JM-a/CYT-2 and JM-b/CYT-2 exhibited the highest AP-1 activity when cells coexpressing KITENIN and each isoform were stimulated by EGF. Interestingly, predominant overexpression of the ErB4-CYT-2 mRNA as well as increased EGFR expression were observed in intestinal adenoma of APCmin/+ mice, which makes the microenvironment of activated EGF signaling. When we crossed villin-KITENIN mice with APCmin/+ mice, intestinal tumor tissues in the crossed mice showed the characteristics of early-stage invading adenocarcinoma. In patients with colorectal cancer, ErbB4-CYT-2 mRNA expression was significantly greater in tumor tissues than in normal adjacent tissues, but no significant differences in tumor tissue expression were found between different colorectal cancer stages. Furthermore, the mRNA expression of KITENIN and that of ErbB4-CYT-2 were positively correlated in human colorectal cancer tissue. Conclusions: Elevated coexpression of KITENIN and ErbB4-CYT-2 promotes the transition of colon adenoma to adenocarcinoma within an APC loss–associated tumor microenvironment. Clin Cancer Res; 22(5); 1284–94. ©2015 AACR.
    Type of Medium: Online Resource
    ISSN: 1078-0432 , 1557-3265
    URL: Article
    DOI: 10.1158/1078-0432.CCR-15-0306
    RVK:
    XA 36791
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2016
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  • 2
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    KAI1 COOH‐terminal interacting tetraspanin (KITENIN) expression in early and advanced laryngeal cancer
    Wiley ; 2010
    In:  The Laryngoscope Vol. 120, No. 5 ( 2010-05), p. 953-958
    Details
    In: The Laryngoscope, Wiley, Vol. 120, No. 5 ( 2010-05), p. 953-958
    Abstract: To investigate the expression of KAI1 COOH‐terminal interacting tetraspanin (KITENIN) in patients with laryngeal cancers and to examine the correlation between its expression and various clinical and pathological variables. Study Design: Cross‐sectional study with planned data collection. Methods: Tumor specimens were collected from 32 patients with laryngeal squamous carcinoma (collection of consecutive 32 tumor samples; 14 early stage, 18 advanced stage). Expression of KITENIN in the tissues obtained was determined by Western blot analysis and immunohistochemical staining. The patient characteristics including age, gender, tumor location, histology, stage, tumor extent, lymph node metastasis, and survival were obtained by review of the hospital records. Results: KITENIN expression was significantly increased in laryngeal cancer tissues compared to adjacent normal tissue mucosa, as well as in metastatic lymph nodes compared to nonmetastatic lymph nodes. High KITENIN expression was significantly associated with advanced stage, tumor extent, and lymph node metastasis ( P = .016, .016, and .005, respectively). There was no difference in the overall survival and disease‐free survival between the low‐ and high‐KITENIN expression groups among patients with laryngeal cancer. Conclusions: These results suggest that KITENIN expression may be associated with tumor progression in patients with laryngeal cancer. Further studies are needed to determine whether KITENIN expression adds prognostic value to conventional factors, such as the stage and status of metastasis, in a large series with a long period of follow‐up. Laryngoscope, 2010
    Type of Medium: Online Resource
    ISSN: 0023-852X , 1531-4995
    URL: Issue
    URL: Article
    DOI: 10.1002/lary.v120:5
    DOI: 10.1002/lary.20864
    Language: English
    Publisher: Wiley
    Publication Date: 2010
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  • 3
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    KITENIN increases invasion and migration of mouse squamous cancer cells and promotes pulmonary metastasis in a mouse squamous tumor model
    Wiley ; 2009
    In:  FEBS Letters Vol. 583, No. 4 ( 2009-02-18), p. 711-717
    Details
    In: FEBS Letters, Wiley, Vol. 583, No. 4 ( 2009-02-18), p. 711-717
    Type of Medium: Online Resource
    ISSN: 0014-5793
    URL: Article
    DOI: 10.1016/j.febslet.2009.01.014
    RVK:
    WA 15000
    Language: English
    Publisher: Wiley
    Publication Date: 2009
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    SSG: 12
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  • 4
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    Solar‐Powered Whole‐Cell P450 Catalytic Platform for C‐Hydroxylation Reactions
    Wiley ; 2021
    In:  ChemSusChem Vol. 14, No. 15 ( 2021-08-09), p. 3054-3058
    Details
    In: ChemSusChem, Wiley, Vol. 14, No. 15 ( 2021-08-09), p. 3054-3058
    Abstract: Photobiocatalysis is a green platform for driving redox enzymatic reactions using solar energy, not needing high‐cost cofactors and redox partners. Here, a visible light‐driven whole‐cell platform for human cytochrome P450 (CYP) photobiocatalysis was developed using natural flavins as a photosensitizer. Photoexcited flavins mediate NADPH/reductase‐free, light‐driven biocatalysis by human CYP2E1 both in vitro and in the whole‐cell systems. In vitro tests demonstrated that the photobiocatalytic activity of CYP2E1 is dependent on the substrate type, the presence of catalase, and the acid type used as a sacificial electron donor. A protective effect of catalase was found against the inactivation of CYP2E1 heme by H 2 O 2 and the direct transfer of photo‐induced electrons to the heme iron not by peroxide shunt. Furthermore, the P450 photobiocatalysis in whole cells containing human CYPs 1A1, 1A2, 1B1, and 3A4 demonstrated the general applicability of the solar‐powered, flavin‐mediated P450 photobiocatalytic system.
    Type of Medium: Online Resource
    ISSN: 1864-5631 , 1864-564X
    URL: Issue
    URL: Article
    DOI: 10.1002/cssc.v14.15
    DOI: 10.1002/cssc.202100944
    Language: English
    Publisher: Wiley
    Publication Date: 2021
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  • 5
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    Abstract 3530: KITENIN works as a fine regulator of ErbB4 expression in colorectal cancer tissues in addition to E3-ubiquitin ligase Nrdp1
    American Association for Cancer Research (AACR) ; 2017
    In:  Cancer Research Vol. 77, No. 13_Supplement ( 2017-07-01), p. 3530-3530
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 77, No. 13_Supplement ( 2017-07-01), p. 3530-3530
    Abstract: Purpose: Understanding the complex biological functions of E3-ubiquitin ligases may facilitate the modulation of E3-ubiquitin ligases as a promising approach for the development of novel anticancer drugs. We recently identified that the KITENIN/ErbB4-Dvl2-c-Jun axis works as a novel unconventional downstream signal of epidermal growth factor in colorectal cancer (CRC) tissues and that the immunohistochemical expression of KITENIN/ErbB4 was highly expressed in tumor tissues from advanced CRC stage. However, the detailed mechanisms that explain the higher levels of ErbB4 in colon cancer tissues are largely unknown. Here we investigated whether E3-ubiquitin ligases participate in the operation of the KITENIN/ErbB4-Dvl2-c-Jun axis and in the maintenance of elevated KITENIN/ErbB4 complex in CRC. Results & Discussion: We found that Nrdp1, an E3-ligase for ErbB3/ErbB4, interacted with KITENIN (KAI1 C-terminal interacting tetraspanin) to form a functional KITENIN/ErbB4/Nrdp1 complex and is responsible for down-regulating Dvl2 within this complex. Interestingly, ErbB4 was resistant to degradation by Nrdp1 in KITENIN/Nrdp1-co-transfected CRC cells, and KITENIN bound to the C-terminal coiled-coil domain of Nrdp1. Chemical blockade of ErbB kinase did not block the action of EGF to increase in total/phospho-ErbB4 and phospho-ERK in KITENIN/ErbB4-cotransfected cells, whereas it blocked the action of EGF in ErbB4 alone-transfected CRC cells. In human CRC tissues, higher expressions of ErbB4 and KITENIN and lower expression of Dvl2 was observed in stage IV samples than in stage I, but a low level of Nrdp1 was expressed in both stages and it did not differ significantly by stage. These results indicated that Nrdp1 is necessary for the reduction in Dvl2 to generate c-Jun in the EGF-KITENIN/ErbB4-c-Jun axis, but more importantly, elevated KITENIN protects KITENIN-bound ErbB4 from Nrdp1-mediated degradation via physical collaboration between the KITENIN/ErbB4 complex and Nrdp1, but not via modulation of ErbB kinase activity. Thus, KITENIN functions in the maintenance of a higher expression level of ErbB4 in advanced CRC tissues, independent of ubiquitin-mediated degradation via Nrdp1. Conclusion: Our present findings add a new component to our understanding of the molecular events underlying the regulation of ErbB4 expression level in CRC tissues: KITENIN is also a fine regulator of ErbB4 expression in addition to E3-ubiquitin ligase Nrdp1. Citation Format: Jeong A Bae, Eun Gene Sun, Yoo-Seung Ko, Hui Jeong Choi, Chaeyong Jung, Kyung-Hwa Lee, Ik Joo Chung, Kyung-Sub Moon, Young Hyun Yu, Hyung-Ho Ha, Hangun Kim, Kyung Keun Kim. KITENIN works as a fine regulator of ErbB4 expression in colorectal cancer tissues in addition to E3-ubiquitin ligase Nrdp1 [abstract]. In: Proceedings of the American Association for Cancer Research Annual Meeting 2017; 2017 Apr 1-5; Washington, DC. Philadelphia (PA): AACR; Cancer Res 2017;77(13 Suppl):Abstract nr 3530. doi:10.1158/1538-7445.AM2017-3530
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2017-3530
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2017
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  • 6
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    Abstract 2733: KITENIN and ErbB4 contribute to further malignant changes in colorectal cancer through c-Jun/AP-1 activation
    American Association for Cancer Research (AACR) ; 2011
    In:  Cancer Research Vol. 71, No. 8_Supplement ( 2011-04-15), p. 2733-2733
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 71, No. 8_Supplement ( 2011-04-15), p. 2733-2733
    Abstract: KITENIN (KAI1 C-terminal interacting tetraspanin, Vangl1) is not only a major component of PCP pathway but also a functional protein promoting colorectal cancer (CRC) cell motility and invasiveness. Here, we report the mechanism of which KITENIN leads further malignant changes in CRC progression after loss of tumor suppressor Adenomatous polyposis coli (APC). KITENIN increases the level of AP-1 activity through interaction with Dvl2, which is subsequently being degraded. Decreasing Dvl2 via interaction with KITENIN or via treatment of si-RNA to Dvl2 significantly increases the AP-1 activity through elevating the level of c-jun and c-jun phosphorylation. EGF acts upstream of KITENIN/AP-1 signaling and induces synergic AP-1 activation in the presence of elevated KITENIN, which requires the interaction of KITENIN with ErbB4. The morphological characteristics of adenocarcinoma were observed in intestinal tumor tissues from compound villin-KITENIN transgenic/APCmin/+ mice but not from APCmin/+ mice, both of which express the elevated level of ErbB4. This result demonstrates that further malignant phenotype of intestinal tumor can be induced by elevated KITENIN and ErbB4 via promoting c-Jun/AP-1 activation within an APC loss-associated tumor microenvironment. Our present results suggest the possibility of the addition of anti-KITENIN therapy to the use of EGFR inhibitors in the treatment of CRC patients with APC mutation. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 102nd Annual Meeting of the American Association for Cancer Research; 2011 Apr 2-6; Orlando, FL. Philadelphia (PA): AACR; Cancer Res 2011;71(8 Suppl):Abstract nr 2733. doi:10.1158/1538-7445.AM2011-2733
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2011-2733
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2011
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  • 7
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    Abstract 4006: Biochemical characteristics of functional domain of KITENIN: Its implication in AP-1 signal activation and colorectal cancer cell motility
    American Association for Cancer Research (AACR) ; 2012
    In:  Cancer Research Vol. 72, No. 8_Supplement ( 2012-04-15), p. 4006-4006
    Details
    In: Cancer Research, American Association for Cancer Research (AACR), Vol. 72, No. 8_Supplement ( 2012-04-15), p. 4006-4006
    Abstract: Background & aims: KITENIN (KAI1 C-terminal interacting tetraspanin) is not only a membrane-associated protein but also a functional protein promoting the invasiveness of colorectal cancer (CRC) cells. Recent studies about the mechanism of KITENIN function in the CRC cells indicate that KITENIN plays a pivotal role in tumor initiation and promotion through activating the activator protein-1 (AP-1) signaling. However, the contribution of each functional domain of KITENIN to AP-1 signaling is still unknown and the biochemical properties of C-terminal region of KITENIN were investigated. Methods: To compare the biochemical and functional properties of KITENIN deletion mutants with wild-type KITENIN, the various mutant constructs of C-terminal region (238-512 aa) were generated and being expressed in the 293T and Caco2 cells. AP-1 activity was measured via AP-1 luciferase reporter assays, and the cellular phenotypes of these cells expressing KITENIN mutants were examined via in vitro cell invasion and wound-healing assays. Results: KITENIN mutant with deletion of C-terminal 63 amino acids (DCKIT) markedly increased the AP-1 activity in contrast to other deletion mutants and wild-type KITENIN. Also, DCKIT increased the degradation of Dvl2 and stability of c-Jun, which are responsible for AP-1 activation by KITENIN. The C-terminal fragment of KITENIN (KICD, roughly 30 kDa) was generated and preferentially translocated to the nucleus after PMA treatment, but its functional significance is under investigation. A mutant construct of 408ALRA411-KITENIN was obtained by mutation of YXXΨ motifs, which directs the clathrin-dependent endocytosis of membrane-spanning proteins. This mutation did not influence the AP-1 activity, cell invasiveness, and cell migration by KITENIN but disrupted the interaction of KITENIN with Dvl2. Moreover, co-expression of this mutant with ErbB4 exhibited more attenuated AP-1 activity than that of forced expression of wild-type KITENIN and ErbB4. These results indicate that endocytosis of KITENIN and subsequent interaction with Dvl2 is essential to activating AP-1 signal and modulating cell motility by KITENIN. Conclusion: These biochemical properties of deletion mutants of KITENIN suggest that the C-terminal region of KITENIN is an important component for modulating AP-1 signal and CRC cell motility by KITENIN. Citation Format: {Authors}. {Abstract title} [abstract]. In: Proceedings of the 103rd Annual Meeting of the American Association for Cancer Research; 2012 Mar 31-Apr 4; Chicago, IL. Philadelphia (PA): AACR; Cancer Res 2012;72(8 Suppl):Abstract nr 4006. doi:1538-7445.AM2012-4006
    Type of Medium: Online Resource
    ISSN: 0008-5472 , 1538-7445
    URL: Article
    DOI: 10.1158/1538-7445.AM2012-4006
    RVK:
    XA 36000
    RVK:
    XA 10000
    Language: English
    Publisher: American Association for Cancer Research (AACR)
    Publication Date: 2012
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  • 8
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    TAp73 inhibits cell invasion and migration by directly activating KAI1 expression in colorectal carcinoma
    Elsevier BV ; 2018
    In:  Cancer Letters Vol. 415 ( 2018-02), p. 106-116
    Details
    In: Cancer Letters, Elsevier BV, Vol. 415 ( 2018-02), p. 106-116
    Type of Medium: Online Resource
    ISSN: 0304-3835
    URL: Article
    DOI: 10.1016/j.canlet.2017.12.002
    Language: English
    Publisher: Elsevier BV
    Publication Date: 2018
    detail.hit.zdb_id: 195674-7
    detail.hit.zdb_id: 2004212-7
    SSG: 12
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  • 9
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    Lgals3bp suppresses colon inflammation and tumorigenesis through the downregulation of TAK1-NF-κB signaling
    Springer Science and Business Media LLC ; 2021
    In:  Cell Death Discovery Vol. 7, No. 1 ( 2021-04-06)
    Details
    In: Cell Death Discovery, Springer Science and Business Media LLC, Vol. 7, No. 1 ( 2021-04-06)
    Abstract: Galectin 3-binding protein (LGALS3BP, also known as 90K) is a multifunctional glycoprotein involved in immunity and cancer. However, its precise role in colon inflammation and tumorigenesis remains unclear. Here, we showed that Lgals3bp −/− mice were highly susceptible to colitis and colon tumorigenesis, accompanied by the induction of inflammatory responses. In acute colitis, NF-κB was highly activated in the colon of Lgals3bp −/− mice, leading to the excessive production of pro-inflammatory cytokines, such as IL-6, TNFα, and IL-1β. Mechanistically, Lgals3bp suppressed NF-κB through the downregulation of TAK1 in colon epithelial cells. There was no significant difference in the pro-inflammatory cytokine levels between wild-type and Lgals3bp −/− mice in a chronic inflammatory state, during colon tumorigenesis. Instead, Lgals3bp −/− mice showed elevated levels of GM-CSF, compared to those in WT mice. We also found that GM-CSF promoted the accumulation of myeloid-derived suppressor cells and ultimately increased colon tumorigenesis in Lgals3bp −/− mice. Taken together, Lgals3bp plays a critical role in the suppression of colitis and colon tumorigenesis through the downregulation of the TAK1-NF-κB-cytokine axis. These findings suggest that LGALS3BP is a novel immunotherapeutic target for colon inflammation and tumorigenesis.
    Type of Medium: Online Resource
    ISSN: 2058-7716
    URL: Article
    DOI: 10.1038/s41420-021-00447-7
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2021
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  • 10
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    Suppression of triple-negative breast cancer aggressiveness by LGALS3BP via inhibition of the TNF-α–TAK1–MMP9 axis
    Springer Science and Business Media LLC ; 2023
    In:  Cell Death Discovery Vol. 9, No. 1 ( 2023-04-11)
    Details
    In: Cell Death Discovery, Springer Science and Business Media LLC, Vol. 9, No. 1 ( 2023-04-11)
    Abstract: Transforming growth factor-β-activated kinase 1 (TAK1), which is highly expressed and aberrantly activated in triple-negative breast cancer (TNBC), plays a pivotal role in metastasis and progression. This makes it a potential therapeutic target for TNBC. Previously, we reported lectin galactoside-binding soluble 3 binding protein (LGALS3BP) as a negative regulator of TAK1 signaling in the inflammatory response and inflammation-associated cancer progression. However, the role of LGALS3BP and its molecular interaction with TAK1 in TNBC remain unclear. This study aimed to investigate the function and underlying mechanism of action of LGALS3BP in TNBC progression and determine the therapeutic potential of nanoparticle-mediated delivery of LGALS3BP in TNBC. We found that LGALS3BP overexpression suppressed the overall aggressive phenotype of TNBC cells in vitro and in vivo. LGALS3BP inhibited TNF-α-mediated gene expression of matrix metalloproteinase 9 ( MMP9 ), which encodes a protein crucial for lung metastasis in TNBC patients. Mechanistically, LGALS3BP suppressed TNF-α-mediated activation of TAK1, a key kinase linking TNF-α stimulation and MMP9 expression in TNBC. Nanoparticle-mediated delivery enabled tumor-specific targeting and inhibited TAK1 phosphorylation and MMP9 expression in tumor tissues, suppressing primary tumor growth and lung metastasis in vivo. Our findings reveal a novel role of LGALS3BP in TNBC progression and demonstrate the therapeutic potential of nanoparticle-mediated delivery of LGALS3BP in TNBC.
    Type of Medium: Online Resource
    ISSN: 2058-7716
    URL: Article
    DOI: 10.1038/s41420-023-01419-9
    Language: English
    Publisher: Springer Science and Business Media LLC
    Publication Date: 2023
    detail.hit.zdb_id: 2842546-7
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