The Experts below are selected from a list of 669 Experts worldwide ranked by ideXlab platform
Byong Chul Yoo - One of the best experts on this subject based on the ideXlab platform.
-
Identification of <B>CalgranulinB> B interacting proteins and network analysis in gastrointestinal cancer cells.
PloS one, 2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:<B>CalgranulinB> B is known to Be involved in tumor development, But the underlying molecular mechanism is not clear. To gain insight into possiBle roles of <B>CalgranulinB> B, we screened for <B>CalgranulinB> B-interacting molecules in the SNU-484 gastric cancer and the SNU-81 colon cancer cells. <B>CalgranulinB> B-interacting partners were identified By yeast two-hyBrid and functional information was oBtained By computational analysis. Most of the <B>CalgranulinB> B-interacting partners were involved in metaBolic and cellular processes, and found to have molecular function of Binding and catalytic activities. Interestingly, 46 molecules in the network of the <B>CalgranulinB> B-interacting proteins are known to Be associated with cancer and FKBP2 was found to interact with <B>CalgranulinB> B in Both SNU-484 and SNU-81 cells. PolyuBiquitin-C encoded By UBC, which exhiBited an interaction with <B>CalgranulinB> B, has Been associated with various molecules of the extracellular space and plasma memBrane identified in our screening, including Na-K-Cl cotransporter 1 and dystonin in SNU-484 cells, and ATPase suBunit Beta-1 in SNU-81 cells. Our data provide novel insight into the roles of <B>CalgranulinB> B of gastrointestinal cancer cells, and offer new clues suggesting <B>CalgranulinB> B acts as an effector molecule through which the cell can communicate with the tumor microenvironment via polyuBiquitin-C.
-
Network analysis and cancer associations of the <B>CalgranulinB> B-interacting molecules.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:In the generated network, molecular interactions are shown By grey lines, the identified <B>CalgranulinB> B-interacting molecules are highlighted in purple, and molecules that have Been associated with cancer are indicated By dotted Blue lines.
-
Communication of <B>CalgranulinB> B with extracellular environment via polyuBiquitin-C(UBC) in SNU-484, SNU-81, and HEK293 cells.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:Direct interactions with <B>CalgranulinB> B (S100A9) were predicted using STRING analysis, and are indicated By different colored lines: green, red, Blue, Black, purple, light Blue, yellow, sky Blue Based on the types of evidence for associations.
-
List of identified significant genes interacting with <B>CalgranulinB> B.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:List of identified significant genes interacting with <B>CalgranulinB> B.
-
Cellular components associated with the <B>CalgranulinB> B-interacting molecules.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:The <B>CalgranulinB> B-interacting molecules identified in SNU-484 (A), SNU-81 (B), and HEK293 (C) cells were categorized according to cellular component information.
Santanu Bose - One of the best experts on this subject based on the ideXlab platform.
-
DAMP Molecule S100A9 Acts as a Molecular Pattern to Enhance Inflammation during Influenza A Virus Infection: Role of DDX21-TRIF-TLR4-MyD88 Pathway
2016Co-Authors: Su Yu Tsai, Jesus A Segovia, Te Hung Chang, Ian R Morris, Michael T Berton, Melanie R Tardif, Annabelle Cesaro, Santanu BoseAbstract:Pathogen-associated molecular patterns (PAMPs) trigger host immune response By activating pattern recognition receptors like toll-like receptors (TLRs). However, the mechanism whereBy several pathogens, including viruses, activate TLRs via a non-PAMP mechanism is unclear. Endogenous ‘‘inflammatory mediators’ ’ called damage-associated molecular patterns (DAMPs) have Been implicated in regulating immune response and inflammation. However, the role of DAMPs in inflammation/immunity during virus infection has not Been studied. We have identified a DAMP molecule, S100A9 (also known as <B>CalgranulinB> B or MRP-14), as an endogenous non-PAMP activator of TLR signaling during influenza A virus (IAV) infection. S100A9 was released from undamaged IAV-infected cells and extracellular S100A9 acted as a critical host-derived molecular pattern to regulate inflammatory response outcome and disease during infection By exaggerating pro-inflammatory response, cell-death and virus pathogenesis. Genetic studies showed that the DDX21-TRIF signaling pathway is required for S100A9 gene expression/production during infection. Furthermore, the inflammatory activity of extracellular S100A9 was mediated By activation of the TLR4-MyD88 pathway. Our studies have thus, underscored the role of a DAMP molecule (i.e. extracellular S100A9) in regulating virus-associated inflammation and uncovered a previously unknow
-
damp molecule s100a9 acts as a molecular pattern to enhance inflammation during influenza a virus infection role of ddx21 trif tlr4 myd88 pathway
PLOS Pathogens, 2014Co-Authors: Su Yu Tsai, Philippe A Tessier, Jesus A Segovia, Te Hung Chang, Ian R Morris, Michael T Berton, Melanie R Tardif, Annabelle Cesaro, Santanu BoseAbstract:Pathogen-associated molecular patterns (PAMPs) trigger host immune response By activating pattern recognition receptors like toll-like receptors (TLRs). However, the mechanism whereBy several pathogens, including viruses, activate TLRs via a non-PAMP mechanism is unclear. Endogenous “inflammatory mediators” called damage-associated molecular patterns (DAMPs) have Been implicated in regulating immune response and inflammation. However, the role of DAMPs in inflammation/immunity during virus infection has not Been studied. We have identified a DAMP molecule, S100A9 (also known as <B>CalgranulinB> B or MRP-14), as an endogenous non-PAMP activator of TLR signaling during influenza A virus (IAV) infection. S100A9 was released from undamaged IAV-infected cells and extracellular S100A9 acted as a critical host-derived molecular pattern to regulate inflammatory response outcome and disease during infection By exaggerating pro-inflammatory response, cell-death and virus pathogenesis. Genetic studies showed that the DDX21-TRIF signaling pathway is required for S100A9 gene expression/production during infection. Furthermore, the inflammatory activity of extracellular S100A9 was mediated By activation of the TLR4-MyD88 pathway. Our studies have thus, underscored the role of a DAMP molecule (i.e. extracellular S100A9) in regulating virus-associated inflammation and uncovered a previously unknown function of the DDX21-TRIF-S100A9-TLR4-MyD88 signaling network in regulating inflammation during infection.
Xueqiong Zhu - One of the best experts on this subject based on the ideXlab platform.
-
The role of <B>CalgranulinB> B gene on the Biological Behavior of squamous cervical cancer in vitro and in vivo.
Cancer management and research, 2018Co-Authors: Wenwen Zhang, Miaomiao Chen, Huihui Cheng, Qi Shen, Ying Wang, Xueqiong ZhuAbstract:OBjective The oBjective of the study was to explore the role of <B>CalgranulinB> B gene on the Biological Behavior of squamous cervical cancer. Methods Differential transcription in <B>CalgranulinB> B gene Between human papillomavirus (HPV)-positive and negative cervical cancer groups was identified, and the relationship Between <B>CalgranulinB> B gene and matrix metalloproteinase (MMP) genes were explored using The Cancer Genome Atlas dataBase. SuBsequently, the role of <B>CalgranulinB> B on the cell proliferation, apoptosis, invasion and migration was investigated, through overexpression and/or underexpression of <B>CalgranulinB> B in cervical cancer cells. In addition, the effect of <B>CalgranulinB> B on the growth of the cervical cancer was studied via constructing xenograft model in BALB/c nude mice that either overexpressed or underexpressed <B>CalgranulinB> B. Results <B>CalgranulinB> B gene transcription in cervical cancer was highly correlated with the high-risk HPV-16 and HPV-45. In addition, overexpression of <B>CalgranulinB> B increased cell proliferation, invasion and migration, whereas it did not significantly affect cell apoptosis. This effect was also confirmed By <B>CalgranulinB> B knockdown assay. Additionally, we found that the transcription of <B>CalgranulinB> B gene was negatively correlated with MMP15 and MMP24 genes, But positively associated with MMP25 genes in cervical cancer. Furthermore, <B>CalgranulinB> B significantly promoted the growth of cervical cancer in vivo. Conclusion <B>CalgranulinB> B promotes cell proliferation, migration and invasion of squamous cervical cancer, possiBly via regulation of MMPs. Whether there are synergistic actions Between <B>CalgranulinB> B and HPV-16/HPV-45 infection on the squamous cervical carcinogenesis or progression need further study.
Charlotta Enerbäck - One of the best experts on this subject based on the ideXlab platform.
-
Loss of ICAM-1 signaling induces psoriasin (S100A7) and MUC1 in mammary epithelial cells
Breast Cancer Research and Treatment, 2011Co-Authors: S. Petersson, Maria Yhr, E. Shubbar, A. Kovacs, Charlotta EnerbäckAbstract:Psoriasin (S100A7), a memBer of the S100 gene family, is highly expressed in high-grade comedo ductal carcinoma in situ (DCIS), with a higher risk of local recurrence. Psoriasin is, therefore, a potential Biomarker for DCIS with a poor prognosis. High-grade DCIS is characterized By a high proliferation rate and crowded cells, consequently, lose contact with the extracellular matrix. The aim of this study was, therefore, to elucidate the involvement of adhesion signals in the regulation of psoriasin. Protein expression was evaluated By Western Blotting, flow cytometry, and immunohistochemistry, and using Breast carcinoma SAGE dataBases availaBle from the CGAP weBsite. Intercellular adhesion molecule 1 (ICAM-1) was down-regulated in MCF10A cells using short hairpin RNA. We found a significant negative correlation Between the expression of ICAM-1 and psoriasin, and a positive correlation Between psoriasin and MUC1 in normal and DCIS SAGE liBraries. In a cluster analysis of 34 adhesion molecules and 20 S100 proteins, we showed that SAGE liBraries expressing the S100 proteins—psoriasin, <B>CalgranulinB>-A, and <B>CalgranulinB>-B—clustered together. Interestingly, the expression of all the three proteins correlated strongly to the oncogenic MUC1. We confirmed the negative correlation Between ICAM-1 and psoriasin/MUC1, when normal and Breast cancer cells were cultured in suspension and on collagen, respectively. The down-regulation of ICAM-1 By short hairpin RNA in MCF10A cells led to the induction of psoriasin, <B>CalgranulinB>-A, <B>CalgranulinB>-B, and MUC1, and we demonstrated that these up-regulations were not ROS dependent. By Blocking the phospholipase C (PLC)-IP3 pathway in these cells, we showed that the induction of psoriasin diminished. The results suggest that psoriasin is an intracellular calcium-dependent target of the PLC pathway. Our findings suggest that the down-regulation of ICAM-1 in mammary epithelial cells may contriBute Both to the high expression of psoriasin seen in some high-grade DCIS tumors and to the induction of MUC1.
-
S100A7 (Psoriasin), highly expressed in Ductal Carcinoma (DCIS), is regulated By IFN-gamma in mammary epithelial cells-0
2011Co-Authors: Stina Petersson, Anna Bylander, Maria Yhr, Charlotta EnerbäckAbstract:Copyright information:Taken from "S100A7 (Psoriasin), highly expressed in Ductal Carcinoma (DCIS), is regulated By IFN-gamma in mammary epithelial cells"http://www.Biomedcentral.com/1471-2407/7/205BMC Cancer 2007;7():205-205.PuBlished online 6 Nov 2007PMCID:PMC2180183.00 u or 1000 u of IFN-gamma. IFN-gamma treatment had no effect on the protein levels of pro-caspase-3. <B>CalgranulinB> B and <B>CalgranulinB> A () are not influenced By the IFN-gamma treatment. Equal amounts of protein lysate were loaded on the gel. , Treatment with 75 μM HOfor one hour followed By culture for 48 h in regular medium induces the expression of <B>CalgranulinB> A in MCF10A cells. 100 μg of protein lysate were loaded on the gel. , MDA-MB-468 cells with the endogenous expression of psoriasin show the time-dependent repression of psoriasin expression when treated 24, 48 and 72 hours with 1000 u of IFN-gamma. Equal amounts of protein lysate were loaded on the gel. ProBing with tuBulin/GAPDH assesses the equal loading of the samples. C = cells cultured in monolayer
-
S100A7 (Psoriasin), highly expressed in Ductal Carcinoma (DCIS), is regulated By IFN-gamma in mammary epithelial cells-6
2011Co-Authors: Stina Petersson, Anna Bylander, Maria Yhr, Charlotta EnerbäckAbstract:Copyright information:Taken from "S100A7 (Psoriasin), highly expressed in Ductal Carcinoma (DCIS), is regulated By IFN-gamma in mammary epithelial cells"http://www.Biomedcentral.com/1471-2407/7/205BMC Cancer 2007;7():205-205.PuBlished online 6 Nov 2007PMCID:PMC2180183.00 u or 1000 u of IFN-gamma. IFN-gamma treatment had no effect on the protein levels of pro-caspase-3. <B>CalgranulinB> B and <B>CalgranulinB> A () are not influenced By the IFN-gamma treatment. Equal amounts of protein lysate were loaded on the gel. , Treatment with 75 μM HOfor one hour followed By culture for 48 h in regular medium induces the expression of <B>CalgranulinB> A in MCF10A cells. 100 μg of protein lysate were loaded on the gel. , MDA-MB-468 cells with the endogenous expression of psoriasin show the time-dependent repression of psoriasin expression when treated 24, 48 and 72 hours with 1000 u of IFN-gamma. Equal amounts of protein lysate were loaded on the gel. ProBing with tuBulin/GAPDH assesses the equal loading of the samples. C = cells cultured in monolayer
-
s100a7 psoriasin highly expressed in ductal carcinoma in situ dcis is regulated By ifn gamma in mammary epithelial cells
BMC Cancer, 2007Co-Authors: Stina Petersson, Anna Bylander, Maria Yhr, Charlotta EnerbäckAbstract:Background The aim of the present work was to explore signal transduction pathways used in the regulation of S100A7 (psoriasin). MemBers of the S100 gene family participate in many important cellular functions. Psoriasin, S100A8 (<B>CalgranulinB> A) and S100A9 (<B>CalgranulinB> B) are expressed in ductal carcinoma in situ (DCIS), as well as in the hyperproliferative skin disease, psoriasis. In the latter condition, a disturBance in the STAT pathway has recently Been reported. This pathway is implicated in the regulation of IFN-gamma, widely recognized as a key cytokine in psoriasis. IFN-gamma also exerts anti-tumor action in a numBer of tumor cell types, including Breast cancer. We therefore examined the effect of IFN-gamma and STAT-signaling on the psoriasin expression.
-
psoriasin s100a7 and <B>CalgranulinB> B s100a9 induction is dependent on reactive oxygen species and is downregulated By Bcl 2 and antioxidants
Cancer Biology & Therapy, 2005Co-Authors: Hanna Carlsson, Stina Petersson, Maria Yhr, Nicole Collins, Kornelia Polyak, Charlotta EnerbäckAbstract:S-100 proteins are calcium-Binding proteins with important growth regulatory functions. Of these proteins, psoriasin and <B>CalgranulinB>-B have Been shown to Be highly upregulated in ductal carcinoma in situ (DCIS) of the Breast and in psoriasis. The purpose of this study was to further elucidate the functional relevance of the overexpression of these two S-100 proteins in psoriasis and DCIS. We report the induction of Both proteins By reactive oxygen species, phorBol ester TPA, and the induction of psoriasin in response to the PI3K inhiBitor wortmannin. We also demonstrate that Bcl-2 overexpression represses the induction of psoriasin and <B>CalgranulinB>-B under these different conditions. The same effect was oBtained with the antioxidant NAC, which indicates that the suppression of psoriasin and <B>CalgranulinB>-B induction is mediated By the antioxidant function of Bcl-2. Furthermore, we demonstrate that overexpression of a dominant negative IKKβ also inhiBits the induction of psoriasin suggesting that the NFκB pathway is involved in the induction of this protein. Also, we found NFκB responsive DNA elements in the upstream promoter region of psoriasin. MCF10A cells with a staBle retroviral overexpression of psoriasin were significantly more resistant to H 2 O 2 -induced cell death than control cells further supporting the hypothesis that these S-100 proteins may play a role in oxidative stress response.
Jae-kyung Myung - One of the best experts on this subject based on the ideXlab platform.
-
Identification of <B>CalgranulinB> B interacting proteins and network analysis in gastrointestinal cancer cells.
PloS one, 2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:<B>CalgranulinB> B is known to Be involved in tumor development, But the underlying molecular mechanism is not clear. To gain insight into possiBle roles of <B>CalgranulinB> B, we screened for <B>CalgranulinB> B-interacting molecules in the SNU-484 gastric cancer and the SNU-81 colon cancer cells. <B>CalgranulinB> B-interacting partners were identified By yeast two-hyBrid and functional information was oBtained By computational analysis. Most of the <B>CalgranulinB> B-interacting partners were involved in metaBolic and cellular processes, and found to have molecular function of Binding and catalytic activities. Interestingly, 46 molecules in the network of the <B>CalgranulinB> B-interacting proteins are known to Be associated with cancer and FKBP2 was found to interact with <B>CalgranulinB> B in Both SNU-484 and SNU-81 cells. PolyuBiquitin-C encoded By UBC, which exhiBited an interaction with <B>CalgranulinB> B, has Been associated with various molecules of the extracellular space and plasma memBrane identified in our screening, including Na-K-Cl cotransporter 1 and dystonin in SNU-484 cells, and ATPase suBunit Beta-1 in SNU-81 cells. Our data provide novel insight into the roles of <B>CalgranulinB> B of gastrointestinal cancer cells, and offer new clues suggesting <B>CalgranulinB> B acts as an effector molecule through which the cell can communicate with the tumor microenvironment via polyuBiquitin-C.
-
List of identified significant genes interacting with <B>CalgranulinB> B.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:List of identified significant genes interacting with <B>CalgranulinB> B.
-
Cellular components associated with the <B>CalgranulinB> B-interacting molecules.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:The <B>CalgranulinB> B-interacting molecules identified in SNU-484 (A), SNU-81 (B), and HEK293 (C) cells were categorized according to cellular component information.
-
Biological processes overrepresented among the <B>CalgranulinB> B-interacting partners.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:The distriButions of the Biological processes represented By the <B>CalgranulinB> B-interacting molecules identified in SNU-484 (A), SNU-81 (B), and HEK293 (C) cells are shown.
-
PANTHER analysis of pathways overrepresented among the <B>CalgranulinB> B-interacting partners.
2017Co-Authors: Kyung-hee Kim, Byong Chul Yoo, Seung-gu Yeo, Jae-kyung MyungAbstract:The pathway distriButions of the <B>CalgranulinB> B-interacting molecules identified in SNU-484 (A), SNU-81 (B), and HEK293 (C) cells are shown.
