Miguel Gonzalez-Andrades, Supriya S Jalimarada, Maria Rodriguez-Benavente, Marissa N Feeley, Ashley M Woodward, Dina B AbuSamra, Pablo Argüeso
{"title":"Golgi α1,2-mannosidase I induces clustering and compartmentalization of CD147 during epithelial cell migration.","authors":"Miguel Gonzalez-Andrades, Supriya S Jalimarada, Maria Rodriguez-Benavente, Marissa N Feeley, Ashley M Woodward, Dina B AbuSamra, Pablo Argüeso","doi":"10.1080/19336918.2020.1764170","DOIUrl":"10.1080/19336918.2020.1764170","url":null,"abstract":"<p><p>CD147 is a widely expressed matrix metalloproteinase inducer involved in the regulation of cell migration. The high glycosylation and ability to undergo oligomerization have been linked to CD147 function, yet there is limited understanding on the molecular mechanisms behind these processes. The current study demonstrates that the expression of Golgi α1,2-mannosidase I is key to maintaining the cell surface organization of CD147 during cell migration. Using an in vitro model of stratified human corneal epithelial wound healing, we show that CD147 is clustered within lateral plasma membranes at the leading edge of adjacent migrating cells. This localization correlates with a surge in matrix metalloproteinase activity and an increase in the expression of α1,2-mannosidase subtype IC (MAN1C1). Global inhibition of α1,2-mannosidase I activity with deoxymannojirimycin markedly attenuates the glycosylation of CD147 and disrupts its surface distribution at the leading edge, concomitantly reducing the expression of matrix metalloproteinase-9. Likewise, treatment with deoxymannojirimycin or siRNA-mediated knockdown of MAN1C1 impairs the ability of the carbohydrate-binding protein galectin-3 to stimulate CD147 clustering in unwounded cells. We conclude that the mannose-trimming activity of α1,2-mannosidase I coordinates the clustering and compartmentalization of CD147 that follows an epithelial injury.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.3,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7250185/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37946691","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The anti-cancer properties of heparin and its derivatives: a review and prospect.","authors":"Sai-Nan Ma, Zhi-Xiang Mao, Yang Wu, Ming-Xing Liang, Dan-Dan Wang, Xiu Chen, Ping-An Chang, Wei Zhang, Jin-Hai Tang","doi":"10.1080/19336918.2020.1767489","DOIUrl":"https://doi.org/10.1080/19336918.2020.1767489","url":null,"abstract":"<p><p>Heparin, including unfractionated heparin (UFH), low-molecular-weight heparin (LMWH) and heparin derivatives, are commonly used in venous thromboembolism treatment and reportedly have beneficial effects on cancer survival. Heparin can affect the proliferation, adhesion, angiogenesis, migration and invasion of cancer cells via multiple mechanisms. The main mechanisms involve inhibition of heparanase, P-/L-selectin, angiogenesis, and interference with the CXCL12-CXCR4 axis. Here we summarize the current experimental evidence regarding the anti-cancer role of heparin and its derivatives, and conclude that there is evidence to support heparin's role in inhibiting cancer progression, making it a promising anti-cancer agent.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2020.1767489","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38046532","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Short-term <i>ex-vivo</i> exposure to hydrogen sulfide enhances murine hematopoietic stem and progenitor cell migration, homing, and proliferation.","authors":"Anoushka Khanna, Namita Indracanti, Rina Chakrabarti, Prem Kumar Indraganti","doi":"10.1080/19336918.2020.1842131","DOIUrl":"10.1080/19336918.2020.1842131","url":null,"abstract":"<p><p>For successful transplantation of Hematopoietic Stem cells (HSCs), it is quite necessary that efficient homing, engraftment and retention of HSC self-renewal capacity takes place, which is often restricted due to inadequate number of adult HSCs. Here, we report that short-term <i>ex-vivo</i> treatment of mouse bone marrow mononuclear cells (BMMNCs) to Sodium Hydrogen Sulfide (NaHS, hydrogen sulfide-H<sub>2</sub>S donor) can be used as a possible strategy to overcome such hurdle. H<sub>2</sub>S increases the expression of CXCR4 on HSPCs, enhancing their migration toward SDF-1α in-vitro and thus homing to BM niche. . Additionally, <i>in-vitro</i> studies revealed that H<sub>2</sub>S has a role in activating mitochondria, thus, pushing quiescent HSCs into division. These results suggest a readily available and cost-effective method to facilitate efficient HSC transplantation.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2020.1842131","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38659480","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"FGFR1 regulates proliferation and metastasis by targeting CCND1 in FGFR1 amplified lung cancer.","authors":"Ying Yang, Tingting Lu, Ziming Li, Shun Lu","doi":"10.1080/19336918.2020.1766308","DOIUrl":"https://doi.org/10.1080/19336918.2020.1766308","url":null,"abstract":"<p><p><b>Aims</b>: The analysis of the online databases revealed that CCND1 expression is correlated with poor prognosis in LSCC. We aimed to explore the function of CCND1 in tumor progression in LSCC.<b>Main methods</b>: The expression of mRNA was measured using qRT-PCR. Protein expression was assessed by Western blot. Cell migration and invasion were assessed by transwell assay.<b>Key findings</b>: CCND1 was co-overexpressed with FGFR1 in lung cancer patients. Overexpression of CCND1 promoted LSCC cell proliferation and metastasis. FGFR1 promoted the processes of EMT through AKT/MAPK signaling by targeting CCND1 in FGFR1-amplification cell lines.<b>Significance</b>: IIn conclusion, our study demonstrated the regulatory mechanism between CCND1 and FGFR1 in FGFR1 amplified LSCC. Co-targeting CCND1 and FGFR1 could provide greater clinical benefits.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2020.1766308","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37912619","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Cell Adhesion & MigrationPub Date : 2020-12-01Epub Date: 2018-09-25DOI: 10.1080/19336918.2018.1516982
Mariana Costa Braga Schmidt, Katia L P Morais, Maíra Estanislau Soares de Almeida, Asif Iqbal, Mauricio Barbugiani Goldfeder, Ana Marisa Chudzinski-Tavassi
{"title":"Amblyomin-X, a recombinant Kunitz-type inhibitor, regulates cell adhesion and migration of human tumor cells.","authors":"Mariana Costa Braga Schmidt, Katia L P Morais, Maíra Estanislau Soares de Almeida, Asif Iqbal, Mauricio Barbugiani Goldfeder, Ana Marisa Chudzinski-Tavassi","doi":"10.1080/19336918.2018.1516982","DOIUrl":"https://doi.org/10.1080/19336918.2018.1516982","url":null,"abstract":"<p><p>In a tumor microenvironment, endothelial cell migration and angiogenesis allow cancer to spread to other organs causing metastasis. Indeed, a number of molecules that are involved in cytoskeleton re-organization and intracellular signaling have been investigated for their effects on tumor cell growth and metastasis. Alongside that, Amblyomin-X, a recombinant Kunitz-type protein, has been shown to reduce metastasis and tumor growth in in vivo experiments. In the present report, we provide a mechanistic insight to these antitumor effects, this is, Amblyomin-X modulates Rho-GTPases and uPAR signaling, and reduces the release of MMPs, leading to disruption of the actin cytoskeleton and decreased cell migration of tumor cell lines. Altogether, our data support a role for Amblyomin-X as a novel potential antitumor drug.</p><p><strong>Abbreviations: </strong>Amb-X: Amblyomin-X; ECGF: endotelial cell growth factor; ECM: extracellular matrix; GAPDH: glyceraldehyde-3-phosphate dehydrogenase; HUVEC: human umbilical vein endothelial cell; LRP1: low-density lipoprotein receptor-related protein; MMP: matrix metalloproteinase; HPI-4: hedgehog pathway inhibitor 4; PAI-1: plasminogen activator inhibitor 1; PMA: phorbol 12-myristate-13-acetate; TFPI: tissue factor pathway inhibitor; uPA: urokinase plasminogen activator; uPAR: uPA receptor.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2018.1516982","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"36509658","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Fibronectin type III domain-containing 4 promotes the migration and differentiation of bovine skeletal muscle-derived satellite cells via focal adhesion kinase.","authors":"Zhao Wang, Zhiqi Wang, Yusheng Pang, Huili Tong, Yunqin Yan, Shuang Li, Shufeng Li","doi":"10.1080/19336918.2020.1810508","DOIUrl":"https://doi.org/10.1080/19336918.2020.1810508","url":null,"abstract":"<p><p>FNDC4 is an anti-inflammatory factor that alters the activation state of macrophages; it is used to treat colitis in mice. However, its role in muscle formation and mechanism of function remains unknown. We found that FNDC4 promotes the bovine MDSCs migration and differentiation. Furthermore, we reported that it interacts with integrin β1 (ITGβ1). FAK, mediated by ITGβ1, regulates cell migration. Our results found FNDC4 to influence the expression of p-FAK, p-paxillin, and vinculin. Then, overexpressed or added FNDC4 protein could not influence migration and differentiation any more when the activated form of FAK was reduced. Therefore, we concluded that FNDC4 promotes the differentiation and migration of bovine MDSCs via the FAK, mediated by the ITGβ1 receptor.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2020.1810508","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38340662","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Joanna Pastwińska, Aurelia Walczak-Drzewiecka, Magdalena Łukasiak, Marcin Ratajewski, Jarosław Dastych
{"title":"Hypoxia regulates human mast cell adhesion to fibronectin via the PI3K/AKT signaling pathway.","authors":"Joanna Pastwińska, Aurelia Walczak-Drzewiecka, Magdalena Łukasiak, Marcin Ratajewski, Jarosław Dastych","doi":"10.1080/19336918.2020.1764690","DOIUrl":"https://doi.org/10.1080/19336918.2020.1764690","url":null,"abstract":"<p><p>A decrease in oxygen concentration is a hallmark of inflammatory reactions resulting from infection or homeostasis disorders. Mast cells interact with extracellular matrix and other cells by adhesion receptors. We investigated the effect of hypoxia on integrin-mediated mast cell adhesion to fibronectin. We found that it was mediated by the α5/β1 receptor and that hypoxia significantly upregulated this process. Hypoxia-mediated increases in mast cell adhesion occurred without increased surface expression of integrins, suggesting regulation by inside-out integrin signaling. Hypoxia also mediated an increase in phosphorylation of Akt, and PI3'kinase inhibitors abolished hypoxia-mediated mast cell adhesion. Hypoxia upregulates the function of integrin receptors by PI3' kinase-dependent signaling. This process might be important for the location of mast cells at inflammatory sites.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2020.1764690","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37952713","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"MicroRNA-203 inhibits epithelial-mesenchymal transition, migration, and invasion of renal cell carcinoma cells via the inactivation of the PI3K/AKT signaling pathway by inhibiting CAV1.","authors":"Ning Han, Hai Li, Hui Wang","doi":"10.1080/19336918.2020.1827665","DOIUrl":"https://doi.org/10.1080/19336918.2020.1827665","url":null,"abstract":"<p><p>The present study aimed to evaluate the underlying mechanism of microRNA-203 (miR-203) in renal cell carcinoma (RCC) involving the PI3K/AKT signaling pathway. The results revealed downregulated miR-203 and upregulated CAV1 in RCC tissues. Upregulated miR-203 and downregulated CAV1 increased E-cadherin expression and cell apoptosis, decreased β-catenin and N-cadherin expression and cell proliferation, migration and invasion, and blocked cell cycle entry. CAV1, a target gene of miR-203, decreased by up-regulated miR-203, and silencing CAV1 led to the inactivation of PI3K/AKT signaling pathway. In conclusion, our findings suggested that miR-203-mediated direct suppression of CAV1 inhibits EMT of RCC cells via inactivation of the PI3K/AKT signaling pathway.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2020.1827665","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38528317","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Structure, regulatory factors and cancer-related physiological effects of ADAM9.","authors":"M A Haoyuan, L I Yanshu","doi":"10.1080/19336918.2020.1817251","DOIUrl":"https://doi.org/10.1080/19336918.2020.1817251","url":null,"abstract":"<p><p>The ADAMs family belongs to the transmembrane protein superfamily of zinc-dependent metalloproteases, which consists of multiple domains. These domains have independent but complementary functions that enable them to participate in multiple biological processes. Among them, ADAM9 can not only participate in the degradation of extracellular matrix as a metalloprotease, but also mediate tumor cell adhesion through its deintegrin domain, which is closely related to tumor invasion and metastasis. It is widely expressed in a variety of tumor cells and can affect the proliferation, invasion and metastasis of related cancer cells. We provide our views on current progress, its increasing importance as a strategic treatment goal, and our vision for the future of ADAM9.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2020.1817251","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"38335795","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Effect arylamine N-acetyltransferase 1 on morphology, adhesion, migration, and invasion of MDA-MB-231 cells: role of matrix metalloproteinases and integrin αV.","authors":"Pengcheng Li, Neville J Butcher, Rodney F Minchin","doi":"10.1080/19336918.2019.1710015","DOIUrl":"https://doi.org/10.1080/19336918.2019.1710015","url":null,"abstract":"<p><p>Reducted arylamine N-acetyltransferase (NAT1) in breast cancers is associated with poor patient survival. NAT1 has also been associated with changes in cancer cell survival and invasion both <i>in</i><i>vitro</i> and <i>in</i><i>vivo</i>. Here, we report the effects of NAT1 in cancer cell invasion by addressing its role in adherence, migration, and invasion <i>in vitro</i>. The NAT1 gene was deleted in MDA-MB-231, HT-29 and HeLa cells using CRISPR/Cas9 gene editing. Loss of NAT1 increased adherence to collagen in all three cell-lines but migration was unaffected. NAT1 deletion decreased invasion and induced changes to cell morphology. These effects were independent of matrix metalloproteinases but were related to integrin ITGαV expression. The data suggest NAT1 is important in adhesion and invasion through integrin expression.</p>","PeriodicalId":9680,"journal":{"name":"Cell Adhesion & Migration","volume":null,"pages":null},"PeriodicalIF":3.2,"publicationDate":"2020-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1080/19336918.2019.1710015","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"37518425","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":3,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}