{"title":"ADAMDEC1 and Its Role in Inflammatory Disease and Cancer","authors":"T. Kumagai, S. Fan, A. M. Smith","doi":"10.2147/mnm.s263813","DOIUrl":"https://doi.org/10.2147/mnm.s263813","url":null,"abstract":": A disintegrin and metalloprotease like decysin (ADAMDEC1) is a highly conserved secreted metalloprotease that belongs to a family of A disintegrin and metalloprotease (ADAMs). It is expressed exclusively in the gastrointestinal tract of animals and is known to possess a very rare zinc-binding motif (HEXXHXXGXXD) within the metalloprotease domain. The biological function of ADAMDEC1 as well as its true biological substrates remains unknown although its characteristic features reported to date suggest it plays a fundamental role in the physiology of mammals. Historically its expression, in healthy state, was believed to be limited to the monocyte-derived macrophages (MDMs) and dendritic cells within the gastrointestinal tract; however, the recent development of single-cell sequencing has provided evidence supporting its expression in a wider range of cell types. There is an increasing body of evidence linking the alterations in ADAMDEC1 expression and various inflammatory diseases and cancers. Although a detailed mechanistic role of ADAMDEC1 in these conditions remains elusive. In this review, we aim to summarise the characteristic features of this unique metalloprotease, discuss the associations with various human diseases and define the potential mechanistic role of ADAMDEC1 in mammalian physiology.","PeriodicalId":91141,"journal":{"name":"Metalloproteinases in medicine","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2020-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/mnm.s263813","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"42420149","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"The role of tissue inhibitors of metalloproteinases in microvascular endothelial cell barrier dysfunction during sepsis","authors":"Devika P Jayawardena, Nidhi P Kulkarni, S. Gill","doi":"10.2147/MNM.S156245","DOIUrl":"https://doi.org/10.2147/MNM.S156245","url":null,"abstract":"php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms (https://www.dovepress.com/terms.php). Metalloproteinases In Medicine 2019:6 1–12 Metalloproteinases In Medicine Dovepress","PeriodicalId":91141,"journal":{"name":"Metalloproteinases in medicine","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2019-05-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/MNM.S156245","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48693124","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Nicholas Pullen, A. Pickford, M. Perry, D. Jaworski, Katie F. Loveson, D. Arthur, J. Holliday, T. Van Meter, R. Peckham, W. Younas, S. Briggs, Sophie MacDonald, Thomas M. Butterfield, Myrianni Constantinou, H. Fillmore
{"title":"Current insights into matrix metalloproteinases and glioma progression: transcending the degradation boundary","authors":"Nicholas Pullen, A. Pickford, M. Perry, D. Jaworski, Katie F. Loveson, D. Arthur, J. Holliday, T. Van Meter, R. Peckham, W. Younas, S. Briggs, Sophie MacDonald, Thomas M. Butterfield, Myrianni Constantinou, H. Fillmore","doi":"10.2147/MNM.S105123","DOIUrl":"https://doi.org/10.2147/MNM.S105123","url":null,"abstract":"php and incorporate the Creative Commons Attribution – Non Commercial (unported, v3.0) License (http://creativecommons.org/licenses/by-nc/3.0/). By accessing the work you hereby accept the Terms. Non-commercial uses of the work are permitted without any further permission from Dove Medical Press Limited, provided the work is properly attributed. For permission for commercial use of this work, please see paragraphs 4.2 and 5 of our Terms (https://www.dovepress.com/terms.php). Metalloproteinases In Medicine 2018:5 13–30 Metalloproteinases In Medicine Dovepress","PeriodicalId":91141,"journal":{"name":"Metalloproteinases in medicine","volume":"1 1","pages":""},"PeriodicalIF":0.0,"publicationDate":"2018-09-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/MNM.S105123","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"48525731","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Tyler Duellman, Andrea Doll, Xi Chen, Rie Wakamiya, Jay Yang
{"title":"dCas9-mediated transcriptional activation of tissue inhibitor of metalloproteinases.","authors":"Tyler Duellman, Andrea Doll, Xi Chen, Rie Wakamiya, Jay Yang","doi":"10.2147/MNM.S146752","DOIUrl":"https://doi.org/10.2147/MNM.S146752","url":null,"abstract":"<p><p>Selective gene activation with the dCas9 (deactivated clustered regularly interspaced short palindromic repeats [CRISPR] associated protein 9)/CRISPR targeting of a transcriptional activator effector is now well established. However, the optimal targeting of guide RNA (gRNA) for a given gene is largely a matter of trial and error. We explored the optimal targeting site for tissue inhibitor of metalloproteinases (TIMPs) by first screening multiple gRNA target sites using a luciferase-based promoter-reporter system and next confirmed the effective TIMP induction in the mouse motor neuron-like neuron-enriched spinal cord 34 (NSC34) cells. Screening of many gRNAs targeting the 1-1.9 kB promoter regions of TIMP1-3 identified several hot-spots for optimal gene induction, however, no general pattern defining the optimal target site with respect to the proximity of known transcription factor binding sites or distance from the start ATG was apparent. TIMP2 with a larger basal transcriptional activity showed a greater fold-induction with gRNA compared with TIMP1 or 3 supporting the importance of an open-chromatin for best gRNA-mediated transcriptional induction. The rank order of induction potency for different gRNA identified in the promoter-reporter screening held true for the NSC34 cells. Co-activation with multiple gRNAs greatly increased the gene induction.</p>","PeriodicalId":91141,"journal":{"name":"Metalloproteinases in medicine","volume":"4 ","pages":"63-73"},"PeriodicalIF":0.0,"publicationDate":"2017-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/MNM.S146752","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"35574025","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Emergence of a metalloproteinase / phospholipase A2 axis of systemic inflammation.","authors":"Carlos Fernandez-Patron, Dickson Leung","doi":"10.2147/MNM.S48748","DOIUrl":"https://doi.org/10.2147/MNM.S48748","url":null,"abstract":"<p><p>We review select aspects of the biology of matrix metalloproteinases (MMPs) with a focus on the modulation of inflammatory responses by MMP-2. MMP-2 is a zinc- and calcium-dependent endoprotease with substrates including extracellular matrix proteins, vasoactive peptides and chemokines. Humans and mice with MMP-2 deficiency exhibit a predominantly inflammatory phenotype. Recent research shows that MMP-2 deficient mice display elevated activity of a secreted phospholipase A<sub>2</sub> in the heart. Additionally, MMP-2 deficient mice exhibit abnormally high prostaglandin E<sub>2</sub> levels in various organs (i.e., the heart, brain and liver), signs of inflammation and exacerbated lipopolysaccharide-induced fever. We briefly review the biology of sPLA<sub>2</sub> enzymes to propose the existence of a heart-centric MMP-2/sPLA<sub>2</sub> axis of systemic inflammation. Moreover, we postulate that PLA<sub>2</sub> activation is induced by chemokines, whose ability to signal inflammation is regulated in a tissue-specific fashion by MMPs. Thus, genetic and pharmacologically induced MMP-deficiencies can be expected to perturb PLA<sub>2</sub>-mediated inflammatory mechanisms.</p>","PeriodicalId":91141,"journal":{"name":"Metalloproteinases in medicine","volume":"2 ","pages":"29-38"},"PeriodicalIF":0.0,"publicationDate":"2015-08-13","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/MNM.S48748","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34278553","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Rugmani Padmanabhan Iyer, Mira Jung, Merry L Lindsey
{"title":"Using the laws of thermodynamics to understand how matrix metalloproteinases coordinate the myocardial response to injury.","authors":"Rugmani Padmanabhan Iyer, Mira Jung, Merry L Lindsey","doi":"10.2147/MNM.S74093","DOIUrl":"https://doi.org/10.2147/MNM.S74093","url":null,"abstract":"<p><p>Following myocardial infarction (MI), the left ventricle (LV) undergoes a series of molecular, cellular, and functional alterations that are both part of the wound healing response to form a scar in the infarct region and the consequence of that response. Using the laws of thermodynamics as an analogy, we present here three laws for categorizing the post-MI LV remodeling process. The first law is that the LV will attempt to maintain equilibrium and compensate as a way to maximize function, the second law is that remodeling is progressive and unidirectional, and the third law is that the final goal is (ideally, but not always achievable) a stable, equilibrated scar. This comparison helps to define the boundaries of the system, whether it be the infarct zone, the LV, the heart, or the entire body. This review provides an overview for those not directly in the field and establishes a framework to help prioritize future research directions.</p>","PeriodicalId":91141,"journal":{"name":"Metalloproteinases in medicine","volume":"2 ","pages":"75-82"},"PeriodicalIF":0.0,"publicationDate":"2015-01-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.2147/MNM.S74093","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"34635972","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}