Matrix Biology Plus最新文献

{"title":"The role of the multifaceted long non-coding RNAs: A nuclear-cytosolic interplay to regulate hyaluronan metabolism","authors":"Arianna Parnigoni,&nbsp;Ilaria Caon,&nbsp;Paola Moretto,&nbsp;Manuela Viola,&nbsp;Evgenia Karousou,&nbsp;Alberto Passi,&nbsp;Davide Vigetti","doi":"10.1016/j.mbplus.2021.100060","DOIUrl":"10.1016/j.mbplus.2021.100060","url":null,"abstract":"<div><p>In the extracellular matrix (ECM), the glycosaminoglycan (GAG) hyaluronan (HA) has different physiological roles favouring hydration, elasticity and cell survival. Three different isoforms of HA synthases (HAS1, 2, and 3) are responsible for the production of HA. In several pathologies the upregulation of HAS enzymes leads to an abnormal HA accumulation causing cell dedifferentiation, proliferation and migration thus favouring cancer progression, fibrosis and vascular wall thickening. An intriguing new player in HAS2 gene expression regulation and HA production is the long non-coding RNA (lncRNA) hyaluronan synthase 2 antisense 1 (HAS2-AS1). A significant part of mammalian genomes corresponds to genes that transcribe lncRNAs; they can regulate gene expression through several mechanisms, being involved not only in maintaining the normal homeostasis of cells and tissues, but also in the onset and progression of different diseases, as demonstrated by the increasing number of studies published through the last decades. HAS2-AS1 is no exception: it can be localized both in the nucleus and in the cytosol, regulating cancer cells as well as vascular smooth muscle cells behaviour.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100060"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100060","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347651","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":"Driving fibrosis in neuromuscular diseases: Role and regulation of Connective tissue growth factor (CCN2/CTGF)","authors":"Daniela L. Rebolledo ,&nbsp;Kenneth E. Lipson ,&nbsp;Enrique Brandan","doi":"10.1016/j.mbplus.2021.100059","DOIUrl":"10.1016/j.mbplus.2021.100059","url":null,"abstract":"<div><p>Connective tissue growth factor or cellular communication network 2 (CCN2/CTGF) is a matricellular protein member of the CCN family involved in several crucial biological processes. In skeletal muscle, CCN2/CTGF abundance is elevated in human muscle biopsies and/or animal models for diverse neuromuscular pathologies, including muscular dystrophies, neurodegenerative disorders, muscle denervation, and muscle overuse. In this context, CCN2/CTGF is deeply involved in extracellular matrix (ECM) modulation, acting as a strong pro-fibrotic factor that promotes excessive ECM accumulation. Reducing CCN2/CTGF levels or biological activity in pathological conditions can decrease fibrosis, improve muscle architecture and function. In this work, we summarize information about the role of CCN2/CTGF in fibrosis associated with neuromuscular pathologies and the mechanisms and signaling pathways that regulate their expression in skeletal muscle.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100059"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100059","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39345197","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":"BMP antagonists in tissue development and disease","authors":"Annkatrin Correns ,&nbsp;Laura-Marie A. Zimmermann ,&nbsp;Clair Baldock ,&nbsp;Gerhard Sengle","doi":"10.1016/j.mbplus.2021.100071","DOIUrl":"10.1016/j.mbplus.2021.100071","url":null,"abstract":"<div><p>Bone morphogenic proteins (BMPs) are important growth regulators in embryogenesis and postnatal homeostasis. Their tight regulation is crucial for successful embryonic development as well as tissue homeostasis in the adult organism. BMP inhibition by natural extracellular biologic antagonists represents the most intensively studied mechanistic concept of BMP growth factor regulation. It was shown to be critical for numerous developmental programs, including germ layer specification and spatiotemporal gradients required for the establishment of the dorsal–ventral axis and organ formation. The importance of BMP antagonists for extracellular matrix homeostasis is illustrated by the numerous human connective tissue disorders caused by their mutational inactivation. Here, we will focus on the known functional interactions targeting BMP antagonists to the ECM and discuss how these interactions influence BMP antagonist activity. Moreover, we will provide an overview about the current concepts and investigated molecular mechanisms modulating BMP inhibitor function in the context of development and disease.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100071"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100071","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347658","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":"Procollagen C-proteinase enhancer-1 (PCPE-1), a potential biomarker and therapeutic target for fibrosis","authors":"Priscillia Lagoutte,&nbsp;Emmanuel Bettler,&nbsp;Sandrine Vadon-Le Goff,&nbsp;Catherine Moali","doi":"10.1016/j.mbplus.2021.100062","DOIUrl":"10.1016/j.mbplus.2021.100062","url":null,"abstract":"<div><p>The correct balance between collagen synthesis and degradation is essential for almost every aspect of life, from development to healthy aging, reproduction and wound healing. When this balance is compromised by external or internal stress signals, it very often leads to disease as is the case in fibrotic conditions. Fibrosis occurs in the context of defective tissue repair and is characterized by the excessive, aberrant and debilitating deposition of fibril-forming collagens. Therefore, the numerous proteins involved in the biosynthesis of fibrillar collagens represent a potential and still underexploited source of therapeutic targets to prevent fibrosis. One such target is procollagen C-proteinase enhancer-1 (PCPE-1) which has the unique ability to accelerate procollagen maturation by BMP-1/tolloid-like proteinases (BTPs) and contributes to trigger collagen fibrillogenesis, without interfering with other BTP functions or the activities of other extracellular metalloproteinases. This role is achieved through a fine-tuned mechanism of action that is close to being elucidated and offers promising perspectives for drug design. Finally, the <em>in vivo</em> data accumulated in recent years also confirm that PCPE-1 overexpression is a general feature and early marker of fibrosis. In this review, we describe the results which presently support the driving role of PCPE-1 in fibrosis and discuss the questions that remain to be solved to validate its use as a biomarker or therapeutic target.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100062"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100062","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347653","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":"Scaffold-free 3D cell culture of primary skin fibroblasts induces profound changes of the matrisome","authors":"Bich Vu ,&nbsp;Glauco R. Souza ,&nbsp;Jörn Dengjel","doi":"10.1016/j.mbplus.2021.100066","DOIUrl":"10.1016/j.mbplus.2021.100066","url":null,"abstract":"<div><p>The human skin has a highly developed extracellular matrix (ECM) that is vital for proper skin functioning, its 3D architecture playing a pivotal role in support and guidance of resident and invading cells. To establish relevant <em>in vitro</em> models mimicking the complex design observed <em>in vivo,</em> scaffold-based and scaffold-free 3D cell culture systems have been developed. Here we show that scaffold-free systems are well suited for the analysis of ECM protein regulation. Using quantitative mass spectrometry-based proteomics in combination with magnetic 3D bioprinting we characterize changes in the proteome of skin fibroblasts and squamous cell carcinoma cells. Transferring cells from 2D to 3D without any additional scaffold induces a profound upregulation of matrisome proteins indicating the generation of a complex, tissue-like ECM.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100066"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100066","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347655","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":"Multimerin-2 orchestrates the cross-talk between endothelial cells and pericytes: A mechanism to maintain vascular stability","authors":"Albina Fejza ,&nbsp;Evelina Poletto ,&nbsp;Greta Carobolante ,&nbsp;Lucrezia Camicia ,&nbsp;Eva Andreuzzi ,&nbsp;Alessandra Capuano ,&nbsp;Eliana Pivetta ,&nbsp;Rosanna Pellicani ,&nbsp;Roberta Colladel ,&nbsp;Stefano Marastoni ,&nbsp;Roberto Doliana ,&nbsp;Renato V. Iozzo ,&nbsp;Paola Spessotto ,&nbsp;Maurizio Mongiat","doi":"10.1016/j.mbplus.2021.100068","DOIUrl":"10.1016/j.mbplus.2021.100068","url":null,"abstract":"<div><p>Tumor angiogenesis is vital for the growth and development of various solid cancers and as such is a valid and promising therapeutic target. Unfortunately, the use of the currently available anti-angiogenic drugs increases the progression-free survival by only a few months. Conversely, targeting angiogenesis to prompt both vessel reduction and normalization, has been recently viewed as a promising approach to improve therapeutic efficacy. As a double-edged sword, this line of attack may on one side halt tumor growth as a consequence of the reduction of nutrients and oxygen supplied to the tumor cells, and on the other side improve drug delivery and, hence, efficacy. Thus, it is of upmost importance to better characterize the mechanisms regulating vascular stability. In this context, recruitment of pericytes along the blood vessels is crucial to their maturation and stabilization. As the extracellular matrix molecule Multimerin-2 is secreted by endothelial cells and deposited also in juxtaposition between endothelial cells and pericytes, we explored Multimerin-2 role in the cross-talk between the two cell types. We discovered that Multimerin-2 is an adhesion substrate for pericytes. Interestingly, and consistent with the notion that Multimerin-2 is a homeostatic molecule deposited in the later stages of vessel formation, we found that the interaction between endothelial cells and pericytes promoted the expression of Multimerin-2. Furthermore, we found that Multimerin-2 modulated the expression of key cytokines both in endothelial cells and pericytes. Collectively, our findings posit Multimerin-2 as a key molecule in the cross-talk between endothelial cells and pericytes and suggest that the expression of this glycoprotein is required to maintain vascular stability.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100068"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100068","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347656","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":"Distinct contributions of meprins to skin regeneration after injury – Meprin α a physiological processer of pro-collagen VII","authors":"Daniel Kruppa ,&nbsp;Florian Peters ,&nbsp;Olivier Bornert ,&nbsp;Mareike D. Maler ,&nbsp;Stefan F. Martin ,&nbsp;Christoph Becker-Pauly ,&nbsp;Alexander Nyström","doi":"10.1016/j.mbplus.2021.100065","DOIUrl":"10.1016/j.mbplus.2021.100065","url":null,"abstract":"<div><p>Astacin-like proteinases (ALPs) are regulators of tissue and extracellular matrix (ECM) homeostasis. They convey this property through their ability to convert ECM protein pro-forms to functional mature proteins and by regulating the bioavailability of growth factors that stimulate ECM synthesis. The most studied ALPs in this context are the BMP-1/tolloid-like proteinases. The other subclass of ALPs in vertebrates – the meprins, comprised of meprin α and meprin β – are emerging as regulators of tissue and ECM homeostasis but have so far been only limitedly investigated. Here, we functionally assessed the roles of meprins in skin wound healing using mice genetically deficient in one or both meprins. Meprin deficiency did not change the course of macroscopic wound closure. However, subtle but distinct contributions of meprins to the healing process and dermal homeostasis were observed. Loss of both meprins delayed re-epithelialization and reduced macrophage infiltration. Abnormal dermal healing and ECM regeneration was observed in meprin deficient wounds. Our analyses also revealed meprin α as one proteinase responsible for maturation of pro-collagen VII to anchoring fibril-forming-competent collagen VII <em>in vivo</em>. Collectively, our study identifies meprins as subtle players in skin wound healing.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100065"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100065","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347654","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":"Small leucine-rich proteoglycans in physiological and biomechanical function of bone","authors":"Rui Hua,&nbsp;Jean X. Jiang","doi":"10.1016/j.mbplus.2021.100063","DOIUrl":"10.1016/j.mbplus.2021.100063","url":null,"abstract":"<div><p>Proteoglycans (PGs) contain long unbranched glycosaminoglycan (GAG) chains attached to core proteins. In the bone extracellular matrix, PGs represent a class of non-collagenous proteins, and have high affinity to minerals and collagen. Considering the highly negatively charged character of GAGs and their interfibrillar positioning interconnecting with collagen fibrils, PGs and GAGs play pivotal roles in maintaining hydrostatic and osmotic pressure in the matrix. In this review, we will discuss the role of PGs, especially the small leucine-rich proteoglycans, in regulating the bioactivity of multiple cytokines and growth factors, and the bone turnover process. In addition, we focus on the coupling effects of PGs and GAGs in the hydration status of bone extracellular matrix, thus modulating bone biomechanical properties under physiological and pathological conditions.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100063"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100063","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347652","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":"The Yin and Yang of extracellular matrix","authors":"Maurizio Mongiat ,&nbsp;Alexander Nyström","doi":"10.1016/j.mbplus.2021.100075","DOIUrl":"10.1016/j.mbplus.2021.100075","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"11 ","pages":"Article 100075"},"PeriodicalIF":0.0,"publicationDate":"2021-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100075","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39347657","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":"The critical role of collagen VI in lung development and chronic lung disease","authors":"Jared A. Mereness,&nbsp;Thomas J. Mariani","doi":"10.1016/j.mbplus.2021.100058","DOIUrl":"10.1016/j.mbplus.2021.100058","url":null,"abstract":"<div><p>Type VI collagen (collagen VI) is an obligate extracellular matrix component found mainly in the basement membrane region of many mammalian tissues and organs, including skeletal muscle and throughout the respiratory system. Collagen VI is probably most recognized in medicine as the genetic cause of a spectrum of muscular dystrophies, including Ullrich Congenital Myopathy and Bethlem Myopathy. Collagen VI is thought to contribute to myopathy, at least in part, by mediating muscle fiber integrity by anchoring myoblasts to the muscle basement membrane. Interestingly, collagen VI myopathies present with restrictive respiratory insufficiency, thought to be due primarily to thoracic muscular weakening. Although it was recently recognized as one of the (if not the) most abundant collagens in the mammalian lung, there is a substantive knowledge gap concerning its role in respiratory system development and function. A few studies have suggested that collagen VI insufficiency is associated with airway epithelial cell survival and altered lung function. Our recent work suggested collagen VI may be a genomic risk factor for chronic lung disease in premature infants. Using this as motivation, we thoroughly assessed the role of collagen VI in lung development and in lung epithelial cell biology. Here, we describe the state-of-the-art for collagen VI cell and developmental biology within the respiratory system, and reveal its essential roles in normal developmental processes and airway epithelial cell phenotype and intracellular signaling.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"10 ","pages":"Article 100058"},"PeriodicalIF":0.0,"publicationDate":"2021-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100058","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39058764","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}