Matrix Biology Plus最新文献

{"title":"Deletion of type VIII collagen reduces blood pressure, increases carotid artery functional distensibility and promotes elastin deposition","authors":"Amanda L. Mohabeer ,&nbsp;Jeffrey T. Kroetsch ,&nbsp;Meghan McFadden ,&nbsp;Negin Khosraviani ,&nbsp;Thomas J. Broekelmann ,&nbsp;Guangpei Hou ,&nbsp;Hangjun Zhang ,&nbsp;Yu-Qing Zhou ,&nbsp;Minyao Wang ,&nbsp;Anthony O. Gramolini ,&nbsp;Robert P. Mecham ,&nbsp;Scott P. Heximer ,&nbsp;Steffen-Sebastian Bolz ,&nbsp;Michelle P. Bendeck","doi":"10.1016/j.mbplus.2021.100085","DOIUrl":"10.1016/j.mbplus.2021.100085","url":null,"abstract":"<div><p>Arterial stiffening is a significant predictor of cardiovascular disease development and mortality. In elastic arteries, stiffening refers to the loss and fragmentation of elastic fibers, with a progressive increase in collagen fibers. Type VIII collagen (Col-8) is highly expressed developmentally, and then once again dramatically upregulated in aged and diseased vessels characterized by arterial stiffening. Yet its biophysical impact on the vessel wall remains unknown. The purpose of this study was to test the hypothesis that Col-8 functions as a matrix scaffold to maintain vessel integrity during extracellular matrix (ECM) development. These changes are predicted to persist into the adult vasculature, and we have tested this in our investigation. Through our <em>in vivo</em> and <em>in vitro</em> studies, we have determined a novel interaction between Col-8 and elastin. Mice deficient in Col-8 (Col8^−/−) had reduced baseline blood pressure and increased arterial compliance, indicating an enhanced Windkessel effect in conducting arteries. Differences in both the ECM composition and VSMC activity resulted in Col8^−/− carotid arteries that displayed increased crosslinked elastin and functional distensibility, but enhanced catecholamine-induced VSMC contractility. <em>In vitro</em> studies revealed that the absence of Col-8 dramatically increased tropoelastin mRNA and elastic fiber deposition in the ECM, which was decreased with exogenous Col-8 treatment. These findings suggest a causative role for Col-8 in reducing mRNA levels of tropoelastin and the presence of elastic fibers in the matrix. Moreover, we also found that Col-8 and elastin have opposing effects on VSMC phenotype, the former promoting a synthetic phenotype, whereas the latter confers quiescence. These studies further our understanding of Col-8 function and open a promising new area of investigation related to elastin biology.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100085"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/39/d3/main.PMC8517381.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39556913","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":"Comprehensive quantitative characterization of the human term amnion proteome","authors":"Eva Avilla-Royo ,&nbsp;Katharina Gegenschatz-Schmid ,&nbsp;Jonas Grossmann ,&nbsp;Tobias Kockmann ,&nbsp;Roland Zimmermann ,&nbsp;Jess Gerrit Snedeker ,&nbsp;Nicole Ochsenbein-Kölble ,&nbsp;Martin Ehrbar","doi":"10.1016/j.mbplus.2021.100084","DOIUrl":"10.1016/j.mbplus.2021.100084","url":null,"abstract":"<div><p>The loss of fetal membrane (FM) integrity and function at an early time point during pregnancy can have devastating consequences for the fetus and the newborn. However, biomaterials for preventive sealing and healing of FMs are currently non-existing, which can be partly attributed to the current fragmentary knowledge of FM biology. Despite recent advances in proteomics analysis, a robust and comprehensive description of the amnion proteome is currently lacking. Here, by an optimized protein sample preparation and offline fractionation before liquid chromatography coupled to mass spectrometry (LC-MS) analysis, we present a characterization of the healthy human term amnion proteome, which covers more than 40% of the previously reported transcripts in similar RNA sequencing datasets and, with more than 5000 identifications, greatly outnumbers previous reports. Together, beyond providing a basis for the study of compromised and preterm ruptured FMs, this comprehensive human amnion proteome is a stepping-stone for the development of novel healing-inducing biomaterials. The proteomic dataset has been deposited in the ProteomeXchange Consortium with the identifier PXD019410.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100084"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/c6/31/main.PMC8572956.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39614108","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":"Cooperation of cell adhesion and autophagy in the brain: Functional roles in development and neurodegenerative disease","authors":"Sarah J. Hernandez ,&nbsp;Gianna Fote ,&nbsp;Andrea M. Reyes-Ortiz ,&nbsp;Joan S. Steffan ,&nbsp;Leslie M. Thompson","doi":"10.1016/j.mbplus.2021.100089","DOIUrl":"10.1016/j.mbplus.2021.100089","url":null,"abstract":"<div><p>Cellular adhesive connections directed by the extracellular matrix (ECM) and maintenance of cellular homeostasis by autophagy are seemingly disparate functions that are molecularly intertwined, each regulating the other. This is an emerging field in the brain where the interplay between adhesion and autophagy functions at the intersection of neuroprotection and neurodegeneration. The ECM and adhesion proteins regulate autophagic responses to direct protein clearance and guide regenerative programs that go awry in brain disorders. Concomitantly, autophagic flux acts to regulate adhesion dynamics to mediate neurite outgrowth and synaptic plasticity with functional disruption contributed by neurodegenerative disease. This review highlights the cooperative exchange between cellular adhesion and autophagy in the brain during health and disease. As the mechanistic alliance between adhesion and autophagy has been leveraged therapeutically for metastatic disease, understanding overlapping molecular functions that direct the interplay between adhesion and autophagy might uncover therapeutic strategies to correct or compensate for neurodegeneration.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100089"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/75/fe/main.PMC8579148.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39630668","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":"Biomechanical properties of endothelial glycocalyx: An imperfect pendulum","authors":"Xi Zhuo Jiang ,&nbsp;Michael S. Goligorsky","doi":"10.1016/j.mbplus.2021.100087","DOIUrl":"10.1016/j.mbplus.2021.100087","url":null,"abstract":"<div><p>Endothelial glycocalyx plays a crucial role in hemodynamics in health and disease, yet studying it is met by multiple technical hindrances. We attempted to outline our views on some biomechanical properties of endothelial glycocalyx, which are potentially amenable to mathematical modeling. We start with the null-hypothesis ascribing to glycocalyx the properties of a pendulum and reject this hypothesis on the grounds of multiple obstacles for pendulum behavior, such as rich decoration with flexible negatively charged side-chains, variable length and density, fluid fixation to the plasma membrane. We next analyze the current views on membrane attachments to the cortical actin web, its pulsatile contraction-relaxation cycles which rebound to the changes in tension of the plasma membrane. Based on this, we consider the outside-in signaling, the basis for mechanotransduction, and the dampening action of the inside-out signaling. The aperiodic oscillatory motions of glycocalyx and cortical actin web underlie our prediction of two functional pacemakers. We next advance an idea that the glycocalyx, plasma membrane, and cortical actin web represent a structure-functional unit and propose the concept of tensegrity model. Finally, we present our recent data suggesting that erythrocytes are gliding or hovering and rotating over the surface of intact glycocalyx, whereas the rotational and hovering components of their passage along the capillaries are lost when glycocalyx of either is degraded. These insights into the mechanics of endothelial glycocalyx motions may be of value in crosspollination between biomechanics, physiology, and pathophysiology for deeper appreciation of its rich untapped resources in health and pharmacotherapy in disease.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100087"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f3/3e/main.PMC8596327.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39657247","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":"Biophotonic tools for probing extracellular matrix mechanics","authors":"B.E. Sherlock ,&nbsp;J. Chen ,&nbsp;J.C. Mansfield ,&nbsp;E. Green ,&nbsp;C.P. Winlove","doi":"10.1016/j.mbplus.2021.100093","DOIUrl":"10.1016/j.mbplus.2021.100093","url":null,"abstract":"<div><p>The complex, hierarchical and heterogeneous biomechanics of the extracellular matrix (ECM) are central to the health of multicellular organisms. Characterising the distribution, dynamics and above all else origins of ECM biomechanics are challenges that have captivated researchers for decades. Recently, a suite of biophotonics techniques have emerged as powerful new tools to investigate ECM biomechanics. In this mini-review, we discuss how the non-destructive, sub-micron resolution imaging capabilities of Raman spectroscopy and nonlinear microscopy are being used to interrogate the biomechanics of thick, living tissues. These high speed, label-free techniques are implemented during mechanical testing, providing unprecedented insight into the compositional and structural response of the ECM to changes in the mechanical environment.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100093"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC8661043/pdf/main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39746298","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 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}