Matrix Biology Plus最新文献

{"title":"Glycocalyx mechanotransduction mechanisms are involved in renal cancer metastasis","authors":"Heriberto Moran ,&nbsp;Limary M. Cancel ,&nbsp;Peigen Huang ,&nbsp;Sylvie Roberge ,&nbsp;Tuoye Xu ,&nbsp;John M. Tarbell ,&nbsp;Lance L. Munn","doi":"10.1016/j.mbplus.2021.100100","DOIUrl":"10.1016/j.mbplus.2021.100100","url":null,"abstract":"<div><p>Mammalian cells, including cancer cells, are covered by a surface layer containing cell bound proteoglycans, glycoproteins, associated glycosaminoglycans and bound proteins that is commonly referred to as the glycocalyx. Solid tumors also have a dynamic fluid microenvironment with elevated interstitial flow. In the present work we further investigate the hypothesis that interstitial flow is sensed by the tumor glycocalyx leading to activation of cell motility and metastasis. Using a highly metastatic renal carcinoma cell line (SN12L1) and its low metastatic counterpart (SN12C) we demonstrate in vitro that the small molecule Suberoylanilide Hydroxamic Acid (SAHA) inhibits the heparan sulfate synthesis enzyme N-deacetylase-N-sulfotransferase-1, reduces heparan sulfate in the glycocalyx and suppresses SN12L1 motility in response to interstitial flow. SN12L1 cells implanted in the kidney capsule of SCID mice formed large primary tumors and metastasized to distant organs, but when treated with SAHA metastases were not detected. In another set of experiments, the role of hyaluronic acid was investigated. Hyaluronan synthase 1, a critical enzyme in the synthetic pathway for hyaluronic acid, was knocked down in SN12L1 cells and in vitro experiments revealed inhibition of interstitial flow induced migration. Subsequently these cells were implanted in mouse kidneys and no distant metastases were detected. These findings suggest new therapeutic approaches to the treatment of kidney carcinoma metastasis.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"13 ","pages":"Article 100100"},"PeriodicalIF":0.0,"publicationDate":"2022-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/09/3c/main.PMC8789524.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39879600","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":"Multiscale modelling of the extracellular matrix","authors":"Hua Wong ,&nbsp;Jean-Marc Crowet ,&nbsp;Manuel Dauchez ,&nbsp;Sylvie Ricard-Blum ,&nbsp;Stéphanie Baud ,&nbsp;Nicolas Belloy","doi":"10.1016/j.mbplus.2021.100096","DOIUrl":"10.1016/j.mbplus.2021.100096","url":null,"abstract":"<div><p>The extracellular matrix is a complex three-dimensional network of molecules that provides cells with a complex microenvironment. The major constituents of the extracellular matrix such as collagen, elastin and associated proteins form supramolecular assemblies contributing to its physicochemical properties and organization. The structure of proteins and their supramolecular assemblies such as fibrils have been studied at the atomic level (e.g., by X-ray crystallography, Nuclear Magnetic Resonance and cryo-Electron Microscopy) or at the microscopic scale. However, many protein complexes are too large to be studied at the atomic level and too small to be studied by microscopy. Most extracellular matrix components fall into this intermediate scale, so-called the mesoscopic scale, preventing their detailed characterization. Simulation and modelling are some of the few powerful and promising approaches that can deepen our understanding of mesoscale systems. We have developed a set of modelling tools to study the self-organization of the extracellular matrix and large motion of macromolecules at the mesoscale level by taking advantage of the dynamics of articulated rigid bodies as a mean to study a larger range of motions at the cost of atomic resolution.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"13 ","pages":"Article 100096"},"PeriodicalIF":0.0,"publicationDate":"2022-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/d4/d5/main.PMC8763633.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39853728","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":"Coordinate roles for collagen VI and biglycan in regulating tendon collagen fibril structure and function","authors":"Ryan J. Leiphart ,&nbsp;Hai Pham ,&nbsp;Tyler Harvey ,&nbsp;Taishi Komori ,&nbsp;Tina M. Kilts ,&nbsp;Snehal S. Shetye ,&nbsp;Stephanie N. Weiss ,&nbsp;Sheila M. Adams ,&nbsp;David E. Birk ,&nbsp;Louis J. Soslowsky ,&nbsp;Marian F. Young","doi":"10.1016/j.mbplus.2021.100099","DOIUrl":"10.1016/j.mbplus.2021.100099","url":null,"abstract":"<div><p>Tendon is a vital musculoskeletal tissue that is prone to degeneration. Proper tendon maintenance requires complex interactions between extracellular matrix components that remain poorly understood. Collagen VI and biglycan are two matrix molecules that localize pericellularly within tendon and are critical regulators of tissue properties. While evidence suggests that collagen VI and biglycan interact within the tendon matrix, the relationship between the two molecules and its impact on tendon function remains unknown. We sought to elucidate potential coordinate roles of collagen VI and biglycan within tendon by defining tendon properties in knockout models of collagen VI, biglycan, or both molecules. We first demonstrated co-expression and co-localization of collagen VI and biglycan within the healing tendon, providing further evidence of cooperation between the two molecules during nascent tendon matrix formation. Deficiency in collagen VI and/or biglycan led to significant reductions in collagen fibril size and tendon mechanical properties. However, collagen VI-null tendons displayed larger reductions in fibril size and mechanics than seen in biglycan-null tendons. Interestingly, knockout of both molecules resulted in similar properties to collagen VI knockout alone. These results indicate distinct and non-additive roles for collagen VI and biglycan within tendon. This work provides better understanding of regulatory interactions between two critical tendon matrix molecules.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"13 ","pages":"Article 100099"},"PeriodicalIF":0.0,"publicationDate":"2022-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/a4/a2/main.PMC8749075.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9349536","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":"Uncovering mediators of collagen degradation in the tumor microenvironment","authors":"Marie-Louise Thorseth ,&nbsp;Marco Carretta ,&nbsp;Christina Jensen ,&nbsp;Kasper Mølgaard ,&nbsp;Henrik J. Jürgensen ,&nbsp;Lars H. Engelholm ,&nbsp;Niels Behrendt ,&nbsp;Nicholas Willumsen ,&nbsp;Daniel H. Madsen","doi":"10.1016/j.mbplus.2022.100101","DOIUrl":"10.1016/j.mbplus.2022.100101","url":null,"abstract":"<div><p>Increased remodeling of the extracellular matrix in malignant tumors has been shown to correlate with tumor aggressiveness and a poor prognosis. This remodeling involves degradation of the original extracellular matrix (ECM) and deposition of a new tumor-supporting ECM. The main constituent of the ECM is collagen and collagen turnover mainly occurs in a sequential manner, where initial proteolytic cleavage of the insoluble fibers is followed by cellular internalization of large well-defined collagen fragments for lysosomal degradation. However, despite extensive research in the field, a lack of consensus on which cell types within the tumor microenvironment express the involved proteases still exists. Furthermore, the relative contribution of different cell types to collagen internalization is not well-established. Here, we developed quantitative <em>ex vivo</em> collagen degradation assays and show that the proteases responsible for the initial collagen cleavage in two murine syngeneic tumor models are matrix metalloproteinases produced by cancer-associated fibroblasts and that collagen degradation fragments are endocytosed primarily by tumor-associated macrophages and cancer-associated fibroblasts from the tumor stroma. Using tumors from mannose receptor-deficient mice, we show that this receptor is essential for collagen-internalization by tumor-associated macrophages. Together, these findings identify the cell types responsible for the entire collagen degradation pathway, from initial cleavage to endocytosis of fragments for intracellular degradation.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"13 ","pages":"Article 100101"},"PeriodicalIF":0.0,"publicationDate":"2022-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/5d/5e/main.PMC8841889.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39948820","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":"PRIMUS: Comprehensive proteomics of mouse intervertebral discs that inform novel biology and relevance to human disease modelling","authors":"Mateusz Kudelko ,&nbsp;Peikai Chen ,&nbsp;Vivian Tam ,&nbsp;Ying Zhang ,&nbsp;Oi-Yin Kong ,&nbsp;Rakesh Sharma ,&nbsp;Tiffany Y.K. Au ,&nbsp;Michael Kai-Tsun To ,&nbsp;Kathryn S.E. Cheah ,&nbsp;Wilson C.W. Chan ,&nbsp;Danny Chan","doi":"10.1016/j.mbplus.2021.100082","DOIUrl":"10.1016/j.mbplus.2021.100082","url":null,"abstract":"<div><p>Mice are commonly used to study intervertebral disc (IVD) biology and related diseases such as IVD degeneration. Discs from both the lumbar and tail regions are used. However, little is known about compartmental characteristics in the different regions, nor their relevance to the human setting, where a functional IVD unit depends on a homeostatic proteome. Here, we address these major gaps through comprehensive proteomic profiling and in-depth analyses of 8-week-old healthy murine discs, followed by comparisons with human. Leveraging on a dataset of over 2,700 proteins from 31 proteomic profiles, we identified key molecular and cellular differences between disc compartments and spine levels, but not gender. The nucleus pulposus (NP) and annulus fibrosus (AF) compartments differ the most, both in matrisome and cellularity contents. Differences in the matrisome are consistent with the fibrous nature required for tensile strength in the AF and hydration property in the NP. Novel findings for the NP cells included an enrichment in cell junction proteins for cell–cell communication (Cdh2, Dsp and Gja1) and osmoregulation (Slc12a2 and Wnk1). In NP cells, we detected heterogeneity of vacuolar organelles; where about half have potential lysosomal function (Vamp3, Copb2, Lamp1/2, Lamtor1), some contain lipid droplets and others with undefined contents. The AF is enriched in proteins for the oxidative stress responses (Sod3 and Clu). Interestingly, mitochondrial proteins are elevated in the lumbar than tail IVDs that may reflect differences in metabolic requirement. Relative to the human, cellular and structural information are conserved for the AF. Even though the NP is more divergent between mouse and human, there are similarities at the level of cell biology. Further, common cross-species markers were identified for both NP (KRT8/19, CD109) and AF (COL12A1). Overall, mouse is a relevant model to study IVD biology, and an understanding of the limitation will facilitate research planning and data interpretation, maximizing the translation of research findings to human IVDs.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100082"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100082","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39324449","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":"Extended disorder at the cell surface: The conformational landscape of the ectodomains of syndecans","authors":"Frank Gondelaud ,&nbsp;Mathilde Bouakil ,&nbsp;Aurélien Le Fèvre ,&nbsp;Adriana Erica Miele ,&nbsp;Fabien Chirot ,&nbsp;Bertrand Duclos ,&nbsp;Adam Liwo ,&nbsp;Sylvie Ricard-Blum","doi":"10.1016/j.mbplus.2021.100081","DOIUrl":"10.1016/j.mbplus.2021.100081","url":null,"abstract":"<div><p>Syndecans are membrane proteoglycans regulating extracellular matrix assembly, cell adhesion and signaling. Their ectodomains can be shed from the cell surface, and act as paracrine and autocrine effectors or as competitors of full-length syndecans. We report the first biophysical characterization of the recombinant ectodomains of the four human syndecans using biophysical techniques, and show that they behave like flexible random-coil intrinsically disordered proteins, and adopt several conformation ensembles in solution. We have characterized their conformational landscapes using native mass spectrometry (MS) and ion-mobility MS, and demonstrated that the syndecan ectodomains explore the majority of their conformational landscape, from minor compact, globular-like, conformations to extended ones. We also report that the ectodomain of syndecan-4, corresponding to a natural isoform, is able to dimerize via a disulfide bond. We have generated a three-dimensional model of the C-terminus of this dimer, which supports the dimerization via a disulfide bond. Furthermore, we have mapped the NXIP adhesion motif of syndecans and their sequences involved in the formation of ternary complexes with integrins and growth factor receptors on the major conformations of their ectodomains, and shown that these sequences are not accessible in all the conformations, suggesting that only some of them are biologically active. Lastly, although the syndecan ectodomains have a far lower number of amino acid residues than their membrane partners, their intrinsic disorder and flexibility allow them to adopt extended conformations, which have roughly the same size as the cell surface receptors (e.g., integrins and growth factor receptors) they bind to.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100081"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100081","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39402756","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":"Collagen fibril assembly: New approaches to unanswered questions","authors":"Christopher K. Revell ,&nbsp;Oliver E. Jensen ,&nbsp;Tom Shearer ,&nbsp;Yinhui Lu ,&nbsp;David F. Holmes ,&nbsp;Karl E. Kadler","doi":"10.1016/j.mbplus.2021.100079","DOIUrl":"10.1016/j.mbplus.2021.100079","url":null,"abstract":"<div><p>Collagen fibrils are essential for metazoan life. They are the largest, most abundant, and most versatile protein polymers in animals, where they occur in the extracellular matrix to form the structural basis of tissues and organs. Collagen fibrils were first observed at the turn of the 20th century. During the last 40 years, the genes that encode the family of collagens have been identified, the structure of the collagen triple helix has been solved, the many enzymes involved in the post-translational modifications of collagens have been identified, mutations in the genes encoding collagen and collagen-associated proteins have been linked to heritable disorders, and changes in collagen levels have been associated with a wide range of diseases, including cancer. Yet despite extensive research, a full understanding of how cells assemble collagen fibrils remains elusive. Here, we review current models of collagen fibril self-assembly, and how cells might exert control over the self-assembly process to define the number, length and organisation of fibrils in tissues.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100079"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100079","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39303382","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":"Runx2 is required for hypertrophic chondrocyte mediated degradation of cartilage matrix during endochondral ossification","authors":"Harunur Rashid,&nbsp;Haiyan Chen,&nbsp;Amjad Javed","doi":"10.1016/j.mbplus.2021.100088","DOIUrl":"10.1016/j.mbplus.2021.100088","url":null,"abstract":"<div><p>The RUNX2 transcription factor is a key regulator for the development of cartilage and bone. Global or resting chondrocyte-specific deletion of the <em>Runx2</em> gene results in failure of chondrocyte hypertrophy, endochondral ossification, and perinatal lethality. The terminally mature hypertrophic chondrocyte regulates critical steps of endochondral ossification. Importantly, expression of the <em>Runx2</em> gene starts in the resting chondrocyte and increases progressively, reaching the maximum level in hypertrophic chondrocytes. However, the RUNX2 role after chondrocyte hypertrophy remains unknown. To answer this question, we deleted the <em>Runx2</em> gene specifically in hypertrophic chondrocytes using the Col10-Cre line. Mice lacking the <em>Runx2</em> gene in hypertrophic chondrocytes (<em>Runx2^HC/HC</em>) survive but exhibit limb dwarfism. Interestingly, the length of the hypertrophic chondrocyte zone is doubled in the growth plate of <em>Runx2^HC/HC</em> mice. Expression of pro-apoptotic <em>Bax</em> decreased significantly while anti-apoptotic <em>Bcl2</em> remains unchanged leading to a four-fold increase in the <em>Bcl2</em>/<em>Bax</em> ratio in mutant mice. In line with this, a significant reduction in apoptosis of <em>Runx2^HC/HC</em> hypertrophic chondrocyte is noted. A large amount of cartilage matrix is present in the long bones that extend toward the diaphyseal region of <em>Runx2^HC/HC</em> mice. This is not due to enhanced synthesis of the cartilage matrix as the expression of both collagen type 2 and aggrecan were comparable among <em>Runx2^HC/HC</em> and WT littermates. Our qPCR analysis demonstrates the increased amount of cartilage matrix is due to impaired expression of cartilage degrading enzymes such as metalloproteinase and aggrecanase as well as tissue inhibitor of metalloproteinases. Moreover, a significant decrease of TRAP positive chondroclasts was noted along the cartilage islands in <em>Runx2^HC/HC</em> mice. Consistently, qPCR data showed an 81% reduction in the <em>Rankl</em>/<em>Opg</em> ratio in <em>Runx2^HC/HC</em> littermates, which is inhibitory for chondroclast differentiation. Finally, we assess if increase cartilage matrix in <em>Runx2^HC/HC</em> mice serves as a template for bone and mineral deposition using micro-CT and Von Kossa. The mutant mice exhibit a significant increase in trabecular bone mass compared to littermates. In summary, our findings have uncovered a novel role of Runx2 in apoptosis of hypertrophic chondrocytes and degradation of cartilage matrix during endochondral ossification.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100088"},"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/01/53/main.PMC8586806.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39644967","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":"Structural studies of elastic fibre and microfibrillar proteins","authors":"Mukti Singh,&nbsp;Mark Becker,&nbsp;Alan R.F. Godwin,&nbsp;Clair Baldock","doi":"10.1016/j.mbplus.2021.100078","DOIUrl":"10.1016/j.mbplus.2021.100078","url":null,"abstract":"<div><p>Elastic tissues owe their functional properties to the composition of their extracellular matrices, particularly the range of extracellular, multidomain extensible elastic fibre and microfibrillar proteins. These proteins include elastin, fibrillin, latent TGFβ binding proteins (LTBPs) and collagens, where their biophysical and biochemical properties not only give the matrix structural integrity, but also play a vital role in the mechanisms that underlie tissue homeostasis. Thus far structural information regarding the structure and hierarchical assembly of these molecules has been challenging and the resolution has been limited due to post-translational modification and their multidomain nature leading to flexibility, which together result in conformational and structural heterogeneity. In this review, we describe some of the matrix proteins found in elastic fibres and the new emerging techniques that can shed light on their structure and dynamic properties.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100078"},"PeriodicalIF":0.0,"publicationDate":"2021-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://sci-hub-pdf.com/10.1016/j.mbplus.2021.100078","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39281140","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":"Protection and rebuilding of the endothelial glycocalyx in sepsis – Science or fiction?","authors":"Carolin Christina Drost,&nbsp;Alexandros Rovas,&nbsp;Philipp Kümpers","doi":"10.1016/j.mbplus.2021.100091","DOIUrl":"10.1016/j.mbplus.2021.100091","url":null,"abstract":"<div><p>The endothelial glycocalyx (eGC), a delicate carbohydrate-rich structure lining the luminal surface of the vascular endothelium, is vital for maintenance of microvascular homeostasis. In sepsis, damage of the eGC triggers the development of vascular hyperpermeability with consecutive edema formation and organ failure. While there is evidence that protection or rebuilding of the eGC might counteract sepsis-induced vascular leakage and improve outcome, approved therapeutics are not yet available. This narrative review aims to outline possible therapeutic strategies to ameliorate organ dysfunction caused by eGC impairment.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"12 ","pages":"Article 100091"},"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/9a/65/main.PMC8633034.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"39790977","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}