Matrix Biology Plus最新文献

{"title":"The glycocalyx: Pathobiology and repair","authors":"Jillian R. Richter , Ralph D. Sanderson","doi":"10.1016/j.mbplus.2023.100128","DOIUrl":"10.1016/j.mbplus.2023.100128","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"17 ","pages":"Article 100128"},"PeriodicalIF":0.0,"publicationDate":"2023-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f6/fa/main.PMC9923180.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10871691","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":"Fibrosis resolution in the mouse liver: Role of Mmp12 and potential role of calpain 1/2","authors":"Toshifumi Sato ,&nbsp;Kimberly Z. Head ,&nbsp;Jiang Li ,&nbsp;Christine E. Dolin ,&nbsp;Daniel Wilkey ,&nbsp;Nolan Skirtich ,&nbsp;Katelyn Smith ,&nbsp;Dylan D. McCreary ,&nbsp;Sylvia Liu ,&nbsp;Juliane I. Beier ,&nbsp;Aatur D. Singhi ,&nbsp;Ryan M. McEnaney ,&nbsp;Michael L. Merchant ,&nbsp;Gavin E. Arteel","doi":"10.1016/j.mbplus.2022.100127","DOIUrl":"10.1016/j.mbplus.2022.100127","url":null,"abstract":"<div><p>Although most work has focused on resolution of collagen ECM, fibrosis resolution involves changes to several ECM proteins. The purpose of the current study was twofold: 1) to examine the role of MMP12 and elastin; and 2) to investigate the changes in degraded proteins in plasma (i.e., the “degradome”) in a preclinical model of fibrosis resolution. Fibrosis was induced by 4 weeks carbon tetrachloride (CCl₄) exposure, and recovery was monitored for an additional 4 weeks. Some mice were treated with daily MMP12 inhibitor (MMP408) during the resolution phase. Liver injury and fibrosis was monitored by clinical chemistry, histology and gene expression. The release of degraded ECM peptides in the plasma was analyzed using by 1D-LC-MS/MS, coupled with PEAKS Studio (v10) peptide identification. Hepatic fibrosis and liver injury rapidly resolved in this mouse model. However, some collagen fibrils were still present 28d after cessation of CCl₄. Despite this persistent collagen presence, expression of canonical markers of fibrosis were also normalized. The inhibition of MMP12 dramatically delayed fibrosis resolution under these conditions. LC-MS/MS analysis identified that several proteins were being degraded even at late stages of fibrosis resolution. Calpains 1/2 were identified as potential new proteases involved in fibrosis resolution. CONCLUSION. The results of this study indicate that remodeling of the liver during recovery from fibrosis is a complex and highly coordinated process that extends well beyond the degradation of the collagenous scar. These results also indicate that analysis of the plasma degradome may yield new insight into the mechanisms of fibrosis recovery, and by extension, new “theragnostic” targets. Lastly, a novel potential role for calpain activation in the degradation and turnover of proteins was identified.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"17 ","pages":"Article 100127"},"PeriodicalIF":0.0,"publicationDate":"2023-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/cf/aa/main.PMC9826883.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9796941","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 molecule inhibitors of mammalian glycosylation","authors":"Karim Almahayni ,&nbsp;Malte Spiekermann ,&nbsp;Antonio Fiore ,&nbsp;Guoqiang Yu ,&nbsp;Kayvon Pedram ,&nbsp;Leonhard Möckl","doi":"10.1016/j.mbplus.2022.100108","DOIUrl":"10.1016/j.mbplus.2022.100108","url":null,"abstract":"<div><p>Glycans are one of the fundamental biopolymers encountered in living systems. Compared to polynucleotide and polypeptide biosynthesis, polysaccharide biosynthesis is a uniquely combinatorial process to which interdependent enzymes with seemingly broad specificities contribute. The resulting intracellular cell surface, and secreted glycans play key roles in health and disease, from embryogenesis to cancer progression. The study and modulation of glycans in cell and organismal biology is aided by small molecule inhibitors of the enzymes involved in glycan biosynthesis. In this review, we survey the arsenal of currently available inhibitors, focusing on agents which have been independently validated in diverse systems. We highlight the utility of these inhibitors and drawbacks to their use, emphasizing the need for innovation for basic research as well as for therapeutic applications.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100108"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/38/f7/main.PMC9713294.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10536198","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":"Modelling stromal compartments to recapitulate the ameloblastoma tumour microenvironment","authors":"Deniz Bakkalci ,&nbsp;Amir Zaki Abdullah Zubir ,&nbsp;Syed Ali Khurram ,&nbsp;Judith Pape ,&nbsp;Kristiina Heikinheimo ,&nbsp;Stefano Fedele ,&nbsp;Umber Cheema","doi":"10.1016/j.mbplus.2022.100125","DOIUrl":"10.1016/j.mbplus.2022.100125","url":null,"abstract":"<div><p>Tumour development and progression is dependent upon tumour cell interaction with the tissue stroma. Bioengineering the tumour-stroma microenvironment (TME) into 3D biomimetic models is crucial to gain insight into tumour cell development and progression pathways and identify therapeutic targets. Ameloblastoma is a benign but locally aggressive epithelial odontogenic neoplasm that mainly occurs in the jawbone and can cause significant morbidity and sometimes death. The molecular mechanisms for ameloblastoma progression are poorly understood. A spatial model recapitulating the tumour and stroma was engineered to show that without a relevant stromal population, tumour invasion is quantitatively decreased. Where a relevant stroma was engineered in dense collagen populated by gingival fibroblasts, enhanced receptor activator of nuclear factor kappa-B ligand (RANKL) expression was observed and histopathological properties, including ameloblastoma tumour islands, developed and were quantified. Using human osteoblasts (bone stroma) further enhanced the biomimicry of ameloblastoma histopathological phenotypes. This work demonstrates the importance of the two key stromal populations, osteoblasts, and gingival fibroblasts, for accurate 3D biomimetic ameloblastoma modelling.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100125"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9703037/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40518763","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":"Lysyl oxidase-like 1 deficiency alters ultrastructural and biomechanical properties of the peripapillary sclera in mice","authors":"Lauren K. Wareham ,&nbsp;John Kuchtey ,&nbsp;Hang-Jing Wu ,&nbsp;Evan Krystofiak ,&nbsp;Yusheng Wu ,&nbsp;Cynthia A. Reinhart-King ,&nbsp;Rachel W. Kuchtey","doi":"10.1016/j.mbplus.2022.100120","DOIUrl":"10.1016/j.mbplus.2022.100120","url":null,"abstract":"<div><p>Lysyl oxidase-like 1 encoded by the <em>LOXL1</em> gene is a member of the lysyl oxidase family of enzymes that are important in the maintenance of extracellular matrix (ECM)-rich tissue. LOXL1 is important for proper elastic fiber formation and mice lacking LOXL1 (<em>Loxl1^−/−</em>) exhibit systemic elastic fiber disorders, such as pelvic organ prolapse, a phenotype associated with exfoliation syndrome (XFS) in humans. Patients with XFS have a significant risk of developing exfoliation glaucoma (XFG), a severe form of glaucoma, which is a neurodegenerative condition leading to irreversible blindness if not detected and treated in a timely fashion. Although <em>Loxl1^−/−</em> mice have been used extensively to investigate mechanisms of pelvic organ prolapse, studies of eyes in those mice are limited and some showed inconsistent ocular phenotypes. In this study we demonstrate that <em>Loxl1^−/−</em> mice have significant anterior segment biometric abnormalities which recapitulate some human XFS features. We then focused on the peripapillary sclera (PPS), a critical structure for maintaining optic nerve health. We discovered quantitative and qualitive changes in ultrastructure of PPS, such as reduced elastic fibers, enlarged collagen fibrils, and transformed collagen lamella organization detected by transmission electron microscopy (TEM). Importantly, these changes corelate with altered tissue biomechanics detected by Atomic Force Microscopy (AFM) of PPS in mice. Together, our results support a crucial role for LOXL1 in ocular tissue structure and biomechanics, and <em>Loxl1^−/−</em> mice could be a valuable resource for understanding the role of scleral tissue biomechanics in ocular disease.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100120"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/dc/14/main.PMC9436796.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40350325","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":"Erratum to “Small molecule inhibitors of mammalian glycosylation” [Matrix Biol. Plus 16C (2022) 100108]","authors":"Karim Almahayni ,&nbsp;Malte Spiekermann ,&nbsp;Antonio Fiore ,&nbsp;Guoqiang Yu ,&nbsp;Kayvon Pedram ,&nbsp;Leonhard Möckl","doi":"10.1016/j.mbplus.2022.100126","DOIUrl":"10.1016/j.mbplus.2022.100126","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100126"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9805958/pdf/main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"10847356","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":"Targeted conditional collagen XII deletion alters tendon function","authors":"Ashley Fung ,&nbsp;Mei Sun ,&nbsp;Louis J. Soslowsky ,&nbsp;David E. Birk","doi":"10.1016/j.mbplus.2022.100123","DOIUrl":"10.1016/j.mbplus.2022.100123","url":null,"abstract":"<div><p>Collagen XII is a fibril-associated collagen with interrupted triple helices (FACIT). This non-fibrillar collagen is a homotrimer composed of three α1(XII) chains assembled into a collagenous molecule with a C terminal collagenous domain and a large N terminal non-collagenous domain. During tendon development and growth, collagen XII is broadly expressed throughout the extracellular matrix and enriched pericellularly around tenocytes. Tendons in a global <em>Col12a1</em>^<em>-/-</em> knockout model demonstrated disrupted fibril and fiber structure and disordered tenocyte organization, highlighting the critical regulatory roles of collagen XII in determining tendon structure and function. However, muscle and bone also are affected in the collagen XII knockout model. Therefore, secondary effects on tendon due to involvement of bone and muscle may occur in the global knockout. The global knockout does not allow the definition of intrinsic mechanisms involving collagen XII in tendon versus extrinsic roles involving muscle and bone. To address this limitation, we created and characterized a conditional <em>Col12a1</em>-null mouse model to permit the spatial and temporal manipulation of <em>Col12a1</em> expression. Collagen XII knockout was targeted to tendons by breeding conditional <em>Col12a1</em>^{<em>flox/flox</em>} mice with Scleraxis-Cre (<em>Scx-</em>Cre) mice to yield a tendon-specific <em>Col12a1</em>-null mouse line, <em>Col12a1</em>^{<em>Δten/Δten</em>}. Both mRNA and protein expression in <em>Col12a1</em>^{<em>Δten/Δten</em>} mice decreased to near baseline levels in flexor digitorum longus tendons (FDL). Collagen XII immuno-localization revealed an absence of reactivity in the tendon proper, but there was reactivity in the cells of the surrounding peritenon. This supports a targeted knockout in tenocytes while peritenon cells from a non-tendon lineage were not targeted and retained collagen XII expression. The tendon-targeted, <em>Col12a1</em>^{<em>Δten/Δten</em>} <!-->mice had significantly reduced forelimb grip strength, altered gait and a significant decrease in biomechanical properties. While the observed decrease in tendon modulus suggests that differences in tendon material properties in the absence of <em>Col12a1</em> expression underlie the functional deficiencies. Together, these findings suggest an intrinsic role for collagen XII critical for development of a functional tendon.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100123"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/56/8d/main.PMC9597098.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"9366343","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":"Extracellular Matrix Profiling and Disease Modelling in Engineered Vascular Smooth Muscle Cell Tissues","authors":"Ella Reed ,&nbsp;Adam Fellows ,&nbsp;Ruifang Lu ,&nbsp;Marieke Rienks ,&nbsp;Lukas Schmidt ,&nbsp;Xiaoke Yin ,&nbsp;Elisa Duregotti ,&nbsp;Mona Brandt ,&nbsp;Susanne Krasemann ,&nbsp;Kristin Hartmann ,&nbsp;Javier Barallobre-Barreiro ,&nbsp;Owen Addison ,&nbsp;Friederike Cuello ,&nbsp;Arne Hansen ,&nbsp;Manuel Mayr","doi":"10.1016/j.mbplus.2022.100122","DOIUrl":"10.1016/j.mbplus.2022.100122","url":null,"abstract":"<div><p>Aortic smooth muscle cells (SMCs) have an intrinsic role in regulating vessel homeostasis and pathological remodelling. In two-dimensional (2D) cell culture formats, however, SMCs are not embedded in their physiological extracellular matrix (ECM) environment. To overcome the limitations of conventional 2D SMC cultures, we established a 3D <em>in vitro</em> model of engineered vascular smooth muscle cell tissues (EVTs). EVTs were casted from primary murine aortic SMCs by suspending a SMC-fibrin master mix between two flexible silicon-posts at day 0 before prolonged culture up to 14 days. Immunohistochemical analysis of EVT longitudinal sections demonstrated that SMCs were aligned, viable and secretory. Mass spectrometry-based proteomics analysis of murine EVT lysates was performed and identified 135 matrisome proteins. Proteoglycans, including the large aggregating proteoglycan versican, accumulated within EVTs by day 7 of culture. This was followed by the deposition of collagens, elastin-binding proteins and matrix regulators up to day 14 of culture. In contrast to 2D SMC controls, accumulation of versican occurred in parallel to an increase in versikine, a cleavage product mediated by proteases of the A Disintegrin and Metalloproteinase with Thrombospondin motifs (ADAMTS) family. Next, we tested the response of EVTs to stimulation with transforming growth factor beta-1 (TGFβ-1). EVTs contracted in response to TGFβ-1 stimulation with altered ECM composition. In contrast, treatment with the pharmacological activin-like kinase inhibitor (ALKi) SB 431542 suppressed ECM secretion. As a disease stimulus, we performed calcification assays. The ECM acts as a nidus for calcium phosphate deposition in the arterial wall. We compared the onset and extent of calcification in EVTs and 2D SMCs cultured under high calcium and phosphate conditions for 7 days. Calcified EVTs displayed increased tissue stiffness by up to 30 % compared to non-calcified controls. Unlike the rapid calcification of SMCs in 2D cultures, EVTs sustained expression of the calcification inhibitor matrix Gla protein and allowed for better discrimination of the calcification propensity between independent biological replicates. In summary, EVTs are an intuitive and versatile model to investigate ECM synthesis and turnover by SMCs in a 3D environment. Unlike conventional 2D cultures, EVTs provide a more relevant pathophysiological model for retention of the nascent ECM produced by SMCs.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100122"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC9526190/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33487604","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":"Alterations in heparan sulfate proteoglycan synthesis and sulfation and the impact on vascular endothelial function","authors":"Danielle Pretorius ,&nbsp;Robert P. Richter ,&nbsp;Tanya Anand ,&nbsp;Jessica C. Cardenas ,&nbsp;Jillian R. Richter","doi":"10.1016/j.mbplus.2022.100121","DOIUrl":"10.1016/j.mbplus.2022.100121","url":null,"abstract":"<div><p>The glycocalyx attached to the apical surface of vascular endothelial cells is a rich network of proteoglycans, glycosaminoglycans, and glycoproteins with instrumental roles in vascular homeostasis. Given their molecular complexity and ability to interact with the intra- and extracellular environment, heparan sulfate proteoglycans uniquely contribute to the glycocalyx’s role in regulating endothelial permeability, mechanosignaling, and ligand recognition by cognate cell surface receptors. Much attention has recently been devoted to the enzymatic shedding of heparan sulfate proteoglycans from the endothelial glycocalyx and its impact on vascular function. However, other molecular modifications to heparan sulfate proteoglycans are possible and may have equal or complementary clinical significance. In this narrative review, we focus on putative mechanisms driving non-proteolytic changes in heparan sulfate proteoglycan expression and alterations in the sulfation of heparan sulfate side chains within the endothelial glycocalyx. We then discuss how these specific changes to the endothelial glycocalyx impact endothelial cell function and highlight therapeutic strategies to target or potentially reverse these pathologic changes.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100121"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/53/3a/main.PMC9494232.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"33484981","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":"Integrin α3 negative podocytes: A gene expression study","authors":"L.H. Frommherz ,&nbsp;S.B. Sayar ,&nbsp;Y. Wang ,&nbsp;L.K. Trefzer ,&nbsp;Y. He ,&nbsp;J. Leppert ,&nbsp;P. Eßer ,&nbsp;C. Has","doi":"10.1016/j.mbplus.2022.100119","DOIUrl":"10.1016/j.mbplus.2022.100119","url":null,"abstract":"<div><p>Integrin α3β1 is a cell adhesion receptor widely expressed in epithelial cells. Pathogenic variants in the gene encoding the integrin α3 subunit <em>ITGA3</em> lead to a syndrome including interstitial lung disease, nephrotic syndrome, and epidermolysis bullosa (ILNEB). Renal involvement mainly consists of glomerular disease caused by loss of adhesion between podocytes and the glomerular basement membrane.</p><p>The aim of this study was to characterize the impact of loss of integrin α3 on human podocytes.</p><p><em>ITGA3</em> was stably knocked-out in the human podocyte cell line AB8/13, designated as Podo^A3−, and in human proximal tubule epithelial cell line HK2 using the targeted genome editing technique CRISPR/Cas9. Cell clones were characterized by Sanger sequencing, quantitative PCR, Western Blot and immunofluorescence staining. RNASeq of integrin α3 negative cells and controls was performed to identify differential gene expression patterns.</p><p>Differentiated Podo^A3− did not substantially change morphology and adhesion under standard culture conditions, but displayed significantly reduced spreading and adhesion when seed on laminin 511 in serum free medium. Gene expression studies demonstrated a distinct dysregulation of the adhesion network with downregulation of most integrin α3 interaction partners. In agreement with this, biological processes such as “extracellular matrix organization” and “cell differentiation” as well as KEGG pathways such as “ECM-receptor interaction”, “focal adhesion” and the “PI3K-Akt signaling pathway” were significantly downregulated in human podocytes lacking the integrin α3 subunit.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"16 ","pages":"Article 100119"},"PeriodicalIF":0.0,"publicationDate":"2022-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://ftp.ncbi.nlm.nih.gov/pub/pmc/oa_pdf/f8/d4/main.PMC9429797.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"40350324","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}