Matrix Biology Plus最新文献

{"title":"Binding requirements for latent transforming growth factor Beta2 activation","authors":"Nalani Sachan ,&nbsp;Colin K.L. Phoon ,&nbsp;Lei Bu ,&nbsp;Lior Zilberberg ,&nbsp;Jasimuddin Ahamed ,&nbsp;Daniel B. Rifkin","doi":"10.1016/j.mbplus.2024.100149","DOIUrl":"10.1016/j.mbplus.2024.100149","url":null,"abstract":"<div><p>Although the mechanism for activation of latent TGFβ1 and TGFβ3 is understood to involve the binding of the TGFβ propeptide (LAP) to both an integrin and an insoluble substrate, the activation of latent TGFβ2 has been unclear because the TGFβ2 LAP does not have the classical integrin binding sequence found in the other two TGFβ isoform LAPs. To assess the potential requirement for covalent linkage with a matrix or cell surface protein for the activation of latent TGFβ2, we generated mice in which the TGFβ2 Cys residue predicted to be involved in binding was mutated to Ser (<em>Tgfb2^C24S</em>). We reasoned that, if covalent interaction with a second molecule is required for latent TGFβ2 activation, mutant mice should display a <em>Tgfb2</em> null (<em>Tgfb2^−/−</em>)-like phenotype. <em>Tgfb2^C24S</em> mice closely phenocopy <em>Tgfb2^−/−</em> mice with death in utero between E18 and P1 and with congenital heart and kidney defects similar to those described for <em>Tgfb2^−/−</em> mice. The mutant latent TGFβ2 is secreted at levels similar to WT, yet TGFβ signaling monitored as nuclear pSmad2 is suppressed. We conclude that, like latent TGFβ1, latent TGFβ2 activation requires binding to an immobilized matrix or plasma membrane molecule.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"22 ","pages":"Article 100149"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028524000097/pdfft?md5=9d9845444985c386c38f833f6bf3b4c3&pid=1-s2.0-S2590028524000097-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141037843","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 stiffness mediates insulin secretion in pancreatic islets via mechanosensitive Piezo1 channel regulated Ca2+ dynamics","authors":"Chelsea G. Johansen ,&nbsp;Keifer Holcomb ,&nbsp;Amit Sela ,&nbsp;Stephanie Morrall ,&nbsp;Daewon Park ,&nbsp;Nikki L. Farnsworth","doi":"10.1016/j.mbplus.2024.100148","DOIUrl":"10.1016/j.mbplus.2024.100148","url":null,"abstract":"<div><p>The pancreatic islet is surrounded by ECM that provides both biochemical and mechanical cues to the islet β-cell to regulate cell survival and insulin secretion. Changes in ECM composition and mechanical properties drive β-cell dysfunction in many pancreatic diseases. While several studies have characterized changes in islet insulin secretion with changes in substrate stiffness, little is known about the mechanotransduction signaling driving altered islet function in response to mechanical cues. We hypothesized that increasing matrix stiffness will lead to insulin secretion dysfunction by opening the mechanosensitive ion channel Piezo1 and disrupting intracellular Ca²⁺ dynamics in mouse and human islets. To test our hypothesis, mouse and human cadaveric islets were encapsulated in a biomimetic reverse thermal gel (RTG) scaffold with tailorable stiffness that allows formation of islet focal adhesions with the scaffold and activation of Piezo1 in 3D. Our results indicate that increased scaffold stiffness causes insulin secretion dysfunction mediated by increases in Ca²⁺ influx and altered Ca²⁺ dynamics via opening of the mechanosensitive Piezo1 channel. Additionally, inhibition of Piezo1 rescued glucose-stimulated insulin secretion (GSIS) in islets in stiff scaffolds. Overall, our results emphasize the role mechanical properties of the islet microenvironment plays in regulating function. It also supports further investigation into the modulation of Piezo1 channel activity to restore islet function in diseases like type 2 diabetes (T2D) and pancreatic cancer where fibrosis of the <em>peri</em>-islet ECM leads to increased tissue stiffness and islet dysfunction.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"22 ","pages":"Article 100148"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028524000085/pdfft?md5=d2836de4464c289026850dc0eaad9f95&pid=1-s2.0-S2590028524000085-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141044007","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":"ColPTMScape: An open access knowledge base for tissue-specific collagen PTM maps","authors":"Ashutosh Joshi ,&nbsp;Ayush Nigam ,&nbsp;Lalit Narayan Mudgal ,&nbsp;Bhaskar Mondal ,&nbsp;Trayambak Basak","doi":"10.1016/j.mbplus.2024.100144","DOIUrl":"https://doi.org/10.1016/j.mbplus.2024.100144","url":null,"abstract":"<div><p>Collagen is a key component of the extracellular matrix (ECM). In the remodeling of ECM, a remarkable variation in collagen post-translational modifications (PTMs) occurs. This makes collagen a potential target for understanding extracellular matrix remodeling during pathological conditions. Over the years, scientists have gathered a huge amount of data about collagen PTM during extracellular matrix remodeling. To make such information easily accessible in a consolidated space, we have developed ColPTMScape (<span>https://colptmscape.iitmandi.ac.in/</span><svg><path></path></svg>), a dedicated knowledge base for collagen PTMs. The identified site-specific PTMs, quantitated PTM sites, and PTM maps of collagen chains are deliverables to the scientific community, especially to matrix biologists. Through this knowledge base, users can easily gain information related to the difference in the collagen PTMs across different tissues in different organisms.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"22 ","pages":"Article 100144"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028524000048/pdfft?md5=ee9db8c435eaf7dbec4ec7529118646f&pid=1-s2.0-S2590028524000048-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"140041796","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":"Corrigendum to “A preliminary study into the emergence of tendon microstructure during postnatal development” [Matrix Biol. Plus 21 (2024) 100142]","authors":"Helena Raymond-Hayling ,&nbsp;Yinhui Lu ,&nbsp;Richa Garva ,&nbsp;Tom Shearer ,&nbsp;Karl E. Kadler","doi":"10.1016/j.mbplus.2024.100147","DOIUrl":"10.1016/j.mbplus.2024.100147","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"22 ","pages":"Article 100147"},"PeriodicalIF":0.0,"publicationDate":"2024-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028524000073/pdfft?md5=a2165a3107a9bf148e6b5e909fe703d0&pid=1-s2.0-S2590028524000073-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"141035022","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":"A preliminary study into the emergence of tendon microstructure during postnatal development","authors":"Helena Raymond-Hayling ,&nbsp;Yinhui Lu ,&nbsp;Tom Shearer ,&nbsp;Karl Kadler","doi":"10.1016/j.mbplus.2024.100142","DOIUrl":"10.1016/j.mbplus.2024.100142","url":null,"abstract":"<div><p>Tendons maintain mechanical function throughout postnatal development whilst undergoing significant microstructural changes. We present a study of postnatal tendon growth and characterise the major changes in collagen fibril architecture in mouse tail tendon from birth to eight weeks by analysing the geometries of cross-sectional transmission electron microscopy images. This study finds that a bimodal distribution of fibril diameters emerges from a unimodal distribution of narrow fibrils as early as the eighth day postnatal, and three distinct fibril populations are visible at around 14 days. The tendons in this study do not show evidence of precise hexagonal packing, even at birth, and the spaces between the fibrils remain constant throughout development. The fibril number in the tissue stabilises around day 28, and the fibril area fraction stabilises around day 26. This study gives coarse-grained insight into the transition periods in early tendon development.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"21 ","pages":"Article 100142"},"PeriodicalIF":0.0,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028524000024/pdfft?md5=45dd56b1c29032ce3e1911900a9f3479&pid=1-s2.0-S2590028524000024-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139637217","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":"Designing collagens to shed light on the multi-scale structure–function mapping of matrix disorders","authors":"Sonal Gahlawat ,&nbsp;Vikas Nanda ,&nbsp;David I. Shreiber","doi":"10.1016/j.mbplus.2023.100139","DOIUrl":"10.1016/j.mbplus.2023.100139","url":null,"abstract":"<div><p>Collagens are the most abundant structural proteins in the extracellular matrix of animals and play crucial roles in maintaining the structural integrity and mechanical properties of tissues and organs while mediating important biological processes. Fibrillar collagens have a unique triple helix structure with a characteristic repeating sequence of (Gly-X-Y)_n. Variations within the repetitive sequence can cause misfolding of the triple helix, resulting in heritable connective tissue disorders. The most common variations are single-point missense mutations that lead to the substitution of a glycine residue with a bulkier amino acid (Gly → X). In this review, we will first discuss the importance of collagen’s triple helix structure and how single Gly substitutions can impact its folding, structure, secretion, assembly into higher-order structures, and biological functions. We will review the role of “designer collagens,” i.e., synthetic collagen-mimetic peptides and recombinant bacterial collagen as model systems to include Gly → X substitutions observed in collagen disorders and investigate their impact on structure and function utilizing <em>in vitro</em> studies. Lastly, we will explore how computational modeling of collagen peptides, especially molecular and steered molecular dynamics, has been instrumental in probing the effects of Gly substitutions on structure, receptor binding, and mechanical stability across multiple length scales.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"21 ","pages":"Article 100139"},"PeriodicalIF":0.0,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028523000121/pdfft?md5=f665a8dedce3173e618017d91ffbebfd&pid=1-s2.0-S2590028523000121-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139017085","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":"Proteomic analysis of the extracellular matrix of human atherosclerotic plaques shows marked changes between plaque types","authors":"Lasse G. Lorentzen ,&nbsp;Karin Yeung ,&nbsp;Nikolaj Eldrup ,&nbsp;Jonas P. Eiberg ,&nbsp;Henrik H. Sillesen ,&nbsp;Michael J. Davies","doi":"10.1016/j.mbplus.2024.100141","DOIUrl":"10.1016/j.mbplus.2024.100141","url":null,"abstract":"<div><p>Cardiovascular disease is the leading cause of death, with atherosclerosis the major underlying cause. While often asymptomatic for decades, atherosclerotic plaque destabilization and rupture can arise suddenly and cause acute arterial occlusion or peripheral embolization resulting in myocardial infarction, stroke and lower limb ischaemia. As extracellular matrix (ECM) remodelling is associated with plaque instability, we hypothesized that the ECM composition would differ between plaques. We analyzed atherosclerotic plaques obtained from 21 patients who underwent carotid surgery following recent symptomatic carotid artery stenosis. Plaques were solubilized using a new efficient, single-step approach. Solubilized proteins were digested to peptides, and analyzed by liquid chromatography-mass spectrometry using data-independent acquisition. Identification and quantification of 4498 plaque proteins was achieved, including 354 ECM proteins, with unprecedented coverage and high reproducibility. Multidimensional scaling analysis and hierarchical clustering indicate two distinct clusters, which correlate with macroscopic plaque morphology (soft/unstable versus hard/stable), ultrasound classification (echolucent versus echogenic) and the presence of hemorrhage/ulceration. We identified 714 proteins with differential abundances between these groups. Soft/unstable plaques were enriched in proteins involved in inflammation, ECM remodelling, and protein degradation (e.g. matrix metalloproteinases, cathepsins). In contrast, hard/stable plaques contained higher levels of ECM structural proteins (e.g. collagens, versican, nidogens, biglycan, lumican, proteoglycan 4, mineralization proteins). These data indicate that a single-step proteomics method can provide unique mechanistic insights into ECM remodelling and inflammatory mechanisms within plaques that correlate with clinical parameters, and help rationalize plaque destabilization. These data also provide an approach towards identifying biomarkers for individualized risk profiling of atherosclerosis.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"21 ","pages":"Article 100141"},"PeriodicalIF":0.0,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028524000012/pdfft?md5=0cf5c67aa0b3306c6014e70a8011d47f&pid=1-s2.0-S2590028524000012-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139456080","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":"Characterization of an in vitro engineered ligament model","authors":"Alec M. Avey ,&nbsp;Omar Valdez ,&nbsp;Keith Baar","doi":"10.1016/j.mbplus.2023.100140","DOIUrl":"https://doi.org/10.1016/j.mbplus.2023.100140","url":null,"abstract":"<div><p><em>In vivo</em> tendon and ligament research can be limited by the difficultly of obtaining tissue samples that can be biochemically analyzed. In this study, we characterize the most widely used <em>in vitro</em> engineered ligament model. Despite previous works suggesting multiple passages change gene expression in 2D primary tenocytes, we found no relationship between passage number and expression of classical tendon fibroblast markers across different biological donors. When engineered into 3D ligaments, there was an increase in maximal tensile load between 7 and 14 days in culture, that corresponded with an increase in collagen content. By contrast, percent collagen increased logarithmically from Day 7 to Day 14, and this was similar to the increase in the modulus of the tissue. Importantly, there was no relationship between passage number and mechanical function or collagen content in the two independent donors tested. These results suggest that the model develops quickly and is reliable across differing passage numbers. This provides the field with the ability to 1) consistently determine functional changes of interventions out to passage number 10; and 2) to time interventions to the appropriate developmental stage: developing/regenerating (Day 7) or mature (Day 14) tissue.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"21 ","pages":"Article 100140"},"PeriodicalIF":0.0,"publicationDate":"2024-02-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028523000133/pdfft?md5=b6d704769d86e1e0c11806088a61213c&pid=1-s2.0-S2590028523000133-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"139100373","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":"Urokinase-type plasminogen activator (uPA) regulates invasion and matrix remodelling in colorectal cancer","authors":"Auxtine Micalet ,&nbsp;Luke J. Tappouni ,&nbsp;Katarzyna Peszko ,&nbsp;Despoina Karagianni ,&nbsp;Ashley Lam ,&nbsp;John R. Counsell ,&nbsp;Sergio A. Quezada ,&nbsp;Emad Moeendarbary ,&nbsp;Umber Cheema","doi":"10.1016/j.mbplus.2023.100137","DOIUrl":"https://doi.org/10.1016/j.mbplus.2023.100137","url":null,"abstract":"<div><h3>Background</h3><p>Cancer cells remodel their local physical environment through processes of matrix reorganisation, deposition, stiffening and degradation. Urokinase-type plasminogen activator (uPA), which is encoded by the <em>PLAU</em> gene, is an extracellular proteolytic enzyme known to be involved in cancer progression and tumour microenvironment (TME) remodelling. Perturbing uPA therefore has a strong potential as a mechano-based cancer therapy. This work is a bioengineering investigation to validate whether 1) uPA is involved in matrix degradation and 2) preventing matrix degradation by targeting uPA can reduce cancer cell invasion and metastasis.</p></div><div><h3>Methods</h3><p>To this aim, we used an engineered 3D <em>in vitro</em> model, termed the tumouroid, that appropriately mimics the tumour’s native biophysical environment (3 kPa). A CRISPR-Cas9 mediated uPA knockout was performed to introduce a loss of function mutation in the gene coding sequence. Subsequently, to validate the translational potential of blocking uPA action, we tested a pharmacological inhibitor, UK-371,801. The changes in matrix stiffness were measured by atomic force microscopy (AFM). Invasion was quantified using images of the tumouroid, obtained after 21 days of culture.</p></div><div><h3>Results</h3><p>We showed that uPA is highly expressed in invasive breast and colorectal cancers, and these invasive cancer cells locally degrade their TME. <em>PLAU</em> (uPA) gene knock-out (KO) completely stopped matrix remodelling and significantly reduced cancer invasion. Many invasive cancer gene markers were also downregulated in the <em>PLAU</em> KO tumouroids. Pharmacological inhibition of uPA showed similarly promising results, where matrix degradation was reduced and so was the cancer invasion.</p></div><div><h3>Conclusion</h3><p>This work supports the role of uPA in matrix degradation. It demonstrates that the invasion of cancer cells was significantly reduced when enzymatic breakdown of the TME matrix was prevented. Collectively, this provides strong evidence of the effectiveness of targeting uPA as a mechano-based cancer therapy.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"19 ","pages":"Article 100137"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028523000108/pdfft?md5=47553b59807ff2b369969b99375d6266&pid=1-s2.0-S2590028523000108-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138412731","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":"Omentum-derived matrix enables the study of metastatic ovarian cancer and stromal cell functions in a physiologically relevant environment","authors":"Lisa J. Neilson ,&nbsp;Douglas Cartwright ,&nbsp;Maija Risteli ,&nbsp;Elina M. Jokinen ,&nbsp;Lynn McGarry ,&nbsp;Toni Sandvik ,&nbsp;Konstantina Nikolatou ,&nbsp;Kelly Hodge ,&nbsp;Samuel Atkinson ,&nbsp;Maria Vias ,&nbsp;Emily J. Kay ,&nbsp;James D. Brenton ,&nbsp;Leo M. Carlin ,&nbsp;David M. Bryant ,&nbsp;Tuula Salo ,&nbsp;Sara Zanivan","doi":"10.1016/j.mbplus.2023.100136","DOIUrl":"https://doi.org/10.1016/j.mbplus.2023.100136","url":null,"abstract":"<div><p>High-grade serous (HGS) ovarian cancer is the most lethal gynaecological disease in the world and metastases is a major cause. The omentum is the preferential metastatic site in HGS ovarian cancer patients and <em>in vitro</em> models that recapitulate the original environment of this organ at cellular and molecular level are being developed to study basic mechanisms that underpin this disease. The tumour extracellular matrix (ECM) plays active roles in HGS ovarian cancer pathology and response to therapy. However, most of the current <em>in vitro</em> models use matrices of animal origin and that do not recapitulate the complexity of the tumour ECM in patients.</p><p>Here, we have developed omentum gel (OmGel), a matrix made from tumour-associated omental tissue of HGS ovarian cancer patients that has unprecedented similarity to the ECM of HGS omental tumours and is simple to prepare. When used in 2D and 3D <em>in vitro</em> assays to assess cancer cell functions relevant to metastatic ovarian cancer, OmGel performs as well as or better than the widely use Matrigel and does not induce additional phenotypic changes to ovarian cancer cells. Surprisingly, OmGel promotes pronounced morphological changes in cancer associated fibroblasts (CAFs). These changes were associated with the upregulation of proteins that define subsets of CAFs in tumour patient samples, highlighting the importance of using clinically and physiologically relevant matrices for <em>in vitro</em> studies. Hence, OmGel provides a step forward to study the biology of HGS omental metastasis. Metastasis in the omentum are also typical of other cancer types, particularly gastric cancer, implying the relevance of OmGel to study the biology of other highly lethal cancers.</p></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"19 ","pages":"Article 100136"},"PeriodicalIF":0.0,"publicationDate":"2023-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.sciencedirect.com/science/article/pii/S2590028523000091/pdfft?md5=db15a375c67dbdf83c9f1115a1abae05&pid=1-s2.0-S2590028523000091-main.pdf","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"138439427","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}