Matrix BiologyPub Date : 2025-08-14DOI: 10.1016/j.matbio.2025.08.004
Andrea Page-McCaw , Nicholas Ferrell
{"title":"Basement membrane structure and function: Relating biology to mechanics","authors":"Andrea Page-McCaw , Nicholas Ferrell","doi":"10.1016/j.matbio.2025.08.004","DOIUrl":"10.1016/j.matbio.2025.08.004","url":null,"abstract":"<div><div>Basement membranes are key mediators of many biological processes such as epithelial morphogenesis, kidney filtration, and muscle function among others. Basement membranes provide structural support to tissues so understanding their mechanical properties is important for determining how they contribute to tissue form and function. Further, basement membranes are altered in many diseases including cancer, diabetes, and fibrosis, and these changes may contribute to disease pathogenesis and progression. Understanding how basement membrane mechanics integrate with tissue function is the work of both biologists and engineers/material scientists, yet these disciplines have very different foundations. This review discusses basement membrane macromolecular structure with a view to illuminate how this structure confers basement membranes with unique mechanical properties adapted to resisting physiological stresses. The pathological implications of altered basement membrane mechanics are discussed in the context of different diseases. Additionally, we survey methods used to measure basement membrane mechanical properties, including atomic force microscopy, tensile stiffness assays, and non-quantitative assays such as cell bursting, assessing their strengths and limitations and their accessibility for different types of <em>in vivo</em> studies. We focus on explaining and illuminating the complexities of basement membrane material properties for biologists, and explaining the biological aspects for engineers, with the goal of making interdisciplinary science more accessible to experimentalists and readers.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"141 ","pages":"Pages 16-31"},"PeriodicalIF":4.8,"publicationDate":"2025-08-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144862618","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Matrix BiologyPub Date : 2025-08-12DOI: 10.1016/j.matbio.2025.08.001
Mariano Colon-Caraballo , Nicole Lee , Shanmugasundaram Nallasamy , Kristin Myers , David Hudson , Renato V. Iozzo , Mala Mahendroo
{"title":"Retraction Notice for “Novel regulatory roles of small leucine-rich proteoglycans in remodeling of the uterine cervix in pregnancy” [Matrix Biology, Volume 105, January 2022, Pages 53-71]","authors":"Mariano Colon-Caraballo , Nicole Lee , Shanmugasundaram Nallasamy , Kristin Myers , David Hudson , Renato V. Iozzo , Mala Mahendroo","doi":"10.1016/j.matbio.2025.08.001","DOIUrl":"10.1016/j.matbio.2025.08.001","url":null,"abstract":"","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 154-155"},"PeriodicalIF":4.8,"publicationDate":"2025-08-12","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144827504","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Matrix BiologyPub Date : 2025-08-10DOI: 10.1016/j.matbio.2025.08.003
Argyris Spyrou , Ananya Roy , Anqi Xiong , Soumi Kundu , Xi Lu , Ylva Jansson , Anna Falk , Christoph Riethmüller , Burkhard Greve , Martin Götte , Xinqi Chen , Lena Kjellén , Karin Forsberg-Nilsson
{"title":"Heparan sulfate N-deacetylase/N-sulfotransferase-1 regulates glioblastoma cell migration and invasion","authors":"Argyris Spyrou , Ananya Roy , Anqi Xiong , Soumi Kundu , Xi Lu , Ylva Jansson , Anna Falk , Christoph Riethmüller , Burkhard Greve , Martin Götte , Xinqi Chen , Lena Kjellén , Karin Forsberg-Nilsson","doi":"10.1016/j.matbio.2025.08.003","DOIUrl":"10.1016/j.matbio.2025.08.003","url":null,"abstract":"<div><div>The glioblastoma (GBM) microenvironment undergoes adaptations to support tumor progression, including a dysregulated extracellular matrix, with altered heparan sulfate (HS) proteoglycans. We investigated N-deacetylase/N-sulfotransferase-1 (NDST1) because NDSTs are initial modifying enzymes of HS biosynthesis and have key roles in designing the HS sulfation pattern. This, in turn governs interactions with growth factors and other biomolecules. We report that NDST1 expression is lower in GBM than in the normal brain, and that patient-derived GBM cells, grown under neural stem cell culture conditions have lower levels of HS than normal astrocytes. Overexpression of NDST1 in GBM cells with low inherent NDST1 levels stimulates cell migration, reduce cell adhesion, induce EMT markers and increase invasion. Conversely, when NDST1 levels were reduced by shRNA in GBM cells, that had higher baseline expression, we find that invasion is reduced, and instead, self-renewal capacity increases alongside elevated stem cell marker expression. Moreover, overexpression of NDST1 changes chromatin accessibility of gene regulatory regions with the capacity to affect transcription factor expression, and pathways that favors cell motility and invasion. Furthermore, NDST1 overexpression results in increased activation of several receptor tyrosine kinases. This study shows that low NDST1 levels support GBM cell stemness, whereas high NDST1 levels endow tumor cells with a motile cell phenotype. We therefore propose that NDST1 is important for regulation of the balance between proliferation and invasive properties in GBM cells.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"141 ","pages":"Pages 1-15"},"PeriodicalIF":4.8,"publicationDate":"2025-08-10","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144838410","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Matrix BiologyPub Date : 2025-07-28DOI: 10.1016/j.matbio.2025.07.007
Matilda Thuringer , Roy Zent , Rachel Lennon , Erin J. Plosa
{"title":"Basement membranes in lung development, disease, and repair","authors":"Matilda Thuringer , Roy Zent , Rachel Lennon , Erin J. Plosa","doi":"10.1016/j.matbio.2025.07.007","DOIUrl":"10.1016/j.matbio.2025.07.007","url":null,"abstract":"<div><div>The primary function of the respiratory system is the exchange of oxygen and carbon dioxide across the alveolar-capillary barrier in the distal lung. This structure is composed of alveolar epithelial cells (type 1 and type 2) and capillary endothelial cells, separated by a thin, fused alveolar basement membrane. The developmental programming that creates this specialized niche is largely unexplored and the role of lung basement membranes in respiratory disease pathogenesis and repair remains an emerging field of study. Thus, in this review, we discuss the distribution, composition, and function of the alveolar basement membrane, as well as the other three lung basement membranes that support the airway epithelium, airway smooth muscles, and the endothelium of the macrovasculature in lung development and disease.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 123-132"},"PeriodicalIF":4.8,"publicationDate":"2025-07-28","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144754962","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Collagen diversity in human skin: Aging, wound healing, and disorders","authors":"Mélanie Salamito , Valérie Haydont , Hervé Pageon , Florence Ruggiero , Sarah Girardeau-Hubert","doi":"10.1016/j.matbio.2025.07.006","DOIUrl":"10.1016/j.matbio.2025.07.006","url":null,"abstract":"<div><div>Collagen is an essential skin protein, accounting for 75 % of the skin’s dry weight. The collagen superfamily encompasses a diverse group of proteins with a variety of structures that fulfil a wide range of functions. The half-life of collagen in the skin is generally estimated at 10 to 15 years; however, the expression pattern of the different types of skin collagen varies throughout life. Both intrinsic and extrinsic factors influence collagen turn-over within the different skin layers. In this review, we discuss current knowledge of the different types of collagen present in human skin, focusing on insights gained from research exploring the dynamic roles of these proteins in skin development, homeostasis including aging, collagen-linked pathologies, adaptability in response to stress, and wound healing-related processes and disorders. Specificities of skin diversity due to ancestral origin and gender will also be discussed.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 133-153"},"PeriodicalIF":4.8,"publicationDate":"2025-07-25","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144734955","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Matrix BiologyPub Date : 2025-07-22DOI: 10.1016/j.matbio.2025.07.005
Angus Nichols, Besaiz J. Sánchez-Sánchez, Stefania Marcotti, María-del-Carmen Díaz-de-la-Loza, Leonel C. Menezes, Tingfei Wang, Robert M. Johnson, Brian M. Stramer
{"title":"Drosophila Col4a1 Glycine mutations highlight allelic heterogeneity and mechanistic pleiotropy","authors":"Angus Nichols, Besaiz J. Sánchez-Sánchez, Stefania Marcotti, María-del-Carmen Díaz-de-la-Loza, Leonel C. Menezes, Tingfei Wang, Robert M. Johnson, Brian M. Stramer","doi":"10.1016/j.matbio.2025.07.005","DOIUrl":"10.1016/j.matbio.2025.07.005","url":null,"abstract":"<div><div>Collagen IV (Col4) is a heterotrimer containing a triple helical domain broken up by short interruptions. Mutation of Glycine residues within the Glycine-X-Y triple helical repeat leads to genetically dominant disease in humans that affects multiple organ systems. Mouse and cell culture-based models have revealed allelic heterogeneity, resulting in a range of Col4 secretion defects depending on the position of the mutation. However, genetic background also affects phenotypic severity, making it challenging to understand the precise underlying molecular mechanisms driving disease. Here, we characterize an allelic series of dominant temperature-sensitive <em>Drosophila</em> Glycine mutations to identify the potential molecular mechanisms driving phenotypic heterogeneity. Analysis of developmental viability at the non-permissive temperature revealed that mutations show a range of developmental lethality that is not correlated with their position within the triple helix nor with the degree of Col4 secretion defect. Backcrossing the series of fly lines led to increased lethality for almost all alleles, highlighting the presence of genetic modifiers, which paradoxically led to a reduction in secretion defects; this further suggests that defective secretion cannot explain the allelic heterogeneity in mutant viability. Analysis of the Col4 network surrounding the central nervous system (CNS) revealed that Glycine mutations can also affect basement membrane (BM) structure and alter its mechanical properties. Additionally, fluorescent tagging of a Glycine mutant variant showed that the mutated trimer is sufficiently secreted and can be incorporated into the network to dominantly affect BM organization. These data reveal that Col4 Glycine mutations can cause both secretion and direct BM network defects, suggesting that Col4-related pathologies may be mechanistically pleiotropic.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 113-122"},"PeriodicalIF":4.5,"publicationDate":"2025-07-22","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144700161","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Matrix BiologyPub Date : 2025-07-15DOI: 10.1016/j.matbio.2025.06.003
K. Yanín Guerra Santillán, Christian Dahmann, Elisabeth Fischer-Friedrich
{"title":"ECM proteins shape topographical patterns in the basement membrane of Drosophila wing discs","authors":"K. Yanín Guerra Santillán, Christian Dahmann, Elisabeth Fischer-Friedrich","doi":"10.1016/j.matbio.2025.06.003","DOIUrl":"10.1016/j.matbio.2025.06.003","url":null,"abstract":"<div><div>The basal surface of epithelial tissues is attached to a thin network of macromolecules known as the basement membrane. The core components of the basement membrane — Collagen IV, Laminin, Perlecan, and Nidogen — are conserved extracellular matrix (ECM) proteins across species. However, the topography of basement membranes and the contribution of individual core components to its establishment remain poorly understood. Here, we used AFM-aided PeakForce tapping to analyze the topography of the basement membrane of <em>Drosophila</em> larval wing discs. We identified a self-affine surface topography, appearing structurally similar across multiple scales. Further, the topography is characterized by thin fiber-like structures that are intermittently aligned with a preferred orientation along the anterior-posterior axis. During larval development, the amplitude of surface patterns overall decreases, whereas the abundance of basement membrane components increases. Using targeted knockdown experiments, we show that Collagen IV is essential for the formation of fiber-like structures, while Laminin and Collagen IV appear to smooth or level out large-scale groove-like patterns. In contrast, Nidogen contributes to the maintenance of these grooves, and Perlecan increases surface pattern amplitudes at all length scales. Our findings reveal distinct topographical features in the basement membrane, whose amplitude and organization depend on its specific molecular composition.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 78-87"},"PeriodicalIF":4.5,"publicationDate":"2025-07-15","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144655501","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
{"title":"Role of extracellular space and matrix remodeling in cardiac amyloidosis","authors":"Francesca Lavatelli , Loredana Marchese , Palma Patrizia Mangione , Sara Raimondi , Diana Canetti , Guglielmo Verona , Lucia Venneri , Eloisa Arbustini , Laura Obici , Alessandra Corazza , Vittorio Bellotti , Sofia Giorgetti","doi":"10.1016/j.matbio.2025.07.004","DOIUrl":"10.1016/j.matbio.2025.07.004","url":null,"abstract":"<div><div>The hallmark of amyloid diseases is deposition of misfolded proteins as amyloid fibrils in the interstitium of target organs. Amyloid deposits surround cells, distorting the micro and macro-architecture of the extracellular space and profoundly changing the physical and molecular properties of this compartment. In the heart, extracellular matrix (ECM) remodeling has a profound impact on the mechanical properties of this target organ and on the physiology and metabolism of resident cells. This review critically summarizes the available knowledge on ECM alterations in cardiac amyloidosis, with the goal of providing an overview on how biochemical, biophysical and anatomical modifications are interrelated, and how ECM remodeling participates in the pathophysiology of this unique type of cardiopathy.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 100-112"},"PeriodicalIF":4.5,"publicationDate":"2025-07-14","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144622477","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Matrix BiologyPub Date : 2025-07-09DOI: 10.1016/j.matbio.2025.07.001
Alana Stevenson Harris , Rachel Lennon , Jean-Marc Schwartz
{"title":"Building basement membranes with computational approaches","authors":"Alana Stevenson Harris , Rachel Lennon , Jean-Marc Schwartz","doi":"10.1016/j.matbio.2025.07.001","DOIUrl":"10.1016/j.matbio.2025.07.001","url":null,"abstract":"<div><div>Basement membranes (BMs) are dense extracellular matrix scaffolds that support cells. Their composition, structure and dynamic regulation are vital for tissue health and altered in human disease. The expansion of experimental and analytical techniques has generated large multiomic datasets that include BM components; however, the organising principles of BM component assembly and the regulation of BMs remain poorly understood. There are over 160 curated BM proteins, including core, ubiquitous components such as type IV collagen and laminin isoforms, as well as tissue-restricted components, and there is increasing experimental evidence of BM protein-protein interactions. Here we describe and compare multiomic, protein-protein interaction, and BM curation databases and discuss the application of systems biology approaches including network analysis, Boolean networks and Ordinary Differential Equations to integrate data and model BM organisation. Applying computational modelling strategies to BM datasets may reveal unknown organising principles of BM assembly and regulation and predict mechanisms of dysregulation in BM-associated diseases.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 88-99"},"PeriodicalIF":4.5,"publicationDate":"2025-07-09","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144621006","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}
Matrix BiologyPub Date : 2025-07-07DOI: 10.1016/j.matbio.2025.07.003
Sergei P. Boudko
{"title":"Around the collagen triple helix: an introduction to studying associated genetic and acquired diseases","authors":"Sergei P. Boudko","doi":"10.1016/j.matbio.2025.07.003","DOIUrl":"10.1016/j.matbio.2025.07.003","url":null,"abstract":"<div><div>The triple helix structure of collagen is the most abundant motif found in our bodies. It is believed to have emerged during the transition from unicellular to multicellular animal organisms, known as metazoans, and has evolved into various proteins that contribute to the development and function of diverse animal tissues, organs, and systems. Once synthesized, these collagenous proteins undergo post-translational modifications and proper folding inside the cell, after which they primarily function outside the cell. Over 80 collagenous proteins are categorized into two main groups: collagens and collagen-like proteins. However, the distinction between these groups is not clearly defined. Within these categories, there are various types of proteins, including soluble proteins, transmembrane proteins, and those that form the extracellular matrix. Multiple genetic diseases highlight the significance of collagenous proteins, which can be affected by defects in their primary structure, post-translational modifications, or complete loss. While fixing the gene defect may seem like a straightforward solution, we currently lack the capability to do so. Moreover, acquired diseases caused or accompanied by adverse processes in the collagen triple helix are generally not suitable for gene therapy at all. Understanding the pathogenicity of a defective polypeptide chain can provide valuable insights into strategies for mitigating negative consequences for both genetic and acquired diseases. This review highlights the current state of research in the collagen triple helix field, offering insights into how to study specific defects and deepen our understanding of their underlying pathogenic mechanisms.</div></div>","PeriodicalId":49851,"journal":{"name":"Matrix Biology","volume":"140 ","pages":"Pages 43-58"},"PeriodicalIF":4.5,"publicationDate":"2025-07-07","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144602117","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":1,"RegionCategory":"生物学","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}