Matrix Biology Plus最新文献

{"title":"Latent-Transforming growth factor − β Binding protein 1 (LTBP1) in corneal stroma","authors":"Isaac Poonen-Honig ,&nbsp;Ana C Acosta ,&nbsp;Mei Sun ,&nbsp;Victoria Emerick ,&nbsp;Marcel Y Avila ,&nbsp;Curtis E. Margo ,&nbsp;Edgar M Espana","doi":"10.1016/j.mbplus.2025.100185","DOIUrl":"10.1016/j.mbplus.2025.100185","url":null,"abstract":"<div><div>We aim to determine the presence and function of LTBP1 in the corneal stroma. We investigated the temporal and spatial corneal expression of LTBP1, and microfibril-associated glycoprotein 1 (MAGP1), known components of the elastic system and regulators of TGF-β storage and latency. Protein quantification −blotting and proteomics-, immunofluorescence microscopy, mRNA analysis and a luciferase assay were used to study the regulation of transforming growth factor β (TGF-β) by LTBP1 in cornea derived fibroblasts and myofibroblasts. Expression of LTBP1 and MAGP1 was found in adult corneas, and absent or minimal in the scleral stroma. Quantitative polymerase chain reaction and protein blotting analyses showed upregulation of these proteins during early postnatal development and deposition in the corneal matrix with tissue maturation. In vitro, LTBP1 regulated the conversion of fibroblasts to myofibroblasts and maintained TGF-β latent in the matrix. This study shows that LTBP1 and MAGP1, regulators of TGF-β activation and elastic fiber components, are found in adult stroma. LTBP1 is a regulator of TGF-β storage and latency and controls conversion of fibroblast to myofibroblast.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100185"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145528265","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Convergence research in matrix biology and biomaterials science","authors":"Daniel L. Alge ,&nbsp;Ashley Brown","doi":"10.1016/j.mbplus.2025.100180","DOIUrl":"10.1016/j.mbplus.2025.100180","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100180"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145693601","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Presence of type IIB procollagen in mouse articular cartilage and growth plate is revealed by immuno-histochemical analysis with a novel specific antibody” [Matrix Biol. Plus 18 (2023) 100130]","authors":"Emeline Perrier-Groult,&nbsp;Shérine Moustaghfir,&nbsp;Marielle Pasdeloup,&nbsp;Jean-Daniel Malcor,&nbsp;Jérôme Lafont,&nbsp;Frédéric Mallein-Gerin","doi":"10.1016/j.mbplus.2025.100177","DOIUrl":"10.1016/j.mbplus.2025.100177","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100177"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145690605","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Corrigendum to “Obesity-driven changes in breast extracellular matrix exhibit a pro-angiogenic phenotype” [Matrix Biol. Plus 24 (2024) 100162]","authors":"Ellen E. Bamberg ,&nbsp;Mark Maslanka ,&nbsp;Kiran Vinod-Paul ,&nbsp;Sharon Sams ,&nbsp;Erica Pollack ,&nbsp;Matthew Conklin ,&nbsp;Peter Kabos ,&nbsp;Kirk C. Hansen","doi":"10.1016/j.mbplus.2025.100178","DOIUrl":"10.1016/j.mbplus.2025.100178","url":null,"abstract":"","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"28 ","pages":"Article 100178"},"PeriodicalIF":0.0,"publicationDate":"2025-12-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"145693689","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Exosome enriched serum enhances engineered ligament mechanics and collagen content with no additional benefit of resistance exercise.","authors":"Kevin J M Paulussen, Christopher M T Hayden, Taylor Griffin, Keith Baar","doi":"10.1016/j.mbplus.2025.100181","DOIUrl":"10.1016/j.mbplus.2025.100181","url":null,"abstract":"<p><p>Following resistance exercise, systemic changes foster improved functionality of tendons and ligaments. Post-exercise, muscle tissue releases exosomes that are thought to facilitate inter-tissue communication. To determine the potential role of exosomes in the exercise-induced adaptations of tendons and ligaments, we modified our engineered human ligament (EHL) model to work with exosome-enriched serum. Treatment of the EHLs with exosomes enriched from fetal bovine serum (fbEXO) resulted in enhanced ligament mechanics and increased collagen content in a dose-response fashion (maximum tensile load [MTL]: 10 %: 0.196 ± 0.138 N, 20 %: 0.278 ± 0.103 N, 40 %: 0.840 ± 0.092 N; r² = 0.858, <i>P</i> < 0.0001; collagen content: 10 %: 1.073 ± 12.49 µg, 20 %: 86.43 ± 71.65 µg, 40 %: 145.7 ± 84.11 µg; r² = 0.4735, <i>P</i> = 0.0046). After optimizing an exosome enriched feeding protocol using fbEXO, we confirmed that exosomes enriched from human serum (hsEXO) could sustain EHL function. Subsequently, twelve healthy, recreationally active volunteers (22 ± 3 y, 1,68 ± 0.10 m, 65.6 ± 27.8 kg; 6F/6M) performed a single bout of resistance exercise. Serum samples were collected prior to and 15 min post-exercise, and exosomes were enriched from these samples for treatment of EHLs. EHL function and collagen content did not differ when treated with hsEXO obtained at rest or post-resistance exercise (MTL: 1.30 ± 0.36 vs. 1.20 ± 0.36 N, <i>P</i> = 0.3950; collagen content: 424.6 ± 47.68 vs. 425.2 ± 44.46 µg, <i>P</i> = 0.9663). This model provides a novel way to determine the role of exosomes in connective tissue development and adaptation. The identification of circulating exercise factors that enhance tendon and ligament function remains to be fully elucidated.</p>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"27 ","pages":"100181"},"PeriodicalIF":0.0,"publicationDate":"2025-08-08","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"https://www.ncbi.nlm.nih.gov/pmc/articles/PMC12357142/pdf/","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144876723","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 characterization of type I collagen N-terminal crosslinked peptides","authors":"Zsuzsanna Darula ,&nbsp;Maxwell C. McCabe ,&nbsp;Alex Barrett ,&nbsp;Lauren R. Schmitt ,&nbsp;Mark D. Maslanka ,&nbsp;Anthony J Saviola ,&nbsp;Joseph Orgel ,&nbsp;Alma Burlingame ,&nbsp;Claudia A. Staab-Weijnitz ,&nbsp;Kurt Stenmark ,&nbsp;Valerie Weaver ,&nbsp;Robert J. Chalkley ,&nbsp;Kirk C. Hansen","doi":"10.1016/j.mbplus.2025.100179","DOIUrl":"10.1016/j.mbplus.2025.100179","url":null,"abstract":"<div><div>Collagen cross-links mediated by the lysyl oxidase and lysyl hydroxylase families of enzymes significantly contribute to the biomechanical strength and rigidity of tissues, influencing cell signaling and the downstream cell phenotype. In the clinic, the proteolytically liberated N-terminal cross-linked peptide of collagen I (NTX) is used as a biomarker of bone and connective tissue turnover, which is altered in several disease processes. Despite the clinical utility of these collagen breakdown products, the majority of the cross-linked peptide species have not been identified in proteomic datasets. Here, we evaluate several parameters for the preparation and identification of these peptides from the collagen I-rich Achilles tendon. Our refined approach, which involves chemical digestion for protein solubilization coupled with mass spectrometry, enables the identification of NTX cross-links in a range of modification states. We then applied a spectral library approach to identify differences in collagen cross-links in bovine pulmonary hypertension. The presented method offers unique opportunities to understand extracellular matrix remodeling events in development, aging, wound healing, and fibrotic disease that modulate collagen architecture through lysyl hydroxylase and lysyl oxidase enzymes.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"27 ","pages":"Article 100179"},"PeriodicalIF":0.0,"publicationDate":"2025-08-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144330525","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Small Integrin binding Ligand N-linked Glycoproteins, prostate-specific antigen and time to prostate cancer diagnosis","authors":"Alka Jain ,&nbsp;Ying Ni ,&nbsp;Daisy Zhang ,&nbsp;Eleanor M. Simonsick ,&nbsp;E. Jeffrey Metter ,&nbsp;Kalu U. Ogbureke ,&nbsp;Larry W. Fisher ,&nbsp;Neal S. Fedarko","doi":"10.1016/j.mbplus.2025.100171","DOIUrl":"10.1016/j.mbplus.2025.100171","url":null,"abstract":"<div><div>Background: <u>S</u>mall <u>I</u>ntegrin <u>B</u>inding <u>Li</u>gand <u>N</u>-linked <u>G</u>lycoproteins (SIBLINGs¹) were associated with cancer in cross-sectional studies. Whether SIBLINGs associate with preclinical disease is unknown. Methods: A retrospective longitudinal case control study was performed to determine the association of SIBLINGs and prostate-specific antigen (PSA) with preclinical disease. Paired serum samples from 109 cancer-free Baltimore Longitudinal Study on Aging participants were divided into those that were either most distal or proximal to diagnosis (cases) or censored (controls). Dentin sialophosphoprotein (DSPP), bone sialoprotein (BSP), osteopontin (OPN), and PSA were measured by immunoassay and dichotomized into low or high based on their respective cut-off values. Associations of time to diagnosis or death, modeled as disease-free survival (DFS) or overall survival (OS), were assessed using Kaplan Meier and Cox proportional hazard survival estimates on individual and aggregated biomarkers in distal or proximal sets separately. Models were adjusted for relevant covariates. A false discovery rate analysis assessed significance of hazard ratios (HRs) in sets. Results: Biomarkers/aggregates identified as true discoveries for DFS included DSPP + PSA, OPN + PSA, DSPP + BSP + PSA, DSPP + OPN + PSA, where unadjusted distal HRs ranged between 11 and 27 and after adjusting for age from 7 to 15, while proximal HRs ranged between 6 and 10 unadjusted and 5 to 12 after adjusting for age. For proximal OS, true discoveries included DSPP + BSP, DSPP + OPN, DSPP + BSP + OPN, and DSPP + OPN + PSA where unadjusted HRs ranged between 6 and 20 while age-adjusted HRs ranged between 5 and 12. Conclusions: These observations support SIBLINGs as biomarkers that associate with DFS and OS in prediagnosis samples.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"26 ","pages":"Article 100171"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143715291","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"OA","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"The staphylococcal collagen adhesin CNA35 effectively detects collagen and its fragments in blots after SDS-PAGE","authors":"Elena N. Pokidysheva ,&nbsp;Jennifer Diaz Sales ,&nbsp;Shinomi Yagi ,&nbsp;Tomonori Ueno ,&nbsp;Kanako Sasai ,&nbsp;Alice Makarenko ,&nbsp;Hans Peter Bächinger ,&nbsp;Kazunori Mizuno ,&nbsp;Sergei P. Boudko","doi":"10.1016/j.mbplus.2025.100174","DOIUrl":"10.1016/j.mbplus.2025.100174","url":null,"abstract":"<div><div>Collagens are a diverse family of proteins present in the extracellular matrix (ECM) of all animals. They play crucial roles in providing structural support to tissues, forming scaffolds for ECM suprastructures, and signaling cells. Certain collagen-binding proteins from pathogenic bacteria, such as CollageN Adhesin (CNA) from <em>Staphylococcus aureus</em>, interact with the collagen triple helix to promote host invasion. The extracellular portion of CNA, known as CNA35, which has a molecular weight of 35 kDa, has been used for <em>in vitro</em>, <em>ex vivo</em>, and <em>in vivo</em> staining of various collagen types in tissues.</div><div>Detecting various types of collagens necessitates the use of type- and specie-specific antibodies, which typically exhibit weak affinities for the triple helical regions of collagens. Additionally, the fragmentation of collagens can lead to a loss of detection due to the limited number of available epitopes. Furthermore, antibodies can be expensive, require secondary identification methods, and are often suitable for either immunohistochemistry or western blotting. Although successful procedures for staining collagens in tissues have been implemented, the detection of collagens and their fragments using CNA35 has not been reported for protein blots.</div><div>In this study, we examined the detection capabilities of a trimeric form of CNA35 for protein blots following SDS-PAGE. We successfully tested collagens I through VI, as well as fragments of collagen IV, under various conditions. Additionally, we investigated the impact of blocking solutions, incubation time, ligand concentration, and CNA35 concentration on sensitivity.</div><div>We achieved superior detection of all tested collagens and collagen IV fragments, including the 7S domain, which is a highly crosslinked complex composed of four triple-helical strands. The method we developed serves as a universal tool for detecting collagens and collagen-containing peptides in protein blots. It offers several advantages, including sub-nanogram sensitivity, low cost, and compatibility with standard western blotting techniques.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"26 ","pages":"Article 100174"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"144135126","PeriodicalName":null,"FirstCategoryId":null,"ListUrlMain":null,"RegionNum":0,"RegionCategory":"","ArticlePicture":[],"TitleCN":null,"AbstractTextCN":null,"PMCID":"","EPubDate":null,"PubModel":null,"JCR":null,"JCRName":null,"Score":null,"Total":0}

{"title":"Crosstalk between T cells and fibroblasts in biomaterial-mediated fibrosis","authors":"Mathew Kibet,&nbsp;Daniel Abebayehu","doi":"10.1016/j.mbplus.2025.100172","DOIUrl":"10.1016/j.mbplus.2025.100172","url":null,"abstract":"<div><div>Biomaterial implants are a critical aspect of our medical therapies and biomedical research and come in various forms: stents, implantable glucose sensors, orthopedic implants, silicone implants, drug delivery systems, and tissue engineered scaffolds. Their implantation triggers a series of biological responses that often times lead to the foreign body response and subsequent fibrotic encapsulation, a dense ECM-rich capsule that isolates the biomaterial and renders it ineffective. These responses lead to the failure of biomaterials and is a major hurdle to overcome and in promoting their success. Much attention has been given to macrophage populations for the inflammatory component of these responses to biomaterials but recent work has identified an important role of T cells and their ability to modulate fibroblast activity and vice versa. In this review, we focus on T cell-fibroblast crosstalk by exploring T cell subsets, critical signaling pathways, and fibroblast populations that have been shown to dictate biomaterial-mediated fibrosis. We then highlight emerging technologies and model systems that enable new insights and avenues to T cell-fibroblast crosstalk that will improve biomaterial outcomes.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"26 ","pages":"Article 100172"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143703907","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":"Development of an in vitro platform for epithelial-stromal interactions: A basement membrane-containing scaffold from decellularized porcine bladders","authors":"J.A. Ramirez ,&nbsp;S. Estrada ,&nbsp;M.C. Harmsen ,&nbsp;P.K. Sharma","doi":"10.1016/j.mbplus.2025.100169","DOIUrl":"10.1016/j.mbplus.2025.100169","url":null,"abstract":"<div><div>The first organized extracellular matrix that appears during mammalian embryogenesis is a basement membrane (BM), BM is present in all adult epithelia, endothelia, muscle, nerve and fat tissues. BM is a sub-micrometer thick compact lattice of macromolecules that is maintained by the adhered cells. Systems such as collagen gels, Matrigel® or synthetic polymeric scaffolds have been proposed to mimic the BM and to study the interactions between different cell types, but all lack a structured BM. Here we aimed to obtain and characterize a natural, thin basement membrane-containing scaffold from pig urinary bladders that are subjected to blunt dissection of layers and decellularization steps, preserving the near native BM with a few layers of underlying connective tissue to maintain its structural integrity. The scanning electron microscopy, confocal multiphoton microscopy and immunohistochemistry helped confirm the presence of the BM. A veil-like network composed of thin fibers was present on top of a course network, and glycosaminoglycans, collagen and basement membrane proteins were present. The scaffold’s ability to repopulation and basement membrane barrier function were further confirmed when HaCaT and MRC5 cells attached and remained respectively on the epithelial and mesenchymal side without any crossover. Cells remained viable till 2 weeks. This BM-containing scaffold allows to create <em>in vitro</em> models of epithelial-mesenchymal tissues through a structured basement membrane and investigate basement membrane dynamics. The basement membrane-containing scaffold was found to be isotropic under uniaxial tension with a failure strain of 0.25 allowing its use to investigate strain induced basement membrane dynamics.</div></div>","PeriodicalId":52317,"journal":{"name":"Matrix Biology Plus","volume":"26 ","pages":"Article 100169"},"PeriodicalIF":0.0,"publicationDate":"2025-06-01","publicationTypes":"Journal Article","fieldsOfStudy":null,"isOpenAccess":false,"openAccessPdf":"","citationCount":null,"resultStr":null,"platform":"Semanticscholar","paperid":"143552126","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}