Force-mediated recruitment and reprogramming of healthy endothelial cells drive vascular lesion growth

Bravo à l’équipe d’Eva Faurobert (Institute for Advanced Biosciences IAB, CNRS Grenoble) et ses collaborateurs, pour leur article à paraitre. Force-mediated recruitment and reprogramming of healthy endothelial cells drive vascular lesion growth | bioRxiv. sur leurs travaux que nous avons eu le plaisir d’entendre lors du congres de la SFBMEC.

Offre CDD Enseignant Chercheur à l’Université de Cergy

L’Université de Cergy recrute un-e Enseignant-e Chercheur-se en Biologie Cellulaire et Biochimie pour la rentrée 2023, et pour une activité de recherche au sein du laboratoire ERRMECE, dans l’équipe Mec-Up qui étudie l’influence du microenvironnement
sénescent sur la dissémination tumorale. N’hésitez pas à candidater (CV et lettre de motivation) aupres de cedric.picot@cyu.fr. Pour plus d’infos : Offre de CDD Ens Chercheur-MecUp

The critical role of the TB5 domain of fibrillin-1 in endochondral ossification

Félicitations à l’équipe de Carine Le Goff (INSERM U1148, Laboratory of Vascular Translational Science, Bichat Hospital, Paris, Université Paris Cité) et ses collaborateurs pour leur dernière publication dans Human Molecular Genetics !

Laure Delhon, Zakaria Mougin, Jérémie Jonquet, Angélique Bibimbou, Johanne Dubail, Cynthia Bou-Chaaya, Nicolas Goudin, Wilfried Le Goff, Catherine Boileau, Valérie Cormier-Daire, Carine Le Goff, The critical role of the TB5 domain of fibrillin-1 in endochondral ossification, Human Molecular Genetics, Volume 31, Issue 22, 15 November 2022, Pages 3777–3788, https://doi.org/10.1093/hmg/ddac131

Mutations in the fibrillin-1 (FBN1) gene are responsible for the autosomal dominant form of geleophysic dysplasia (GD), which is characterized by short stature and extremities, thick skin and cardiovascular disease. All known FBN1 mutations in patients with GD are localized within the region encoding the transforming growth factor-β binding protein-like 5 (TB5) domain of this protein. Herein, we generated a knock-in mouse model, Fbn1Y1698C by introducing the p.Tyr1696Cys mutation from a patient with GD into the TB5 domain of murine Fbn1 to elucidate the specific role of this domain in endochondral ossification. We found that both Fbn1Y1698C/+ and Fbn1Y1698C/Y1698C mice exhibited a reduced stature reminiscent of the human GD phenotype. The Fbn1 point mutation introduced in these mice affected the growth plate formation owing to abnormal chondrocyte differentiation such that mutant chondrocytes failed to establish a dense microfibrillar network composed of FBN1. This original Fbn1 mutant mouse model offers new insight into the pathogenic events underlying GD. Our findings suggest that the etiology of GD involves the dysregulation of the extracellular matrix composed of an abnormal FBN1 microfibril network impacting the differentiation of the chondrocytes.

Regulation of stem cell fate by HSPGs : implication in hair follicle cycling.

Bravo et merci à Charlie Colin Pierre et ses collaborateurs de l’équipe de Stéphane Brezillon (Université de Reims Champagne-Ardenne, Laboratoire MEDyC, CNRS UMR 7369) pour cette revue très complète en open access dans « Regenerative Medicine ».  Colin-Pierre C, El Baraka O, Danoux L, Bardey V, André V, Ramont L, Brézillon S. NPJ Regen Med. 2022 Dec 28;7(1):77. https://doi.org/10.1038/s41536-022-00267-y PMID: 36577752.

Heparan sulfate proteoglycans (HSPGs) are part of proteoglycan family. They are composed of heparan sulfate (HS)-type glycosaminoglycan (GAG) chains covalently linked to a core protein. By interacting with growth factors and/or receptors, they regulate numerous pathways including Wnt, hedgehog (Hh), bone morphogenic protein (BMP) and fibroblast growth factor (FGF) pathways. They act as inhibitor or activator of these pathways to modulate embryonic and adult stem cell fate during organ morphogenesis, regeneration and homeostasis. This review summarizes the knowledge on HSPG structure and classification and explores several signaling pathways regulated by HSPGs in stem cell fate. A specific focus on hair follicle stem cell fate and the possibility to target HSPGs in order to tackle hair loss are discussed in more dermatological and cosmeceutical perspectives.

 

 

Differential MMP-14 Targeting by Biglycan, Decorin, Fibromodulin and Lumican Unraveled by In Silico Approach.

Félicitations à l’équipe de Stéphane Brezillon et ses collaborateurs pour leur nouvelle publication dans « Am J Physiol Cell Physiol. » sur le rôle des SLRP et de leurs chaines de GAG dans la régulation de l’activité de MMP-14 !

Rivet R, Rao RM, Nizet P, Belloy N, Huber L, Dauchez M, Ramont L, Baud S, Brézillon S. Am J Physiol Cell Physiol. 2022 Dec 19. doi: 10.1152/ajpcell.00429.2022. Online ahead of print.PMID: 36534501

Small leucine-rich proteoglycans (SLRPs) are major regulators of extracellular matrix assembly and cell signaling. Lumican, a member of the SLRPs family, and its derived peptides possess anti-tumor activity by interacting directly with the catalytic domain of MMP-14 leading to the inhibition of its activity. The aim of this report was to characterize by in silico 3D modeling the structure and the dynamics of four SLRPs including their core protein and their specific polysaccharide chains to assess their capacity to bind to MMP-14 and to regulate its activity. Molecular docking experiments were performed to identify the specific amino acids of MMP-14 interacting with each of the four SLRPs. The inhibition of each SLRP (100nM) on MMP-14 activity and the constants of inhibition (Ki) were evaluated. The impact of the number of glycan chains, structures and dynamics of lumican on the interaction with MMP-14 was assessed by molecular dynamics simulations. Molecular docking analysis showed that all SLRPs bind to MMP-14 through their concave face, but in different regions of the catalytic domain of MMP-14. Each SLRPs inhibited significantly the MMP-14 activity. Finally, molecular dynamics showed the role of glycan chains in interaction with MMP-14 and shielding effect of SLRPs. Altogether, the results demonstrated that each SLRP exhibited inhibition of MMP-14 activity. However, the differential targeting of MMP-14 by the SLRPs was shown to be related not only to the core protein conformation but also to the glycan chain structures and dynamics.

 

Call for papers for a Special Issue on Extracellular matrix in « Biomaterials and Biosystems » (Elsevier)

Profs Dimitrios Zevgolis and Nikos Karamanos are putting together a Special Issue entitled ‘Extracellular matrix: The driving force of everything’ in Biomaterials and Biosystems (Elsevier). All papers will be peer-reviewed. Waived publication charges for 2022.

For more informations : Biomaterials and Biosystems | Journal | ScienceDirect.com by Elsevier

And contacts : dimitrios.zevgolis@ucd.ie; n.k.karamanos@upatras.gr; Emma.XU@elsevier.com

 

Zeinab Rekad, créatrice du nouveau logo de notre société, publie cet été une revue dans Matrix Biology : « The alternative matrisome »

Zeinab Rekad est doctorante à l’Université de Nice Côte d’Azur. Elle réalise sa thèse dans le laboratoire d’Ellen Van Obberghen-Schilling à l’Institut de Biologie Valrose. Passionnée par la biologie des ARNs et la matrice extracellulaire, elle s’intéresse aux mécanismes de régulation des interactions entre les cellules et leur matrice extracellulaire et plus spécifiquement au rôle de la protéine liant les ARNs « SAM68 » dans l’adhésion des cellules endothéliales.

Dans cet article de revue, elle décrit avec ses co-auteurs, comment les différentes formes de « splicing » alternatif des gènes codant pour le matrisome impactent les propriétés structurales et fonctionnelles de la matrice extracellulaire et sont à l’origine de sa diversité, mais aussi en quoi des altérations de ces isoformes impactent plus largement l’homéostasie tissulaire et les processus oncogéniques.

https://doi.org/10.1016/j.matbio.2022.05.003

Highlights

•Environmental factors regulate spatial and temporal splicing of matrisome genes throughout life.
•Alternative splicing of matrisome genes drives structural and functional diversification of the ECM.
•Misregulation of ECM splicing isoforms impacts tissue homeostasis and oncogenic processes.
•We describe 4 easy ways to follow bioinformatics approaches to identify ECM gene splicing in cancer.

Lack of the myotendinous junction marker col22a1 results in posture and locomotion disabilities in zebrafish

Bravo a Marilyne Malbouyres de l’équipe de Florence Ruggiero et leurs collaborateurs, pour cette publication dans Matrix Biology, qui démontre que COL22A1, codant pour un marqueur unique de la matrice extracellulaire de la jonction myotendineuse, est un nouveau gène candidat dans les myopathies humaines.

https://doi.org/10.1016/j.matbio.2022.03.002

Extrait Fig. 4. Structural analysis of 5 dpf col22a1TSPN-/− trunk muscle. Whole-mount immunofluorescence staining with antibodies against ColXXII (green) and the myosin light chain 1 marker (F310, red). Nuclei are in blue. Anterior is towards the left.

Pulsed Electric Fields Induce Extracellular Matrix Remodeling through Matrix Metalloproteinases Activation and Decreased Collagen Production

Sara Gouarderes, Camille Ober, Layal Doumard, Jany Dandurand, Patricia Vicendo, Isabelle Fourquaux, Alexander Golberg, Valérie Samouillan, Laure Gibot

J Invest Dermatol 2021 Oct 21;S0022-202X(21)02352-6. doi: 10.1016/j.jid.2021.09.025

Abstract

Impairment of extracellular matrix remodeling is observed in the tumor microenvironment or fibrosis and results in excessive collagen production and/or decreased degradation by matrix metalloproteinases (MMPs). Thanks to their local application and transient effects, physical stimuli appear as attractive tools to remodel the extracellular matrix. We assessed the potential of pulsed electric field technology, classically applied to drug delivery, to induce collagen remodeling at the tissue scale. A sophisticated in vitro tissue-engineered human dermal substitute was used to show that microsecond and millisecond pulsed electric fields induced (i) a rapid modulation (4 hours after electrostimulation) of mRNA genes composing the matrisome, particularly a downregulation of procollagens and extracellular matrix maturation enzymes such as transglutaminase 2 and lysyl oxidase like; (ii) a transient decrease in procollagens production and hydroxyproline tissue content within a week after electrostimulation; (iii) a long-lasting ROS-dependent overactivation of matrix metalloproteinases for at least 48 hours; and (iv) a downregulation of TGFβ1. These observations underpin that pulsed electric fields, a technology already approved for clinical use combined with anticancer agents, are particularly promising to provide local and effective treatment of abnormal extracellular matrix.

Lien vers l’article

Heparan-mimetics: Potential agents of tissue regeneration for bone andperiodontal therapies

Maroun Bou Karam, Joe El Khoury, Carole Chakar, Sylvie Changotade, Didier Lutomski, Nada Naaman, Gaston Godeau, Abdellatif Elm’selmi, Ronald Younes, Karim Senni

Abstract

Heparan sulfate glycosaminoglycans are key players of tissue repair and can be regarded as useful compounds for regenerative medicines. Unfortunately, their therapeutic uses face many technical, industrial, and regulatory hurdles due to their animal origin. So, some non-animal sulfated polysaccharides mimic heparan sulfate properties and offer interesting solutions to replace them. Among them, dextran derivatives, seaweed polysaccharides, or marine bacterial polysaccharides are the best known and have demonstrated their pro-regenerative capabilities
by promoting both extracellular matrix structuring and angiogenesis and limiting degenerative processes such as inflammatory cell migration or tissue proteolysis. These polysaccharides have also shown their ability to specifically promote osteoblastic differentiation and bone wound healing. Furthermore, recent works shows that heparan-mimetics can be used as an additive to improve the cytocompatibility of bone substitutes commonly used in periodontal surgery. The use of these polysaccharides can be regarded as a clever approach to improve the
biointegration of bone substitutes.

Lien vers l’article

 

Special issue: MATRIX MODELING & REMODELING

Dear colleagues,

The special issue given below is online.
Thanks to the contributions by well known authors in the field,  another key area of matrix biology has been published.
Many thanks to editor-in-chief Renato Iozzo for giving us the  opportunity and his great support during all steps of this endeavor !

I hope it will be a useful for your future research.
All the best
Nikos

Matrix Biology
Volume 75, Pages 1-330, January 2019
Matrix Modeling and Remodeling
Edited by Nikos Karamanos

Special Issue: Extracellular Matrix Control of Innate Immunity from JHC

Special Issue Preview: Extracellular Matrix Control of Innate Immunity from Journal of Histochemistry & Cytochemistry

The extracellular matrix (ECM) has long been considered a structural element whose primary role was to define the three-dimensional architecture of tissues. It is now apparent that the ECM is a dynamic structure that undergoes remodeling during tissue morphogenesis and disease to regulate diverse cellular processes, including cellular differentiation, migration and proliferation. As pointed out in the editorial by Stephen Hewitt, the study of the ECM is demanding due to the complexity of the research. Until recently, the lack of the tools required to study the ECM added to the demanding nature of this research. Through the enhancement of existing and development of new research tools and animal models, recent studies show that the ECM contributes to the extracellular-control of numerous cellular processes, providing clear evidence of its critical role in regulating tissue morphogenesis and patterning, tissue homeostasis, and pathogenesis of acute and chronic diseases.
Over the past 15 to 20 years, scientists studying innate immunity have focused on and learned a great deal about the genetic- signaling- and cellular-mechanisms regulating the innate immune response. With increased recognition that extracellular-control of cell function is important, investigators are now providing evidence that specific components of the ECM regulate many of the key processes required for the proper function of innate immunity and tissue inflammation. This includes but is not limited to activation, differentiation, migration, proliferation, and death of immune cells. Due to the emerging evidence that extracellular-control of innate immunity is important, a goal of this special issue is to detail how specific molecules of the ECM – proteoglycans, glycosaminoglycans, and tenascin-C – regulate immune cell function.
To accomplish this goal, the editors and authors of this special issue have included reviews focused on specific topics. This includes a review of select components of the ECM that are Danger Associated Molecular Patterns (DAMPs) that activate innate immune pattern recognition receptors to trigger sterile inflammation. A second review focuses on the ability of proteoglycans and specifically their glycosaminoglycan (GAG) side chains to bind to and provide fine-control of chemokine function and leukocyte migration in tissues. To provide a broader view on the role of the ECM in regulating tissue inflammation, several reviews describe how proteoglycans and GAGs shape the innate immune response in lungs, kidney, brain and intestines. The final review in this special issue details the role of the GAGs, heparan sulfate and heparin, in tissue inflammation and advances the potential development of antiinflammatory strategies using heparan sulfate/heparin biomimetics. It is our hope that the information included in this special issue of the Journal of Histochemistry and Cytochemistry provides scientists with a better understanding of the importance of the ECM in providing fine-control of innate immunity.

 

Danger-Associated Molecular Patterns Derived From the Extracellular Matrix Provide Temporal Control of Innate Immunity by Charles W. Frevert, Jessica Felgenhauer, Malgorzata Wygrecka, Madalina V. Nastase, and Liliana Schaefer

Proteoglycans as Immunomodulators of the Innate Immune Response to Lung Infection by Inkyung Kang, Mary Y. Chang, Thomas N. Wight, and Charles W. Frevert

Small Leucine-Rich Proteoglycans in Renal Inflammation: Two Sides of the Coin by Madalina V. Nastase, Andrea Janicova, Heiko Roedig, Louise Tzung-Harn Hsieh, Malgorzata Wygrecka, and Liliana Schaefer

December issue of Matrix Biology related with the 2nd Matrix Biology Europe Conf. is out

Dear Colleagues and friends,

This is to inform you that, thanks to the editor-in-chief Dr. Renato Iozzo, the December issue of Matrix Biology includes the « Matrix Biologists in Action” related with the 2nd Matrix Biology Europe Conference, held in Athens last june 2016.

The article could be downloaded here.

I hope you will enjoy it.

All the best
Nikos Karamanos

Publication eBook « Matricellular Receptors as Potential Targets in Anti-Cancer Therapeutic Strategies »

couverture-ebook-1Hervé Emonard, Stéphane Dedieu et Laurent Duca ont le plaisir de vous annoncer la publication chez Frontiers in Pharmacology et la mise en ligne d’un numéro spécial intitulé « Matricellular Receptors as Potential Targets in Anti-Cancer Therapeutic Strategies ».

Ce livre, composé d’articles de revue et de recherches originales, présente les données récentes obtenues dans l’étude des récepteurs membranaires dont les rapports, directs ou indirects, avec la matrice extracellulaire modulent le comportement cellulaire. Il fait également le point sur l’identification de ces récepteurs « matricellulaires » comme cibles thérapeutiques dans le contexte de pathologie tumorale.
De nombreux membres de la SFBMEc ont contribué à sa réalisation.

La version electronique de cet ouvrage « Matricellular Receptors as Potential Targets in Anti-Cancer Therapeutic Strategies » est consultable/téléchargeable ici.


Hervé Emonard, Stéphane Dedieu and Laurent Duca are pleased to announce the publication by Frontiers in Pharmacology of a special issue entitled « Matricellular Receptors as Potential Targets in Anti-Cancer Therapeutic Strategies ».

This book, composed of bibliographic reviews and original reports, present recent data on the cell membrane receptors which mediate signaling from the extracellular environment to modulate cell behavior. It also highlights the identification of these « matricellular » receptors as therapeutic targets in the context of tumor pathology.
Many members of the SFBMEc contributed to its realization.

The ebook « Matricellular Receptors as Potential Targets in Anti-Cancer Therapeutic Strategies » can be consulted/downloaded here.

Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis

Naba A, Clauser K.R,and Hynes R.O. Enrichment of Extracellular Matrix Proteins from Tissues and Digestion into Peptides for Mass Spectrometry Analysis. J. Vis. Exp, 2015, (101), e53057, doi:10.3791/53057

Lien vers la vidéo: ici

Lien vers le protocole: ici

The Extracellular Matrix: Tools and Insights for the “Omics” Era

Naba A, Clauser K.R, Ding H, Whittaker C.A, Carr S.A, and Hynes R.O. The Extracellular Matrix: Tools and Insights for the « Omics » Era. Matrix Biology, 2015, pii: S0945-053X(15)00121-3

Liens vers l’article (open access): http://www.sciencedirect.com/science/article/pii/S0945053X15001213

Highlights:
• The matrisome is defined as the ensemble of 1000 + genes encoding ECM and ECM-associated proteins.

• Bioinformatic and experimental approaches to study the ECM/matrisome are discussed.

• We introduce a novel website and database MatrisomeDB to centralize resources on the matrisome.

• We present a draft of an ECM atlas compiling proteomics data on the ECM of 14 different tissues and tumors.

• “Omics” data provide novel insights into ECM functions in development, homeostasis and disease.

 

Special issue of Cell Adhesion & Migration on Tenascins

Tenascins_meetingFollowing the successful meeting organized last year in May 2014, a special issue of Cell Adhesion & Migration on Tenascins: Defining their role in tissue homeostasis and cancer has been published [Volume 9, Issue 1-2, 2015]. This issue is co-edited by Kim Midwood & Gertraud Orend and you access it on the publisher’s website. The foreword signed by the co-editors is in open access.

 

 

Revue « Metalloproteinases in Medicine » (Dove Press)

Une revue est venue s’ajouter à la littérature traitant de la matrice extracellulaire : « Metalloproteinases in Medicine » (Dove Press). Cette revue s’adresse notamment à celles et ceux qui s’intéressent au remodelage protéolytique de la matrice extracellulaire. Elle est en accès libre et a commencé son premier volume en juin 2014. Son éditeur-en-chef est le Pr W.C. Parks du Cedars-Sinai Medical Center à Los Angeles et la liste complète des éditeurs associés est en  ligne ici.

Pour plus d’informations, vous pouvez consulter le site internet de l’éditeur Dove Press à cette adresse : http://www.dovepress.com/metalloproteinases-in-medicine-journal.

Notez que cette nouvelle revue n’est pas encore indexée par PudMed Central mais l’éditeur en chef annonce qu’elle sera prochainement soumise à la banque de données.

Parution de « Aging Facts and Theories » (Interdisciplinary Topics in Gerontoloy vol. 39, 2014)

Robert_Aging_Facts_Theories_BookLadislas Robert, un des fondateurs du Club Français du Tissu Conjonctif qui a été à l’origine de la Société Française de Biologie de la Matrice Extracellulaire, vient d’éditer avec T. Fulop un ouvrage intitulé « Aging Facts and Theories » (Interdisciplinary Topics in Gerontoloy vol. 39, 2014). Il a également rédigé plusieurs chapitres de cet ouvrage dont un intitulé « Aging connective tissues: experimental facts and theoritical considerations ». Je recommande la lecture de ce livre à tous ceux qui travaillent sur le vieillissement bien sûr mais aussi à tous ceux qui souhaitent parfaire leur culture scientifique.

Sylvie Ricard-Blum

 

 

Fiche descriptive de l’ouvrage à télécharger : [button link= »http://www.sfbmec.fr/wp/wp-content/uploads/2014/09/Robert_Aging_Facts_Theories_Content.pdf » icon= »download-alt » color= »#0858cf » size= »medium »] PDF [/button]

 

Volume spécial consacré aux protéoglycanes dans Matrix Biology (Proteoglycan Biology, April 2014)

Un volume spécial consacré aux protéoglycanes et édité par Liliana Schaefer vient d’être publié dans Matrix Biology (Proteoglycan Biology, volume 35, pages 1-276, April 2014). Ce volume résume les récents développements dans la biologie des protéoglycanes et du hyaluronane présentés lors de la 8ème conférence sur les protéoglycanes organisée par LiLiana Schaefer (Francfort, Allemagne) et John Couchman (Copenhague, Danemark) à Francfort du 25 au 29 août 2013. Vous pouvez le consulter à l’adresse suivante : http://www.sciencedirect.com/science/journal/0945053X/35

Extracellular matrix signatures of human mammary carcinoma identify novel metastasis promoters

Alexandra Naba, Karl R. Clauser, John M. Lamar, Steven A. Carr and Richard O. Hynes.
Extracellular matrix signatures of human mammary carcinoma identify novel metastasis promoters. eLife, 2014, 3:e01308

Lien vers l’article: http://elife.elifesciences.org/content/3/e01308

Lien vers le résumé: http://elife.elifesciences.org/content/3/e01308/abstract-2

doi: http://dx.doi.org/10.7554/eLife.01308

Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV collagen assembly in EBM

Lien

Bignon M, Pichol-Thievend C, Hardouin J, Malbouyres M, Bréchot N, Nasciutti L, Barret A, Teillon J, Guillon E, Etienne E, Caron M, Joubert-Caron R, Monnot C, Ruggiero F, Muller L, Germain S.
Lysyl oxidase-like protein-2 regulates sprouting angiogenesis and type IV collagen assembly in the endothelial basement membrane.
Blood. 2011 Oct 6;118(14):3979-89. Epub 2011 Aug 11.
PMID: 21835952
College de France, Center for Interdisciplinary Research in Biology, Paris, France.

Lien vers PubMed.

MatrixDB, the extracellular matrix interaction database.

Lien

Chautard E, Fatoux-Ardore M, Ballut L, Thierry-Mieg N, Ricard-Blum S.
MatrixDB, the extracellular matrix interaction database.
Institut de Biologie et Chimie des Protéines, UMR 5086 CNRS-Université Lyon 1, IFR 128 Biosciences Gerland-Lyon Sud, 7 passage du Vercors 69367, Lyon Cedex 07 and TIMC-IMAG/TIMB, UMR 5525 CNRS-Université Grenoble 1-Faculté de Médecine, 38706 La Tronche Cedex, France.

Lien vers PubMed.