Alignment and Cell-Matrix Interactions of Human Corneal Endothelial Cells on Nanostructured Collagen Type I Matrices

2010 ◽  
Vol 51 (12) ◽  
pp. 6303 ◽  
Author(s):  
Rita Gruschwitz ◽  
Jens Friedrichs ◽  
Monika Valtink ◽  
Clemens M. Franz ◽  
Daniel J. Müller ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Corneal Endothelial Cells ◽  
Human Corneal Endothelial Cells ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions

Collagen type I-PLGA film as an efficient substratum for corneal endothelial cells regeneration

2016 ◽  
Vol 11 (9) ◽  
pp. 2471-2478 ◽  
Author(s):  
Eun Young Kim ◽  
Nirmalya Tripathy ◽  
Sun Ah Cho ◽  
Dongwon Lee ◽  
Gilson Khang
Keyword(s):  
Endothelial Cells ◽  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Corneal Endothelial Cells ◽  
Plga Film

scholarly journals Changes in integrin expression during chondrogenesis in vitro: an immunomorphological study.

1995 ◽  
Vol 43 (10) ◽  
pp. 1061-1069 ◽  
Author(s):  
M Shakibaei ◽  
B Zimmermann ◽  
H J Merker
Keyword(s):  
Collagen Type ◽  
Collagen Type I ◽  
Type I ◽  
Integrin Expression ◽  
Collagen Formation ◽  
Cell Matrix ◽  
Cell Type Specific ◽  
Immunomorphological Study ◽  
Cell Matrix Interactions

Integrins are receptors composed of ligand-specific alpha-chains and cell type-specific beta-chains which are involved in cell-cell and cell-matrix interactions. The distribution of alpha 1- and alpha 3-integrins as well as collagen Types I and II, was investigated by immunofluorescence and immunoelectron microscopy during chondrogenesis in organ culture after various culture periods. Mesenchymal cells from limb buds of Day 12 mouse embryos were grown at high density. Within the first 2 days of the culture period, only alpha 1-integrin could be detected. Formation of cartilage-specific matrix on Day 3 was accompanied by the occurrence of alpha 3-integrin. On Day 7, alpha 3 was present only in cartilage nodules, whereas alpha 1 was strongly expressed in the perichondrium and was more or less homogeneously distributed in the surrounding mesenchyme. On Day 14, alpha 1-integrin was again detectable in cartilage. We suggest that the change in collagen formation from Type I to Type II during chondrogenesis is accompanied by a change in integrin expression from alpha 1 to alpha 3. Conversely, dedifferentiation of chondrocytes in aging cartilage is accompanied by the occurrence of collagen Type I and alpha 1-integrin. Therefore, a strict correlation between the collagen type synthesized by the cells and the appropriate receptor presented by the cells is suggested.

Effects of collagenase-cleavage of type I collagen on alpha2beta1 integrin-mediated cell adhesion

1998 ◽  
Vol 111 (8) ◽  
pp. 1127-1135 ◽  
Author(s):  
A.J. Messent ◽  
D.S. Tuckwell ◽  
V. Knauper ◽  
M.J. Humphries ◽  
G. Murphy ◽  
...  
Keyword(s):  
Cell Adhesion ◽  
Type I Collagen ◽  
Cell Attachment ◽  
Heat Denaturation ◽  
Type I ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Triple Helices ◽  
Collagen Fragment ◽  
Cell Matrix Interactions

In this paper we show that collagenase-3 cleavage of type I collagen has a marked effect on alpha2beta1 integrin-mediated interactions with the collagen fragments generated. Isolated alpha2beta1 integrin and alpha2 integrin A-domain were found to bind to both native collagen and native 3/4 fragment and, to a lesser degree, native 1/4 fragment. Whole integrin and integrin A-domain binding were lost after heat denaturation of the collagen fragments. At physiological temperature, cell adhesion to triple-helical 3/4 fragment via alpha2beta1 integrin was still possible; however, no alpha2beta1 integrin-mediated adhesion to the 1/4 fragment was observed. Unwinding of the collagen fragment triple helices by heating to physiological temperatures prior to adsorption to plastic tissue culture plates resulted in total abrogation of HT1080 cell attachment to either fragment. These results provide significant evidence in support of a role for matrix-metalloproteinase cleavage of the extracellular matrix in modifying cell-matrix interactions.

scholarly journals Extracellular Matrix Hydrogels Promote Expression of Paxillin, a Muscle-Tendon Junction Marker

2021 ◽  
Author(s):  
Lewis S. Gaffney ◽  
Matthew B. Fisher ◽  
Donald O. Freytes
Keyword(s):  
Extracellular Matrix ◽  
Type I Collagen ◽  
Conditioned Media ◽  
Type I ◽  
Tissue Specific ◽  
Cell Matrix ◽  
Matrix Interactions ◽  
Cell Matrix Interactions ◽  
Tissue Models ◽  
Cells Cultured

AbstractMuscle and tendon injuries are prevalent and range from minor sprains and strains to traumatic, debilitating injuries. However, the interactions between these tissues during injury and recovery remain unclear. Three-dimensional tissue models that incorporate both tissues and a physiologically relevant junction between muscle and tendon may aide in understanding how the two tissues interact. Here, we use tissue specific extracellular matrix (ECM) derived from muscle and tendon to determine how cells of each tissue interact with the microenvironment of the opposite tissue resulting in junction specific features. ECM materials were derived from the achilles tendon and gastrocnemius muscle, decellularized, and processed to form tissue specific pre-hydrogel digests. C2C12 myoblasts and tendon fibroblasts were cultured in tissue-specific ECM conditioned media or encapsulated in tissue-specific ECM hydrogels to determine cell-matrix interactions and the effects on a muscle-tendon junction marker, paxillin. ECM conditioned media had only a minor effect on upregulation of paxillin in cells cultured in monolayer. However, cells cultured within ECM hydrogels had 50-70% higher paxillin expression than cells cultured in type I collagen hydrogels. Contraction of the ECM hydrogels varied by the type of ECM used. Subsequent experiments with varying density of type I collagen (and thus contraction) showed no correlation between paxillin expression and the amount of gel contraction, suggesting that a constituent of the ECM was the driver of paxillin expression in the ECM hydrogels. Using tissue specific ECM allowed for the de-construction of the cell-matrix interactions similar to muscle-tendon junctions to study the expression of MTJ specific proteins.Impact StatementThe muscle-tendon junction is an important feature of muscle-tendon units; however, despite cross-talk between the two tissue types, it is overlooked in current research. Deconstructing the cell-matrix interactions will allow the opportunity to study significant junction specific features and markers that should be included in tissue models of the muscle-tendon unit, while gaining a deeper understanding of the natural junction. This research aims to inform future methods to engineer a more relevant multi-tissue platform to study the muscle-tendon unit.

Myocarditis triggers inflammatory response in cardiac fibroblasts and profibrotic activation of myeloid and endothelial cells in mouse model of experimental autoimmune myocarditis

2020 ◽  
Vol 41 (Supplement_2) ◽  
Author(s):  
K Tkacz ◽  
E Dzialo ◽  
K Weglarczyk ◽  
M Czepiel ◽  
M Siedlar ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Collagen Type ◽  
Cardiac Fibroblasts ◽  
Myeloid Cells ◽  
Collagen Type I ◽  
Funding Source ◽  
Type I ◽  
Autoimmune Myocarditis ◽  
Experimental Autoimmune Myocarditis ◽  
Experimental Autoimmune

Abstract Background/Introduction Myocarditis, a heart-specific inflammation, is a common cause of pathological tissue remodeling and cardiac fibrosis resulting in stiffening of ventricles, functional impairment and heart failure. Immunization of susceptible mice with alpha myosin heavy chain (αMyHC) and complete Freund's adjuvant (CFA) induces CD4+ T cell-mediated experimental autoimmune myocarditis (EAM). In EAM model, resolution of acute cardiac inflammation is followed by a progressive dilated cardiomyopathy and systolic dysfunction. Purpose The aim of our study was to identify the role of resident cardiac fibroblasts, cardiac endothelial as well as inflammatory myeloid cells during the course of EAM. Methods EAM was induced by immunization with αMyHC/CFA in reporter BALB/c mice expressing EGFP under collagen type I promoter (Coll-EGFP) and RFP under a control of α-smooth muscle actin (αSMA) promoter (αSMA-RFP). Using flow cytometry analysis, cardiac cells were phenotyped and quantified at inflammatory (d19–21) and fibrotic (d40) stage of EAM. Sorted EGFP-positive cardiac fibroblasts obtained from healthy and myocarditis-positive mice (day 21 of EAM) were comparatively analyzed for the whole genome transcriptomics using the Next Generation Sequencing with read length 2x150bp and 20–30 million reads per sample. Results A massive infiltration of inflammatory CD45+CD11b+ myeloid cells (mainly CD11b+CD36+ macrophages, CD11b+CD36–Ly6GhiLy6chi neutrophils, CD11b+CD36–Ly6G–Ly6c– monocytes, CD11b+CD36–Ly6G–Ly6chi inflammatory monocytes) was observed at day 21 of EAM. Myeloid cells as well as endothelial cells showed increased production of type I collagen at day 21, which was further reduced at day 40 of EAM. At day 21, collagen-producing endothelial cells showed particularly elevated levels of adhesion molecules ICAM and VCAM. On the other hand, the total number of EGFP-positive cardiac fibroblasts remained unchanged during the course of EAM, as well as the percentage of cardiac fibroblasts positive for αSMA (myofibroblasts). Gene ontology analysis of transcripts differentially regulated in cardiac fibroblasts during acute myocarditis pointed mainly to activation of immune processes, response to stress, cytoskeletal and extracellular matrix organization. Specifically, in EAM at day 21 cardiac fibroblasts increased transcription of chemokines (Ccl6, Ccl9, Cxcl2, Cxcl3, Cxcl5, Cxcl9, Cxcl13), collagens (Col6a4, Col6a5, Col9a1, Col9a3, Col11a2, Col12a1, Col24a1, Col28a1), and genes involved in ECM biology (Bmp7, Kng2, Lgals3, Cthrc1, Cela1, Spn). Conclusions In EAM model, inflammatory myeloid and cardiac endothelial cells seem to contribute to excessive collagen type I production, whereas cardiac fibroblasts actively participate in inflammatory and profibrotic responses. Funding Acknowledgement Type of funding source: Public grant(s) – National budget only. Main funding source(s): The National Science Centre (Poland)

scholarly journals Fibrin coating of polymer vascular graft does not reduce its thromboresistance

2020 ◽  
Vol 5 (2) ◽  
pp. 22-29
Author(s):  
E. A. Velikanova ◽  
T. V. Glushkova ◽  
T. N. Akentyeva ◽  
V. G. Matveeva ◽  
M. Yu. Khanova ◽  
...  
Keyword(s):  
Endothelial Cells ◽  
Platelet Aggregation ◽  
Vascular Graft ◽  
Collagen Type ◽  
Platelet Rich Plasma ◽  
Small Diameter ◽  
Collagen Type I ◽  
Type I ◽  
Nuclear Staining ◽  
Human Coronary Artery

Aim. To evaluate biocompatibility along with adhesion and aggregation of platelets on the surface of uncoated and fibrin-coated poly(3-hydroxybutyrate- co-3-hydroxyvalerate)/poly(ε-caprolactone) (PHBV/PCL) small-diameter vascular grafts.Materials and Methods. 4 mm diameter grafts were fabricated by electrospinning from PHBV/ PCL (1:2) blend dissolved in 1,1,1,3,3,3-hexafluoro- 2-propanol. Inner wall of the grafts was produced using co-electrospinning of the polymer blend and collagen type I (5 mg/mL) from two different syringes. Fibrinogen was obtained from the blood of healthy donors by a cryoprecipitation procedure. Sterile polymer scaffolds were impregnated into a fibrinogen solution and immersed in a thrombin/calcium chloride blend for polymerization. To assess the biocompatibility of the grafts, primary human coronary artery endothelial cells were seeded on the luminal surface and counted under a fluorescence microscope after nuclear staining. Hemocompatibility was tested by incubation of the grafts with human platelet-rich plasma. Platelet aggregation was assessed using a platelet aggregation analyser. Surface morphology, platelet adhesion and activation were evaluated by scanning electron microscopy.Results. Fibrin coating promoted cell adhesion and proliferation and improved the graft biocompatibility as evidenced by a higher number of endothelial cells. Fibrin coating did not increase platelet aggregation, adhesion, and activation and therefore did not reduce the thromboresistance of vascular graft.Conclusion. The fibrin modification of polymer grafts from PHBV/PCL blend and collagen type I improves the surface biocompatibility and does not reduce its thromboresistance.

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