scholarly journals Association of endometriosis in horses with differentiation of periglandular myofibroblasts and changes of extracellular matrix proteins

Reproduction ◽  
2001 ◽  
pp. 581-586 ◽  
Author(s):  
I Walter ◽  
J Handler ◽  
M Reifinger ◽  
C Aurich
Keyword(s):  
Extracellular Matrix ◽  
Smooth Muscle Actin ◽  
Extracellular Matrix Proteins ◽  
Collagen Type I ◽  
Collagen I ◽  
Matrix Proteins ◽  
Type I ◽  
Malignant Tumours ◽  
Normal Endometrium ◽  
Collagen Iii

Periglandular fibrosis and cystic dilation of uterine glands are associated with equine endometriosis. The presence of extracellular matrix proteins (collagen type I, III and IV, laminin and fibronectin) in healthy and endometriotic specimens was demonstrated by immunohistochemistry. The distribution of collagen I, but not collagen III, was dependent on the stage of the oestrous cycle. The arrangement of collagen I and collagen III in endometriotic specimens was similar to that in normal endometrium. In periglandular fibrosis, collagen IV, laminin and fibronectin deposition outside the basement membrane was observed. In these regions, stromal cells were characterized immunohistochemically as myofibroblasts because of their expression of a-smooth muscle actin, and occasionally tropomyosin and desmin. Periglandular differentiation of contractile cells could be interpreted as a reaction to support the extrusion of secretions in cystic dilated glands. Moreover, the changes of extracellular matrix proteins are characteristic for neoplastic lesions, although further development of endometriosis to benign or malignant tumours is not known in horses. Knowledge of the factors responsible for these fibroblastic modulations may be the key to explaining the pathogenesis of endometriosis.

Changes in extracellular matrix composition regulate cyclooxygenase-2 expression in human mesangial cells

2011 ◽  
Vol 300 (4) ◽  
pp. C907-C918 ◽  
Author(s):  
Matilde Alique ◽  
Laura Calleros ◽  
Alicia Luengo ◽  
Mercedes Griera ◽  
Miguel Ángel Iñiguez ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Collagen Type ◽  
Mesangial Cells ◽  
Collagen Type I ◽  
Collagen I ◽  
Type I ◽  
Camp Response Element ◽  
Response Element ◽  
Human Mesangial Cells ◽  
Cox 2

Glomerular diseases are characterized by a sustained synthesis and accumulation of abnormal extracellular matrix proteins, such as collagen type I. The extracellular matrix transmits information to cells through interactions with membrane components, which directly activate many intracellular signaling events. Moreover, accumulating evidence suggests that eicosanoids derived from cyclooxygenase (COX)-2 participate in a number of pathological processes in immune-mediated renal diseases, and it is known that protein kinase B (AKT) may act through different transcription factors in the regulation of the COX-2 promoter. The present results show that progressive accumulation of collagen I in the extracellular medium induces a significant increase of COX-2 expression in human mesangial cells, resulting in an enhancement in PGE2 production. COX-2 overexpression is due to increased COX-2 mRNA levels. The study of the mechanism implicated in COX-2 upregulation by collagen I showed focal adhesion kinase (FAK) activation. Furthermore, we observed that the activation of the phosphatidylinositol 3-kinase (PI3K)/AKT pathway by collagen I and collagen I-induced COX-2 overexpression was abolished by PI3K and AKT inhibitors. Additionally, we showed that the cAMP response element (CRE) transcription factor is implicated. Finally, we studied COX-2 expression in an animal model, NG-nitro-l-arginine methyl ester hypertensive rats. In renal tissue and vascular walls, COX-2 and collagen type I content were upregulated. In summary, our results provide evidence that collagen type I increases COX-2 expression via the FAK/PI3K/AKT/cAMP response element binding protein signaling pathway.

scholarly journals Evolution of tubulointerstitial fibrosis in experimental renal infection and scarring.

1998 ◽  
Vol 9 (4) ◽  
pp. 632-642 ◽  
Author(s):  
T D Hewitson ◽  
I A Darby ◽  
T Bisucci ◽  
C L Jones ◽  
G J Becker
Keyword(s):  
Smooth Muscle Actin ◽  
Tubulointerstitial Fibrosis ◽  
Collagen I ◽  
Control Group ◽  
Type I ◽  
Tubular Atrophy ◽  
Matrix Metalloproteinase 1 ◽  
Renal Tubulointerstitial Fibrosis ◽  
Collagen Iii ◽  
Renal Infection

Renal tubulointerstitial fibrosis may result from a loss of tubulointerstitial volume, which produces a disproportionate increase in the density of matrix. This study examines the relationship between fibrogenesis and collapse in scar formation after experimental renal infection. Escherichia coli were inoculated into the renal cortex of Sprague Dawley rats, with saline substituted in a control group. Glomerular, tubular, and interstitial profile areas were determined. Density of glomerular profiles was used as a measure of tubulointerstitial collapse. Collagen type I, III, and IV expression was examined by in situ hybridization and immunohistochemistry. Myofibroblasts were identified by alpha smooth muscle actin immunohistochemistry, and matrix metalloproteinase-1 (MMP-1) and MMP-2 were localized with appropriate antisera. Acute interstitial edema was followed by increasing density of glomerular profiles, paralleled by loss of interstitial volume and progressive tubular atrophy. Glomerular profile area remained unchanged. Density of glomerular profiles was not temporally related to myofibroblast accumulation. Procollagen alpha 1(I), alpha 1(III), and alpha 1(IV) transcription was focal, spatially related but temporally ordered. Collagen I, III, and IV immunostaining was increased from days 3, 24, and 100, respectively (P < 0.05 versus day 0 and day 100 saline). However, when corrected for glomerular density, collagen I immunostaining decreased between days 24 and 100, whereas collagen III and IV no longer differed from day 0. MMP staining within the lesion was confined to occasional interstitial and epithelial cells throughout. It is concluded that in this model, contraction and collapse of the tubulointerstitial parenchyma has a greater influence than new collagen production on final fibrotic density.

scholarly journals Matrilin-2 interacts with itself and with other extracellular matrix proteins

2002 ◽  
Vol 367 (3) ◽  
pp. 715-721 ◽  
Author(s):  
Dorothea PIECHA ◽  
Charlotte WIBERG ◽  
Matthias MÖRGELIN ◽  
Dieter P. REINHARDT ◽  
Ferenc DEÁK ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Basement Membrane ◽  
Extracellular Matrix Proteins ◽  
Collagen I ◽  
Matrix Proteins ◽  
Hek 293 ◽  
Protein Ligands ◽  
293 Cells ◽  
Physiological Relevance ◽  
Kd Values

Matrilin-2 is a component of extracellular filamentous networks. To study the interactions by which it can be integrated into such assemblies, full-length and truncated forms of matrilin-2 were recombinantly expressed in HEK-293 cells and purified from conditioned medium. The recombinant proteins, when used in interaction assays, showed affinity to matrilin-2 itself, but also to other collagenous and non-collagenous extracellular matrix proteins. The interaction between matrilin-2 and collagen I was studied in greater detail and could be shown to occur at distinct sites on the collagen I molecule and to have a KD of about 3×10-8M. Interactions with some non-collagenous protein ligands were even stronger, with matrilin-2 binding to fibrillin-2, fibronectin and laminin-1—nidogen-1 complexes, with KD values in the range of 10-8—10-11M. Co-localization of matrilin-2 with these ligands in the dermal-epidermal basement membrane, in the microfibrils extending from the basement membrane into the dermis, and in the dermal extracellular matrix, indicates a physiological relevance of the interactions in the assembly of supramolecular extracellular matrix structures.

β1 integrin-extracellular matrix protein interaction modulates the migratory response to chemokine stimulation

2001 ◽  
Vol 79 (4) ◽  
pp. 399-407 ◽  
Author(s):  
Priti S Shenoy ◽  
Shashi Uniyal ◽  
Kohei Miura ◽  
Christopher McColl ◽  
Tamas Oravecz ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Collagen Type ◽  
Cell Movement ◽  
Collagen Type I ◽  
Matrix Proteins ◽  
Extracellular Matrix Protein ◽  
Type I ◽  
Migratory Response ◽  
Cc Chemokine Receptor 5

It is well established that chemokines have a major role in the stimulation of cell movement on extracellular matrix (ECM) substrates. However, it is also clear that ECM substrates may influence the ability of cells to undergo migration. Using the migration chamber method, we assessed the migratory response of human embryonic kidney-293 (HEK) transfectant cells expressing the CC chemokine receptor 5 (CCR5) (HEK-CCR5) to stimulation by chemokines (macrophage inflamatory protein (MIP)-1α, MIP-1β, and regulated on activation normal-T cell expressed and secreted (RANTES)) on ECM substrates (collagen type I and fibronectin). Using filters coated with collagen (20 µg/mL), results showed that the chemokines differed in their ability to elicit cell movement according to the order MIP-1β > RANTES [Formula: see text] MIP-1α. In contrast, using filters coated with fibronectin (20 µg/mL), all three chemokines were similar in their ability to stimulate migration of HEK-CCR5 cells. In addition, the migratory response with respect to the concentrations of ECM substrates appeared biphasic; thus, chemokine-stimulated cell movement was inhibited at high ECM concentrations (100 µg/mL). To determine the involvement of β1 integrins, results showed that the migratory response to chemokine stimulation on collagen was largely inhibited by monoclonal antibody (mAb) to α2β1; however, complete inhibition required a combination of mAbs to α1β1 and α2β1. In comparison, migration on fibronectin was inhibited by mAb to α3β1 and α5β1. Our results suggest that the migratory response to CCR5 stimulation may vary quantitatively with both the CCR5 ligand (MIP-1α, MIP-1β, and RANTES), as well as the nature and concentration of the ECM substrate involved.Key words: chemokines, integrins, cell movement, extracellular matrix proteins, CCR5.

scholarly journals Effect of Captopril and Melatonin on Fibrotic Rebuilding of the Aorta in 24 Hour Light-Induced Hypertension

2013 ◽  
pp. S135-S141 ◽  
Author(s):  
K. REPOVÁ-BEDNÁROVÁ ◽  
S. AZIRIOVÁ ◽  
J. HRENÁK ◽  
K. KRAJČÍROVIČOVÁ ◽  
M. ADAMCOVÁ ◽  
...  
Keyword(s):  
Enzyme Inhibitor ◽  
Light Exposure ◽  
Continuous Light ◽  
Collagen Type I ◽  
Collagen I ◽  
Aortic Tissue ◽  
Type I ◽  
Collagen Iii ◽  
Induced Hypertension ◽  
Aortic Media

Chronic continuous light exposure leads to melatonin deficiency along with complex neurohumoral activation resulting in hypertension development in rats. The aim of this study was to show, whether continuous light induces fibrotic rebuilding of the aorta and whether the treatment with melatonin or angiotensin converting enzyme inhibitor captopril can prevent these potential alterations. In a six-week experiment, 3-month-old Wistar rats were divided into 4 groups (ten per group): controls, rats exposed to continuous light, exposed to continuous light plus treated with captopril (100 mg/kg/24 h) and exposed to continuous light plus treated with melatonin (10 mg/kg/24 h). Systolic blood pressure (SBP) and collagen type I and III in the media of thoracic aorta were measured. Continuous light induced hypertension and fibrotic rebuilding of the aorta in terms of enhancement of collagen I and III concentration in the aortic media. Both captopril and melatonin prevented SBP rise and reduced collagen III concentration in the aorta. However, only melatonin reduced collagen I and the sum of collagen I and III in the aortic tissue. We conclude that in continuous light-induced hypertension, administration of melatonin, along with SBP reduction, decreases collagen I and III concentration in the aorta. It is suggested that antifibrotic effect of melatonin may reduce the stiffness of the aorta and small arteries and beneficially influence the nature of the pulse wave and peripheral vascular resistance.

scholarly journals Stimulation of Synthesis and Lysis of Extracellular Matrix Proteins in Fibrosis Associated with Lymphedema

2021 ◽  
Vol 9 (1) ◽  
pp. 1-10
Author(s):  
Jose Maria Pereira de Godoy ◽  
Maria de Fatima Guerreiro Godoy ◽  
Henrique Jose Pereira de Godoy ◽  
Dalisio De Santi Neto
Keyword(s):  
Extracellular Matrix ◽  
Extracellular Matrix Proteins ◽  
Collagen Fibers ◽  
Matrix Proteins ◽  
Elastic Fibers ◽  
Type I ◽  
Treatment Practices ◽  
Before And After ◽  
Primary Lymphedema ◽  
Stimulation Of

Background: Fibrotic diseases pose a problem for overall health due to their chronic, progressive nature; the lack of a cure; and the fact that such conditions are largely refractory to current medical and surgical treatment practices. Objective: The aim of the present study was to report the physiological stimulation of synthesis and lysis of extracellular matrix proteins during the treatment of primary lymphedema. Material and Methods: A clinical trial was conducted involving the analysis of changes in type I and III collagen fibers and elastic fibers as well as the thickness of the epidermis and dermis in 10 histological fields. Samples were taken from the skin before and after intensive treatment using the Godoy Method® and adapted to the treatment of fibrosis in a patient with a clinical diagnosis of lower limb lymphedema. Slides were stained with orcein, hematoxylin and eosin, picrosirius red, and Gomori’s reticulin stains. Weibel’s multipoint method was used for the morphometric evaluation. The data were compared using the t-test with a 95% confidence interval. Results: Significant changes were detected in all aspects of interest (thickness of the epidermis and dermis, type I and III collagen fibers, and elastic fibers). Conclusion: The present findings demonstrate the physiological stimulation of synthesis and lysis of the main components of an extracellular matrix, such as type I and III collagen fibers and elastic fibers, as well as a reduction in the thickness of the epidermis and dermis in cases of fibrosis through adequate stimulation of the lymphatic system.

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