scholarly journals Differential Expression of Extracellular Matrix Components in Nasal Polyp Endotypes

2019 ◽  
Vol 33 (6) ◽  
pp. 665-670 ◽  
Author(s):  
Xin Feng ◽  
Spencer C. Payne ◽  
Larry Borish ◽  
John W. Steinke
Keyword(s):  
Extracellular Matrix ◽  
Nasal Polyp ◽  
Collagen Iv ◽  
Disease State ◽  
Collagen I ◽  
Cellular Infiltrate ◽  
Matrix Deposition ◽  
Total Collagen ◽  
Collagen Iii ◽  
Extracellular Matrix Components

Background Chronic rhinosinusitis is a difficult-to-treat disease that is often characterized by recurrent nasal polyp (NP) growth following surgical removal. The disease has been separated into distinct phenotypes based on cellular infiltrate or underlying physiological mechanisms. NPs are composed in part of an inflammatory cellular infiltrate, blood vessels, and a large amount of extracellular matrix (ECM). Despite the recognition of prominent ECM deposition, few studies have examined the components in detail and how they might differ with disease state. Objective The purpose of this study was to quantitate the expression of ECM components in NPs. Methods NPs were stained with pico-sirius red to determine total collagen content, and immunofluorescence was used to detect collagen I, collagen III, collagen IV, fibronectin, and laminin. Expression of each was quantitated and analyzed in relation to rhinosinusitis phenotype and separately as a function of polyp eosinophil number. Results When analyzed by phenotype, collagen I, collagen III, and fibronectin were expressed at the highest levels in noneosinophilic sinus disease. Collagen IV was not different among any groups, and its location was found predominately around vessels. When analyzed as a function of polyp eosinophil number, total collagen and collagen III showed a significant inverse correlation. Conclusions NP ECM composition differs with disease state with higher expression in cases where eosinophil levels are low. This suggests that in eosinophilic polyps there is a loss of matrix deposition either through break down or a failure to produce the essential components. Understanding these differences may identify new therapeutic targets.

scholarly journals Immunohistochemical evaluation of fibrillar components of the extracellular matrix of transversalis fascia and anterior abdominal rectus sheath in men with inguinal hernia

2014 ◽  
Vol 41 (1) ◽  
pp. 23-29 ◽  
Author(s):  
Rogério De Oliveira Gonçalves ◽  
Evandro De Moraes e Silva ◽  
Gaspar De Jesus Lopes Filho
Keyword(s):  
Extracellular Matrix ◽  
Inguinal Hernia ◽  
Rectus Sheath ◽  
Staining Technique ◽  
Collagen I ◽  
Elastic Fibers ◽  
Collagen Iii ◽  
Extracellular Matrix Components ◽  
Matrix Components ◽  
Age Range

OBJECTIVE: to evaluate the role of fibrillar extracellular matrix components in the pathogenesis of inguinal hernias. METHODS: samples of the transverse fascia and of the anterior sheath of the rectus abdominis muscle were collected from 40 men aged between 20 and 60 years with type II and IIIA Nyhus inguinal hernia and from 10 fresh male cadavers (controls) without hernia in the same age range. The staining technique was immunohistochemistry for collagen I, collagen III and elastic fibers; quantification of fibrillar components was performed with an image analysis processing software. RESULTS: no statistically significant differences were found in the amount of elastic fibers, collagen I and collagen III, and the ratio of collagen I / III among patients with inguinal hernia when compared with subjects without hernia. CONCLUSION: the amount of fibrillar extracellular matrix components did not change in patients with and without inguinal hernia.

Glibenclamide prevents increased extracellular matrix formation induced by high glucose concentration in mesangial cells

2007 ◽  
Vol 292 (1) ◽  
pp. F57-F65 ◽  
Author(s):  
Giovanna Giannico ◽  
Pedro Cortes ◽  
Mohammed H. Baccora ◽  
Clare Hassett ◽  
David W. Taube ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
High Glucose ◽  
Mesangial Cells ◽  
Cell Layer ◽  
Collagen Iv ◽  
Collagen I ◽  
Metabolic Effects ◽  
Extracellular Matrix Components ◽  
Pai 1

Other than stimulation of cell contractility, little is known about the potential metabolic effects induced by sulfonylureas, independently of insulin action. Previous studies from our laboratory demonstrated complete abrogation of glomerulosclerosis in an experimental model of type 1 diabetes chronically (9 mo) treated with low-dose sulfonylureas (Biederman JI, Vera E, Pankhaniya R, Hassett C, Giannico G, Yee J, Cortes P. Kidney Int 67: 554–565, 2005). Therefore, the effects of glibenclamide (Glib) on net collagen I, collagen IV, and fibronectin medium net secretion and cell layer collagen I deposition were investigated in mesangial cells continuously exposed to 25 mM glucose for 8 wk and treated with predetermined increasing concentrations of Glib for the same period. Clinically relevant concentrations (0.01 μM) of Glib fully suppressed the high glucose-enhanced accumulation of collagen I, collagen IV, and fibronectin in the medium and inhibited collagen I deposition in the cell layer. These effects occurred while transforming growth factor (TGF)-β1 medium concentration remained elevated and glucose uptake was increased to levels above those in 25 mM glucose-incubated cultures. The decreased collagen I accumulation occurred simultaneously with enhanced collagen I mRNA expression in concert with marked suppression of plasminogen inhibitor type-1 (PAI-1) mRNA and protein expression. This strongly suggests an accelerated matrix turnover favoring breakdown. Glib-induced effects demonstrated a biphasic pattern, being absent or reversed in cells treated with higher Glib concentrations (0.1 or 1 μM). Therefore, chronic Glib treatment at low concentrations markedly diminishes the high glucose-induced enhanced accumulation of extracellular matrix components by suppression of steady-state PAI-1 transcriptional activity. These results and those previously reported in vivo suggest that long-term Glib treatment may prevent glomerulosclerosis in insulin-deficient diabetes.

scholarly journals Attachment of Actinobacillus suis H91-0380 and Its Isogenic Adhesin Mutants to Extracellular Matrix Components of the Tonsils of the Soft Palate of Swine

2016 ◽  
Vol 84 (10) ◽  
pp. 2944-2952 ◽  
Author(s):  
Adina R. Bujold ◽  
Janet I. MacInnes
Keyword(s):  
Extracellular Matrix ◽  
Soft Palate ◽  
Exponential Growth ◽  
Collagen Iv ◽  
Collagen I ◽  
Upper Respiratory Tract ◽  
Wild Type ◽  
Content Type ◽  
Extracellular Matrix Components ◽  
Actinobacillus Suis

Tonsils conduct immune surveillance of antigens entering the upper respiratory tract. Despite their immunological function, they are also sites of persistence and invasion of bacterial pathogens.Actinobacillus suisis a common resident of the tonsils of the soft palate in pigs, but under certain circumstances it can invade, causing septicemia and related sequelae. Twenty-four putative adhesins are predicted in theA. suisgenome, but to date, little is known about how they might participate in colonization or invasion. To better understand these processes, swine tonsil lysates were characterized by mass spectrometry. Fifty-nine extracellular matrix (ECM) proteins were identified, including small leucine-rich proteoglycans, integrins, and other cell surface receptors. Additionally, attachment of the wild type and 3 adhesin mutants to 5 ECM components was evaluated. Exponential cultures of wild-typeA. suisadhered significantly more than stationary cultures to all ECM components studied except collagen I. During exponential growth, theA. suisΔflp1mutant attached less to collagen IV while the ΔompAmutant attached less to all ECMs. The ΔcomE1strain attached less to collagen IV, fibronectin, and vitronectin during exponential growth and exhibited differential attachment to collagen I over short adherence time points. These results suggest that Flp1, OmpA, and ComE1 are important during early stages of attachment to ECM components found in tonsils, which supports the notion that other adhesins have compensatory effects during later stages of attachment.

Distribution of Collagen I, III, and IV and Laminin in the Human Liver during Prenatal Development

2018 ◽  
Vol 205 (3) ◽  
pp. 164-177
Author(s):  
Marko Jović ◽  
Ivan Nikolić ◽  
Vera Todorović ◽  
Aleksandar Petrović ◽  
Vladimir Petrović ◽  
...  
Keyword(s):  
Basal Membrane ◽  
First Trimester ◽  
Prenatal Development ◽  
Collagen Iv ◽  
Nerve Fibers ◽  
Collagen I ◽  
Connective Tissues ◽  
Portal Area ◽  
Collagen Iii ◽  
Extracellular Matrix Components

In the absence of systematized data on the extracellular matrix components during prenatal liver development, the present study aimed to investigate the time of appearance and distribution of collagen types I, III, and IV and laminin. The study material included embryonic and fetal livers, aged 7–37 weeks, categorized into 3 trimesters. The material was stained using hematoxylin-eosin and immunohistochemistry methods for the identification of collagen I, III, and IV and laminin. Collagen I was detected near the end of the first trimester in the capsules and walls of interlobular veins. As the liver matures, collagen I is increasingly abundant in the capsules, portal area connective tissues, arterial walls, interlobular veins, sinusoids, and central veins. Collagen III and collagen IV appear in the middle of the first trimester in the capsules, portal areas, and walls of central veins, as well as the sinusoids particularly. In trimesters 2 and 3, these collagens are increasingly present in all the structures, but collagen IV is also present in nerve fibers. Laminin is sporadically present adjacent to the sinusoids in trimester 1, while in trimesters 2 and 3 this protein commonly appears in the walls of arteries and interlobular veins, in the basal membrane of bile ducts, and in nerve fibers. The contents of collagen I, III, and IV increase during prenatal development in the liver capsule, arterial and vein walls, sinusoids, and portal area. Laminin expression is consistent with that of the collagens with the exception that, within lobules, laminin disappears with liver maturation.

scholarly journals Physiological regulation of extracellular matrix collagen and elastin in the arterial wall of rats by noradrenergic tone and angiotensin II

2011 ◽  
Vol 13 (1) ◽  
pp. 19-28 ◽  
Author(s):  
Houcine Dab ◽  
Kamel Kacem ◽  
Rafik Hachani ◽  
Nadra Dhaouadi ◽  
Wassim Hodroj ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Angiotensin Ii ◽  
Vascular Diseases ◽  
Vascular Wall ◽  
Collagen I ◽  
Ang Ii ◽  
Physiological Regulation ◽  
Collagen Iii ◽  
Wistar Kyoto

The interactions between the effects of the sympathetic nervous system (SNS) and angiotensin II (ANG II) on vascular extracellular matrix (ECM) synthesis were determined in rats. The mRNA and protein content of collagen I, collagen III and elastin in the abdominal aorta (AA) and femoral artery (FA) was investigated in Wistar–Kyoto rats treated for 5 weeks with guanethidine, a sympathoplegic, losartan, an ANG II AT1 receptor (AT1R) blocker, or both. The effects of noradrenaline (NE) and ANG II on collagen III and elastin mRNA, and the receptor involved, were tested in cultured vascular smooth muscle cells (VSMCs) in vitro. Guanethidine increased collagen types I and III and decreased elastin, while losartan had an opposite effect, although without effect on collagen III. The combination of treatments abrogated changes induced by simple treatment with collagen I and elastin, but increased collagen III mRNA in AA and not in FA. NE stimulated collagen III mRNA via β receptors and elastin via α1 and α2 receptors. ANG II stimulated collagen III but inhibited elastin mRNA via AT1R. Overall, SNS and ANG II exert opposite and antagonistic effects on major components of ECM in the vascular wall. This may be of relevance for the choice of a therapeutic strategy in vascular diseases.

Analysis of human skeletal muscle after 48 h immobilization reveals alterations in mRNA and protein for extracellular matrix components

2006 ◽  
Vol 101 (4) ◽  
pp. 1136-1148 ◽  
Author(s):  
Maria L. Urso ◽  
Angus G. Scrimgeour ◽  
Yi-Wen Chen ◽  
Paul D. Thompson ◽  
Priscilla M. Clarkson
Keyword(s):  
Gene Expression ◽  
Skeletal Muscle ◽  
Extracellular Matrix ◽  
Candidate Genes ◽  
Human Skeletal Muscle ◽  
Rt Pcr ◽  
Collagen Iii ◽  
Extracellular Matrix Components ◽  
Phosphorylated Akt ◽  
Mrna Content

We examined the effects of 48 h of knee immobilization on alterations in mRNA and protein in human skeletal muscle. We hypothesized that 48 h of immobilization would increase gene expression and respective protein products for ubiquitin-proteasome pathway (UPP) components. Also, we used microarray analysis to identify novel pathways. Biopsies were taken from the vastus muscle of five men (20.4 ± 0.5 yr) before and after 48-h immobilization. Global changes in gene expression were analyzed by use of Affymetrix GeneChips. Candidate genes were confirmed via quantitative RT-PCR. Western blotting (WB) was used to quantify protein products of candidate genes and to assess Akt pathway activation. Immunohistochemistry was used to localize proteins found to be altered when assessed via WB. The greatest percentage of genes showing altered expression with the GeneChip included genes involved in the UPP, metallothionein function, and extracellular matrix (ECM) integrity. Quantitative RT-PCR analysis confirmed increases in mRNA for UPP components [USP-6, small ubiquitin-related modifier (SUMO-1)] and the metallothioneins (MT2A, MT1F, MT1H, MT1X) and decreases in mRNA content for matrix metalloproteinases (MMP-28, TIMP-1) and ECM structural components [collagen III (COLIII) and IV (COLIV)]. Only phosphorylated Akt (Ser473, Thr308), COLIII and COLIV protein levels were significantly different postimmobilization (25, 10, 88, and 28% decrease, respectively). Immunohistochemistry confirmed WB showing decreased staining for collagens postimmobilization. Our results suggest that 48 h of immobilization increases mRNA content for components of the UPP and metallothionein function while decreasing mRNA and protein for ECM components as well as decreased phosphorylation of Akt.

scholarly journals Fibronectin Polymerization Regulates the Composition and Stability of Extracellular Matrix Fibrils and Cell-Matrix Adhesions

2002 ◽  
Vol 13 (10) ◽  
pp. 3546-3559 ◽  
Author(s):  
Jane Sottile ◽  
Denise C. Hocking
Keyword(s):  
Extracellular Matrix ◽  
Collagen I ◽  
Matrix Deposition ◽  
Matrix Adhesion ◽  
Cell Matrix ◽  
Adhesion Sites ◽  
Fibronectin Matrix ◽  
Thrombospondin 1 ◽  
Fibronectin Deposition ◽  
Cell Matrix Adhesion

Remodeling of extracellular matrices occurs during development, wound healing, and in a variety of pathological processes including atherosclerosis, ischemic injury, and angiogenesis. Thus, identifying factors that control the balance between matrix deposition and degradation during tissue remodeling is essential for understanding mechanisms that regulate a variety of normal and pathological processes. Using fibronectin-null cells, we found that fibronectin polymerization into the extracellular matrix is required for the deposition of collagen-I and thrombospondin-1 and that the maintenance of extracellular matrix fibronectin fibrils requires the continual polymerization of a fibronectin matrix. Further, integrin ligation alone is not sufficient to maintain extracellular matrix fibronectin in the absence of fibronectin deposition. Our data also demonstrate that the retention of thrombospondin-1 and collagen I into fibrillar structures within the extracellular matrix depends on an intact fibronectin matrix. An intact fibronectin matrix is also critical for maintaining the composition of cell–matrix adhesion sites; in the absence of fibronectin and fibronectin polymerization, neither α5β1 integrin nor tensin localize to fibrillar cell–matrix adhesion sites. These data indicate that fibronectin polymerization is a critical regulator of extracellular matrix organization and stability. The ability of fibronectin polymerization to act as a switch that controls the organization and composition of the extracellular matrix and cell–matrix adhesion sites provides cells with a means of precisely controlling cell-extracellular matrix signaling events that regulate many aspects of cell behavior including cell proliferation, migration, and differentiation.

scholarly journals Physioxia stimulates extra-cellular matrix deposition and increases mechanical properties of human chondrocyte-derived tissue-engineered cartilage

2020 ◽  
Author(s):  
J E Dennis ◽  
G A Whitney ◽  
J Rai ◽  
R J Fernandes ◽  
T J Kean
Keyword(s):  
Extracellular Matrix ◽  
Oxygen Tension ◽  
Atmospheric Oxygen ◽  
Cartilage Tissue ◽  
Type Ii ◽  
Matrix Deposition ◽  
Extracellular Matrix Components ◽  
Cross Links ◽  
Matrix Components ◽  
Engineered Cartilage

AbstractCartilage tissue has been recalcitrant to tissue engineering approaches. In this study, human chondrocytes were formed into self-assembled cartilage sheets, cultured in physiologic (5%) and atmospheric (20%) oxygen conditions and underwent biochemical, histological and biomechanical analysis at one- and two-months. The results indicated that sheets formed at physiological oxygen tension were thicker, contained greater amounts of glycosaminoglycans (GAGs) and type II collagen, and had greater compressive and tensile properties than those cultured in atmospheric oxygen. In all cases, cartilage sheets stained throughout for extracellular matrix components. Type II-IX-XI collagen heteropolymer formed in the neo-cartilage and fibrils were stabilized by trivalent pyridinoline cross-links. Collagen cross-links were not significantly affected by oxygen tension but increased with time in culture. Physiological oxygen tension and longer culture periods both served to increase extracellular matrix components. The foremost correlation was found between compressive stiffness and the GAG to collagen ratio.SummaryTissue-engineered cartilage formed from human articular chondrocytes produces thicker, stiffer, more extracellular-matrix rich cartilage tissue when grown under physiological (5%) vs. atmospheric oxygen (20%) tension.

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