scholarly journals The influence of peptide bioregulators on skin aging in 3D culture model

2016 ◽  
Vol 19 (1) ◽  
pp. 58-63 ◽  
Author(s):  
K. V Kozhina ◽  
E. N Volkova ◽  
I. N Saburina ◽  
Sergey G. Morozov ◽  
I. M Zurina ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
3D Culture ◽  
Dermal Fibroblasts ◽  
Extracellular Matrix Protein ◽  
Cytokeratin 19 ◽  
Collagen Type Iv ◽  
Cultured Fibroblasts ◽  
Study Results ◽  
Extracellular Matrix Components

He effect of mesotherapy injection (Meso-Wharton R199TM) on the dermal fibroblasts culture, simulating condition of (mature) aging skin cells are studied. Material and methods. The culture of 4th passage fibroblasts (P4), that corresponds to young skin fibroblasts (control) and the culture of 18th passage fibroblasts (P18), that has all the signs of aging dermal fibroblasts (predominance of large cells, slow cell division) were used. Bioactivity was assessed by cell morphology, epithelium-mesenchyme plasticity and expression of fibroblasts markers: cytokeratin 19, elastin, a-smooth muscle actin (aSMA), PCNA (proliferation marker), collagen types I, III, IV and fibronectin. The formation of spheroids occur when fibroblasts P18 are cultivating with the injection medication, on terms comparable to the formation of spheroids from P4 young fibroblasts. From culture of fibroblasts P18, that was cultured without medication, does not form the full spheroid, but aggregation of cells and their gradual destruction with necrotic masses within the unit are observed. The presence of the medication stimulates the “rejuvenation” of cells and subsequent recovery of the mesenchyme-epithelial plasticity of cultured fibroblasts due to the reduced ability to synthesize sufficient to establish the amount of intercellular contacts the extracellular matrix components (fibronectin and collagen), which affects the ability to form spheroids. Culturing spheroids formed with the medication stimulates expression of elastin, collagen type IV, fibronectin extracellular matrix protein that supports the skin elasticity and superficial cells actively express cytokeratin 19. The study results clearly demonstrate the effectiveness of mesotherapeutic treatment for skin rejuvenation.

scholarly journals The iron-regulated surface determinant B (IsdB) protein from Staphylococcus aureus acts as a receptor for the host protein vitronectin

2020 ◽  
Vol 295 (29) ◽  
pp. 10008-10022 ◽  
Author(s):  
Giampiero Pietrocola ◽  
Angelica Pellegrini ◽  
Mariangela J. Alfeo ◽  
Loredana Marchese ◽  
Timothy J. Foster ◽  
...  
Keyword(s):  
Staphylococcus Aureus ◽  
Extracellular Matrix ◽  
Matrix Protein ◽  
Wide Spectrum ◽  
Surface Proteins ◽  
Host Protein ◽  
Extracellular Matrix Protein ◽  
Bacterial Cells ◽  
Iron Starvation ◽  
Extracellular Matrix Components

Staphylococcus aureus is an important bacterial pathogen that can cause a wide spectrum of diseases in humans and other animals. S. aureus expresses a variety of virulence factors that promote infection with this pathogen. These include cell-surface proteins that mediate adherence of the bacterial cells to host extracellular matrix components, such as fibronectin and fibrinogen. Here, using immunoblotting, ELISA, and surface plasmon resonance analysis, we report that the iron-regulated surface determinant B (IsdB) protein, besides being involved in heme transport, plays a novel role as a receptor for the plasma and extracellular matrix protein vitronectin (Vn). Vn-binding activity was expressed by staphylococcal strains grown under iron starvation conditions when Isd proteins are expressed. Recombinant IsdB bound Vn dose dependently and specifically. Both near-iron transporter motifs NEAT1 and NEAT2 of IsdB individually bound Vn in a saturable manner, with KD values in the range of 16–18 nm. Binding of Vn to IsdB was specifically blocked by heparin and reduced at high ionic strength. Furthermore, IsdB-expressing bacterial cells bound significantly higher amounts of Vn from human plasma than did an isdB mutant. Adherence to and invasion of epithelial and endothelial cells by IsdB-expressing S. aureus cells was promoted by Vn, and an αvβ3 integrin-blocking mAb or cilengitide inhibited adherence and invasion by staphylococci, suggesting that Vn acts as a bridge between IsdB and host αvβ3 integrin.

scholarly journals Molecular forms, binding functions, and developmental expression patterns of cytotactin and cytotactin-binding proteoglycan, an interactive pair of extracellular matrix molecules

1988 ◽  
Vol 106 (2) ◽  
pp. 519-532 ◽  
Author(s):  
S Hoffman ◽  
KL Crossin ◽  
GM Edelman
Keyword(s):  
Extracellular Matrix ◽  
Chondroitin Sulfate ◽  
Neural Development ◽  
Matrix Protein ◽  
Expression Patterns ◽  
Developmental Expression ◽  
Extracellular Matrix Protein ◽  
Molecular Forms ◽  
Biochemical Alterations ◽  
Extracellular Matrix Components

Cytotactin is an extracellular matrix protein that is found in a restricted distribution and is related to developmental patterning at a number of neural and non-neural sites. It has been shown to bind specifically to other extracellular matrix components including a chondroitin sulfate proteoglycan (cytotactin-binding [CTB] proteoglycan) and fibronectin. Cell binding experiments have revealed that cytotactin interacts with neurons and fibroblasts. When isolated from brain, both cytotactin and CTB proteoglycan contain the HNK-1 carbohydrate epitope. Here, specific antibodies prepared against highly purified cytotactin and CTB proteoglycan were used to correlate the biochemical alterations and modes of binding of these proteins with their differential tissue expression as a function of time and place during chicken embryo development. It was found that, during neural development, both the levels of expression of cytotactin and CTB proteoglycan and of the molecular forms of each molecule varied, following different time courses. In addition, a novel Mr 250,000 form of cytotactin was detected that contained chondroitin sulfate. The intermolecular binding of cytotactin and CTB proteoglycan and the binding of cytotactin to fibroblasts were characterized further and found to be inhibited by EDTA, consistent with a dependence on divalent cations. Unlike the molecules from neural tissue, cytotactin and CTB proteoglycan isolated from non-neural tissues such as fibroblasts lacked the HNK-1 epitope. Nevertheless, the intermolecular and cellular binding activities of cytotactin isolated from fibroblast culture medium were comparable to those of the molecule isolated from brain, suggesting that the HNK-1 epitope is not directly involved in binding. Binding experiments involving enzymatically altered molecules that lack chondroitin sulfate suggested that this glycosaminoglycan is also not directly involved in binding. Although they clearly formed a binding couple, the spatial distributions of cytotactin and CTB proteoglycan in the embryo were not always coincident. They were similar in tissue sections from the cerebellum, gizzard, and vascular smooth muscle. In contrast, CTB proteoglycan was present in cardiac muscle where no cytotactin is present, and it was seen in cartilage throughout development unlike cytotactin, which was present only in immature chondrocytes. Cell culture experiments were consistent with the previous conclusion that cytotactin was specifically synthesized by glia, whereas CTB proteoglycan was specifically synthesized by neurons.(ABSTRACT TRUNCATED AT 400 WORDS)

scholarly journals Sustained β-catenin activity in dermal fibroblasts promotes fibrosis by up-regulating expression of extracellular matrix protein-coding genes

2015 ◽  
Vol 235 (5) ◽  
pp. 686-697 ◽  
Author(s):  
Emily Hamburg-Shields ◽  
Gregg J DiNuoscio ◽  
Nathaniel K Mullin ◽  
Robert Lafyatis ◽  
Radhika P Atit
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Dermal Fibroblasts ◽  
Extracellular Matrix Protein ◽  
Protein Coding ◽  
Protein Coding Genes

scholarly journals The Extracellular Matrix Protein 1 (ECM1) in Skin Biology: An Update for the Pleiotropic Action

2013 ◽  
Vol 7 (1) ◽  
pp. 29-41 ◽  
Author(s):  
Noritaka Oyama ◽  
Joseph Merregaert
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Prognostic Significance ◽  
Dermal Fibroblasts ◽  
T Cell Subsets ◽  
Extracellular Matrix Protein ◽  
Th2 Cells ◽  
Epidermal Keratinocytes ◽  
Extracellular Matrix Protein 1 ◽  
Pleiotropic Action

Extracellular matrix protein 1 (ECM1) is a secreted glycoprotein that plays a pivotal role in the structural and homeostatic biology of the skin, particularly in angiogenesis, reconstitution of basement membrane, proliferation and differentiation of epidermal keratinocytes and dermal fibroblasts, and malignant transformation. This rationale is substantiated by loss-of-function mutations in the ECM1 gene in an autosomal recessive genodermatosis lipoid proteinosis and circulating IgG autoantibodies to this molecule in a humoral autoimmune condition lichen sclerosus, both of which are counterpart disease conditions sharing comparable skin pathology. In the recent decade, considerable progress has been made in determining the in vivo function of ECM1 in animal model studies. Furthermore, underlying insights arose for the genetic predisposition in inflammatory bowel disease ulcerative colitis, acquisition of immune tolerance and allergic responses via particular T cell subsets such as CD4+CD25+ regulatory T cells and Th2 cells, regeneration of certain organs, and clinical advantages for diagnostic and prognostic significance in various cancers. Following our latest review in 2009, we now update the most recent evidences for the pleiotropic action of ECM1 in skin research, and also highlight the novel pathogenic relevance of this molecule in a variety of human disorders.

scholarly journals Gelsolin Contributes to the Motility of A375 Melanoma Cells and this Activity is Mediated by the Fibrous Extracellular Matrix Protein Profile

Cells ◽  
2021 ◽  
Vol 10 (8) ◽  
pp. 1848
Author(s):  
Ewa Mazurkiewicz ◽  
Aleksandra Makowiecka ◽  
Ewa Mrówczyńska ◽  
Iryna Kopernyk ◽  
Dorota Nowak ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Melanoma Cell ◽  
Matrix Protein ◽  
Protein Profile ◽  
Melanoma Cells ◽  
Actin Binding ◽  
Extracellular Matrix Protein ◽  
Collagen Type Iv ◽  
Type I ◽  
A375 Melanoma

Skin melanocytes reside on the basement membrane (BM), which is mainly composed of laminin, collagen type IV, and proteoglycans. For melanoma cells, in order to invade into the skin, melanocytes must cross the BM. It has been reported that changes in the composition of the BM accompany melanocytes tumorigenesis. Previously, we reported high gelsolin (GSN)—an actin-binding protein—levels in melanoma cell lines and GSN’s importance for migration of A375 cells. Here we investigate whether melanoma cells migrate differently depending on the type of fibrous extracellular matrix protein. We obtained A375 melanoma cells deprived of GSN synthesis and tested their migratory properties on laminin, collagens type I and IV, fibronectin, and Matrigel, which resembles the skin’s BM. We applied confocal and structured illuminated microscopy (SIM), gelatin degradation, and diverse motility assays to assess GSN’s influence on parameters associated with cells’ ability to protrude. We show that GSN is important for melanoma cell migration, predominantly on laminin, which is one of the main components of the skin’s BM.

scholarly journals In Vivo and In VitroExpression of Tenascin by Human Thymic Microenvironmental Cells

1995 ◽  
Vol 4 (2) ◽  
pp. 139-147 ◽  
Author(s):  
Claudia Sondermann Freitas ◽  
Jurandy Susana Patricia O'Campo Lyra ◽  
Sergio Ranto Dalmau ◽  
Wilson Savino
Keyword(s):  
Extracellular Matrix ◽  
Matrix Protein ◽  
Basement Membranes ◽  
Extracellular Matrix Protein ◽  
Thymic Epithelial Cell ◽  
Normal Infant ◽  
Cell Network ◽  
Extracellular Matrix Components

Increasing evidence reveals that extracellular matrix components can be regarded as a group of mediators in intrathymic T-cell migration and/or differentiation. Yet, little is kown about the expression and putative function of one particular extracellular matrix protein, namely, tenascin in the thymus. Herein we investigated, by means of immunocytochemistry, tenascin expression in normal infant and fetal human thymuses, as well as in cultures of thymic microenvironmental cells.In situ, tenascin distribution is restricted to the medulla and cortico-medullary regions of normal thymuses. This pattern thus differed from that of fibronectin, laminin and type IV collagen, in which subseptal basement membranes were strongly labeled. Interestingly, tenascin did not co-localize with the cytokeratin-defined thymic epithelial cell network. This was in keeping with thein vitrodata showing that tenascin-bearing cells were nonepithelial (and probably nonfibroblastic) microenvironmental elements.Studies with fetal thymuses revealed a developmentally regulated expression of tenascin, with a faint but consistent network labeling, in thymic rudiments as early as 12 weeks of gestational age, that progressed to a strong TN expression at 18 weeks of fetal development, which was similar to the distribution pattern observed thereafter, including postnatally.Our results clearly indicated that tenascin is constitutively expressed in the human thymus, since early stages of thymic ontogeny, and suggest that the cell type responsible for its secretion is a nonepithelial microenvironmental cell.

Identification of an extracellular matrix protein adhesin, EmaA, which mediates the adhesion of Actinobacillus actinomycetemcomitans to collagen

Microbiology ◽  
2004 ◽  
Vol 150 (8) ◽  
pp. 2677-2688 ◽  
Author(s):  
Keith P. Mintz
Keyword(s):  
Extracellular Matrix ◽  
Connective Tissue ◽  
Matrix Protein ◽  
Actinobacillus Actinomycetemcomitans ◽  
Extracellular Matrix Protein ◽  
Collagen Binding ◽  
Extracellular Matrix Components ◽  
Regulatory Cascades ◽  
Cofactor Biosynthesis ◽  
The Individual

Actinobacillus actinomycetemcomitans is an aetiologic agent in the development of periodontal and some systemic diseases in humans. This pathogen localizes to the underlying connective tissue of the oral cavity in individuals with periodontal disease. The adhesion of A. actinomycetemcomitans to extracellular matrix components of the connective tissue prompted this study to identify gene products mediating the interaction of A. actinomycetemcomitans to these molecules. A transposon mutagenesis system was optimized for use in A. actinomycetemcomitans and used to generate an insertional mutant library. A total of 2300 individual insertion transposon mutants were screened for changes in the adhesion to collagen and fibronectin. Mutants were identified which exhibited the following phenotypes: a decrease in collagen binding; a decrease in fibronectin binding; a decrease in binding to both proteins; and an increase in binding to both collagen and fibronectin. The identification of mutants defective in adhesion to the individual proteins indicates that distinct adhesins are expressed by this organism. Molecular analysis of these mutants implicated 11 independent loci in protein adhesion. One gene, emaA, is likely to encode a direct mediator of collagen adhesion, based on predicted protein features homologous to the collagen-binding protein YadA of Yersinia enterocolitica. EmaA was localized to the outer membrane, as expected for an adhesin. Reduction in fibronectin adhesion appeared to be influenced by abrogation of proteins involved in molybdenum-cofactor biosynthesis. Several other loci identified as reducing or increasing adhesion to both collagen and fibronectin are suggested to be involved in regulatory cascades that promote or repress expression of collagen and fibronectin adhesins. Collectively, the results support the hypothesis that A. actinomycetemcomitans host colonization involves afimbrial adhesins for extracellular matrix proteins, and that the expression of adhesion is modulated by global regulatory mechanisms.

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