Relevant bibliographies by topics / ECM proteiny

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  1. Journal articles
  2. Dissertations / Theses
  3. Books
  4. Book chapters
  5. Conference papers

Academic literature on the topic 'ECM proteiny'

Author: Grafiati
Published: 28 June 2021
Last updated: 7 February 2022

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Journal articles on the topic "ECM proteiny"

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Vallet, Sylvain D., Martin N. Davis, Anna Barqué, Ali H. Thahab, Sylvie Ricard-Blum, and Alexandra Naba. "Computational and experimental characterization of the novel ECM glycoprotein SNED1 and prediction of its interactome." Biochemical Journal 478, no. 7 (April 16, 2021): 1413–34. http://dx.doi.org/10.1042/bcj20200675.

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The extracellular matrix (ECM) is a complex meshwork of proteins and an essential component of multicellular life. We have recently reported the characterization of a novel ECM protein, SNED1, and showed that it promotes breast cancer metastasis and regulates craniofacial development. However, the mechanisms by which it does so remain unknown. ECM proteins exert their functions by binding to cell surface receptors and interacting with other ECM proteins, actions that we can predict using knowledge of protein's sequence, structure, and post-translational modifications. Here, we combined in-silico and in-vitro approaches to characterize the physico-chemical properties of SNED1 and infer its putative functions. To do so, we established a mammalian cell system to produce and purify SNED1 and its N-terminal fragment, which contains a NIDO domain, and demonstrated experimentally SNED1's potential to be glycosylated, phosphorylated, and incorporated into an insoluble ECM. We also determined the secondary and tertiary structures of SNED1 and its N-terminal fragment and obtained a model for its NIDO domain. Using computational predictions, we identified 114 proteins as putative SNED1 interactors, including the ECM protein fibronectin. Pathway analysis of the predicted SNED1 interactome further revealed that it may contribute to signaling through cell surface receptors, such as integrins, and participate in the regulation of ECM organization and developmental processes. Last, using fluorescence microscopy, we showed that SNED1 forms microfibrils within the ECM and partially colocalizes with fibronectin. Altogether, we provide a wealth of information on an understudied yet important ECM protein with the potential to decipher its pathophysiological functions.
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Liu, Binghui, Ling Leng, Xuer Sun, Yunfang Wang, Jie Ma, and Yunping Zhu. "ECMPride: prediction of human extracellular matrix proteins based on the ideal dataset using hybrid features with domain evidence." PeerJ 8 (April 29, 2020): e9066. http://dx.doi.org/10.7717/peerj.9066.

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Extracellular matrix (ECM) proteins play an essential role in various biological processes in multicellular organisms, and their abnormal regulation can lead to many diseases. For large-scale ECM protein identification, especially through proteomic-based techniques, a theoretical reference database of ECM proteins is required. In this study, based on the experimentally verified ECM datasets and by the integration of protein domain features and a machine learning model, we developed ECMPride, a flexible and scalable tool for predicting ECM proteins. ECMPride achieved excellent performance in predicting ECM proteins, with appropriate balanced accuracy and sensitivity, and the performance of ECMPride was shown to be superior to the previously developed tool. A new theoretical dataset of human ECM components was also established by applying ECMPride to all human entries in the SwissProt database, containing a significant number of putative ECM proteins as well as the abundant biological annotations. This dataset might serve as a valuable reference resource for ECM protein identification.
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Papadimitriou, E., V. G. Manolopoulos, G. T. Hayman, M. E. Maragoudakis, B. R. Unsworth, J. W. Fenton, and P. I. Lelkes. "Thrombin modulates vectorial secretion of extracellular matrix proteins in cultured endothelial cells." American Journal of Physiology-Cell Physiology 272, no. 4 (April 1, 1997): C1112—C1122. http://dx.doi.org/10.1152/ajpcell.1997.272.4.c1112.

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We have identified a novel cellular action of thrombin on cultured rat adrenal medullary endothelial cells (RAMEC). Five-minute incubation of RAMEC with physiological concentrations of thrombin (<1 U/ml) caused within 3 h an increase in the basolateral deposition of the extracellular matrix (ECM) proteins fibronectin, laminin, and collagens IV and I, concomitant with a corresponding decrease in the apical release of these proteins into the medium. This shift in vectorial secretion of ECM proteins, quantitated with enzyme-linked immunoassays, was time dependent. Maximal stimulation of ECM protein deposition was observed after incubation of cells with thrombin for 5-15 min. Prolonged exposure (>1 h) to thrombin resulted in loss of proteins from the ECM. Thrombin-stimulated ECM protein deposition exhibited a bell-shaped dose dependence, peaking for all proteins at 0.25 U/ml of thrombin, and was independent of de novo mRNA or protein synthesis. Maximal amounts of deposited proteins increased between 2.5-fold (fibronectin) and 4-fold (collagen I) over baseline values. Similar results were obtained with thrombin receptor agonist peptide (TRAP), proteolytically active gamma-thrombin, and, to a lesser extent, other serine proteases such as trypsin and plasmin. A scrambled TRAP, proteolytically inactive PPACK-thrombin, DIP-thrombin, and type IV collagenase were ineffective. Together, these results suggest that the thrombin effects are mediated by proteolytic activation of the thrombin receptor. Possible involvement of the phospholipase C-signaling pathway in thrombin-mediated ECM protein deposition was also investigated. Inhibition or downregulation of protein kinase C (PKC) and chelation of intracellular or extracellular Ca2+ did not suppress, but rather enhanced, basal and thrombin-stimulated ECM protein deposition. Quantitative differences in augmentation of basolateral deposition by these treatments suggest differential regulatory pathways for individual ECM proteins. Our data indicate that, in cultured RAMEC, short-term activation of the thrombin receptor causes an increase in amounts of deposited ECM protein by a cellular signaling pathway that is independent of PKC activation and/or elevation of intracellular Ca2+.
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Di Mola, Ida, Stefano Conti, Eugenio Cozzolino, Giuseppe Melchionna, Lucia Ottaiano, Antonino Testa, Leo Sabatino, Youssef Rouphael, and Mauro Mori. "Plant-Based Protein Hydrolysate Improves Salinity Tolerance in Hemp: Agronomical and Physiological Aspects." Agronomy 11, no. 2 (February 14, 2021): 342. http://dx.doi.org/10.3390/agronomy11020342.

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Hemp (Cannabis sativa L.) is a multipurpose plant attracting increasing interest as a source for the production of natural fibers, paper, bio-building material and food. In this research we studied the agronomical performance of Cannabis sativa cv. Eletta Campana irrigated with saline water. Under those conditions, we tested the effect of protein hydrolysate (PH) biostimulant application in overcoming and/or balancing deleterious salinity effects. The results of the diverse treatments were also investigated at the physiological level, focusing on photosynthesis by means of a chlorophyll a fluorescence technique, which give an insight into the plant primary photochemical reactions. Four salinity levels of the irrigation solution (fresh water–EC0, and NaCl solutions at EC 2.0, 4.0 or 6.0 dS m−1, EC2, EC4 and EC6, respectively) were combined with 2 biostimulant treatments (untreated (control) or treated with a commercial legume-derived protein hydrolysate (LDPH)). The increasing salinity affected plant photochemistry resulting in lower plant growth and seed production, while the LDPH biostimulant showed a protective effect, which improved crop performance both in control and in salinity conditions. The LDPH treatment improved seeds yield (+38.6% on average of all treated plants respect to untreated plants), as well as residual biomass, relevant in fiber production.
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Liem, David A., Sanjana Murali, Dibakar Sigdel, Yu Shi, Xuan Wang, Jiaming Shen, Howard Choi, et al. "Phrase mining of textual data to analyze extracellular matrix protein patterns across cardiovascular disease." American Journal of Physiology-Heart and Circulatory Physiology 315, no. 4 (October 1, 2018): H910—H924. http://dx.doi.org/10.1152/ajpheart.00175.2018.

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Extracellular matrix (ECM) proteins have been shown to play important roles regulating multiple biological processes in an array of organ systems, including the cardiovascular system. Using a novel bioinformatics text-mining tool, we studied six categories of cardiovascular disease (CVD), namely, ischemic heart disease, cardiomyopathies, cerebrovascular accident, congenital heart disease, arrhythmias, and valve disease, anticipating novel ECM protein-disease and protein-protein relationships hidden within vast quantities of textual data. We conducted a phrase-mining analysis, delineating the relationships of 709 ECM proteins with the 6 groups of CVDs reported in 1,099,254 abstracts. The technology pipeline known as Context-Aware Semantic Online Analytical Processing was applied to semantically rank the association of proteins to each CVD and all six CVDs, performing analyses to quantify each protein-disease relationship. We performed principal component analysis and hierarchical clustering of the data, where each protein was visualized as a six-dimensional vector. We found that ECM proteins display variable degrees of association with the six CVDs; certain CVDs share groups of associated proteins, whereas others have divergent protein associations. We identified 82 ECM proteins sharing associations with all 6 CVDs. Our bioinformatics analysis ascribed distinct ECM pathways (via Reactome) from this subset of proteins, namely, insulin-like growth factor regulation and interleukin-4 and interleukin-13 signaling, suggesting their contribution to the pathogenesis of all six CVDs. Finally, we performed hierarchical clustering analysis and identified protein clusters predominantly associated with a targeted CVD; analyses of these proteins revealed unexpected insights underlying the key ECM-related molecular pathogenesis of each CVD, including virus assembly and release in arrhythmias. NEW & NOTEWORTHY The present study is the first application of a text-mining algorithm to characterize the relationships of 709 extracellular matrix-related proteins with 6 categories of cardiovascular disease described in 1,099,254 abstracts. Our analysis informed unexpected extracellular matrix functions, pathways, and molecular relationships implicated in the six cardiovascular diseases.
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Hoke, David E., Suhelen Egan, Paul A. Cullen, and Ben Adler. "LipL32 Is an Extracellular Matrix-Interacting Protein of Leptospira spp. and Pseudoalteromonas tunicata." Infection and Immunity 76, no. 5 (February 19, 2008): 2063–69. http://dx.doi.org/10.1128/iai.01643-07.

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ABSTRACT LipL32 is the major outer membrane protein in pathogenic Leptospira. It is highly conserved throughout pathogenic species and is expressed in vivo during human infection. While these data suggest a role in pathogenesis, a function for LipL32 has not been defined. Outer membrane proteins of gram-negative bacteria are the first line of molecular interaction with the host, and many have been shown to bind host extracellular matrix (ECM). A search for leptospiral ECM-interacting proteins identified the major outer membrane protein, LipL32. To verify this finding, recombinant LipL32 was expressed in Escherichia coli and was found to bind Matrigel ECM and individual components of ECM, including laminin, collagen I, and collagen V. Likewise, an orthologous protein found in the genome of Pseudoalteromonas tunicata strain D2 was expressed and found to be functionally similar and immunologically cross-reactive. Lastly, binding activity was mapped to the C-terminal 72 amino acids. These studies show that LipL32 and an orthologous protein in P. tunicata are immunologically cross-reactive and function as ECM-interacting proteins via a conserved C-terminal region.
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Chan, Gek Cher, Diana G. Eng, Jeffrey H. Miner, Charles E. Alpers, Kelly Hudkins, Anthony Chang, Jeffrey W. Pippin, and Stuart J. Shankland. "Differential expression of parietal epithelial cell and podocyte extracellular matrix proteins in focal segmental glomerulosclerosis and diabetic nephropathy." American Journal of Physiology-Renal Physiology 317, no. 6 (December 1, 2019): F1680—F1694. http://dx.doi.org/10.1152/ajprenal.00266.2019.

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In healthy glomeruli, parietal epithelial cell (PEC)-derived extracellular matrix (ECM) proteins include laminin-β1, perlecan, and collagen type IV-α2 and podocyte-specific ECM proteins include laminin-β2, agrin, and collagen type IV-α4. This study aimed to define individual ECM protein isoform expression by PECs in both experimental and human focal segmental glomerulosclerosis (FSGS) and diabetic nephropathy (DN) and to determine if changes were CD44 dependent. In experimental FSGS induced with a cytotoxic podocyte antibody and in the BTBR ob/ob mouse model of DN, PEC-derived protein staining was significantly increased in PECs. Dual staining also showed de novo expression of the podocyte-specific ECM proteins laminin-β2 and agrin in PECs. Similar findings were observed in biopsies from patients with FSGS and DN. Increases in individual ECM proteins colocalized with CD44 in PECs in disease. To determine the role of CD44, FSGS was induced in CD44−/− and CD44+/+ mice. PEC staining for perlecan, collagen type IV-α2, laminin-β2, and agrin were significantly lower in diseased CD44−/− mice compared with diseased CD44+/+ mice. These results show that in experimental and human FSGS and DN, PECs typically in an activated state, produce both PEC-derived and podocyte-specific ECM protein isoforms, and that the majority of these changes were dependent on CD44.
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Lipp, Sarah N., Kathryn R. Jacobson, David S. Hains, Andrew L. Schwarderer, and Sarah Calve. "3D Mapping Reveals a Complex and Transient Interstitial Matrix During Murine Kidney Development." Journal of the American Society of Nephrology 32, no. 7 (April 19, 2021): 1649–65. http://dx.doi.org/10.1681/asn.2020081204.

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BackgroundThe extracellular matrix (ECM) is a network of proteins and glycosaminoglycans that provides structural and biochemical cues to cells. In the kidney, the ECM is critical for nephrogenesis; however, the dynamics of ECM composition and how it relates to 3D structure during development is unknown.MethodsUsing embryonic day 14.5 (E14.5), E18.5, postnatal day 3 (P3), and adult kidneys, we fractionated proteins based on differential solubilities, performed liquid chromatography–tandem mass spectrometry, and identified changes in ECM protein content (matrisome). Decellularized kidneys were stained for ECM proteins and imaged in 3D using confocal microscopy.ResultsWe observed an increase in interstitial ECM that connects the stromal mesenchyme to the basement membrane (TNXB, COL6A1, COL6A2, COL6A3) between the embryo and adult, and a transient elevation of interstitial matrix proteins (COL5A2, COL12A1, COL26A1, ELN, EMID1, FBN1, LTBP4, THSD4) at perinatal time points. Basement membrane proteins critical for metanephric induction (FRAS1, FREM2) were highest in abundance in the embryo, whereas proteins necessary for integrity of the glomerular basement membrane (COL4A3, COL4A4, COL4A5, LAMB2) were more abundant in the adult. 3D visualization revealed a complex interstitial matrix that dramatically changed over development, including the perinatal formation of fibrillar structures that appear to support the medullary rays.ConclusionBy correlating 3D ECM spatiotemporal organization with global protein abundance, we revealed novel changes in the interstitial matrix during kidney development. This new information regarding the ECM in developing kidneys offers the potential to inform the design of regenerative scaffolds that can guide nephrogenesis in vitro.
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Ghanemi, Abdelaziz, Mayumi Yoshioka, and Jonny St-Amand. "Secreted Protein Acidic and Rich in Cysteine: Metabolic and Homeostatic Properties beyond the Extracellular Matrix Structure." Applied Sciences 10, no. 7 (April 1, 2020): 2388. http://dx.doi.org/10.3390/app10072388.

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An extracellular matrix (ECM) is a network of numerous macromolecules that represents the cellular structural support involved in key biofunctions such as signal transduction and cellular adhesion. In addition, ECM-associated proteins interact with ECM and with other endogenous structures and molecules to control cellular growth, structural modifications, cellular migration, etc. Among the ECM-associated proteins, secreted protein acidic and rich in cysteine (SPARC) is a protein that is known to be expressed when tissues change. Herein, we put a spotlight on selected, metabolic and homeostatic properties beyond the known properties of ECM and SPARC. Importantly, the synchronization of the metabolic and structural implications of SPARC and the ECM would indicate an adaptation of the metabolism to meet the needs of the changes that the tissues undergo. Highlighting such properties would have important applications in diverse fields that include therapeutics, metabolics, and pathogenesis.
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Curtis, Patrick D., James Atwood, Ron Orlando, and Lawrence J. Shimkets. "Proteins Associated with the Myxococcus xanthus Extracellular Matrix." Journal of Bacteriology 189, no. 21 (August 31, 2007): 7634–42. http://dx.doi.org/10.1128/jb.01007-07.

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ABSTRACT Fruiting body formation of Myxococcus xanthus, like biofilm formation of many other organisms, involves the production of an extracellular matrix (ECM). While the polysaccharide component has been studied, the protein component has been largely unexplored. Proteins associated with the ECM were solubilized from purified ECM by boiling with sodium dodecyl sulfate and were identified by liquid chromatography-tandem mass spectrometry of tryptic fragments. The ECM is enriched in proteins of novel function; putative functions were assigned for only 5 of the 21 proteins. Thirteen putative ECM proteins had lipoprotein secretion signals. The genes for many ECM proteins were disrupted in the wild-type (WT), fibA, and pilA backgrounds. Disruption of the MXAN4860 gene had no effect in the WT or fibA background but in the pilA background resulted in a 24-h delay in aggregation and sporulation compared to its parent. The results of this study show that the M. xanthus ECM proteome is diverse and novel.
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Dissertations / Theses on the topic "ECM proteiny"

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Dvořák, Pavel. "Biomedicínské aplikace polykaprolaktonových nanovlákenných membrán." Master's thesis, Vysoké učení technické v Brně. Fakulta chemická, 2021. http://www.nusl.cz/ntk/nusl-444549.

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The diploma thesis deals with the treatment of polycaprolactone (PCL) nanofibers. PCL fibers were subjected to the deposition of plasma amine polymers in a low pressure pulsed radiofrequency capacitively coupled discharge using cyclopropylamine monomer (CPA). Collagen as an extracellular matrix (ECM) protein was immobilized and cell proliferation on the modified nanofiber surface was monitored. Untreated PCL fibers were also subjected to the deposition of an antibacterial copper layer, and the fibers were characterized by scanning electron microscopy (SEM), X-ray photoelectron spectroscopy (XPS), and energy dispersive spectroscopy (EDX).
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Gründel, Anne. "Funktion glykolytischer Enzyme von Mycoplasma pneumoniae in der Wirt-Erreger-Interaktion." Doctoral thesis, Saechsische Landesbibliothek- Staats- und Universitaetsbibliothek Dresden, 2016. http://nbn-resolving.de/urn:nbn:de:bsz:14-qucosa-213500.

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Mycoplasma pneumoniae ist ein parasitär lebendes Bakterium, das eine atypische Pneumonie beim Menschen verursacht. Aufgrund seiner geringen Genomgröße besitzt dieser Organismus einen eingeschränkten Metabolismus sowie eine limitierte Zahl an Pathogenitätsfaktoren. Dennoch ist dieser Mikroorganismus perfekt an seinen Wirt angepasst und es war zu vermuten, dass neben dem komplexen Adhäsionsapparat von M. pneumoniae auch glykolytische Enzyme eine Rolle bei der Interaktion mit humanen Zellen spielen. Diese Enzyme sind maßgeblich bei intrazellulär ablaufenden Stoffwechselprozessen beteiligt. Es wurde jedoch bereits bei anderen Bakterien gezeigt, dass glykolytische Enzyme ebenfalls auf der Bakterienoberfläche zu finden sind und dort mit Komponenten der extrazellulären Matrix des Wirtes interagieren können. Dieser Vorgang trägt offensichtlich zur erfolgreichen Kolonisation des Wirtes bei. Ziel dieser Arbeit war es, alle glykolytischen Enzyme von M. pneumoniae hinsichtlich ihrer Lokalisierung zu beschreiben und Teilaspekte ihrer Funktion in der Interaktion mit Wirtskomponenten zu analysieren. Die glykolytischen Enzyme wurden rekombinant produziert und für die Herstellung von monospezifischen polyklonalen Antikörpern verwendet. Die Lokalisation der Enzyme wurde durch Nachweis in der Membran- und Zytosolfraktion des M. pneumoniae Gesamtantigens untersucht. Mittels Immunfluoreszenz, Colony Blot und Protease-Verdau intakter Bakterienzellen wurde bestätigt, dass acht (Glycerinaldehyd-3-phosphat-Dehydrogenase, Lactatdehydrogenase, Transketolase, Pyruvatdehydrogenase, Phosphoglyceratmutase und Pyruvatdehydrogenase Untereinheiten A-C) der 19 glykolytischen Enzyme mit der Bakterienoberfläche assoziiert vorkommen. Die Untersuchung von Mutanten ergab, dass die Lokalisation der Enzyme nicht an das Vorkommen der für die Anheftung der Bakterien an Zielstrukturen wesentlichen Adhäsine wie die Proteine P1, P40 und P90 sowie das Oberflächenprotein P01, gekoppelt ist. Jedoch sind sowohl intakte Zellen von M. pneumoniae als auch die oberflächenlokalisierten glykolytischen Enzyme in der Lage, an verschiedene humane Zellen zu binden. Eine Analyse der nachweisbaren Proteine auf der Oberfläche der Zellen führte zur Auswahl von sechs humanen Proteinen für weiterführende Studien: Plasminogen, Vitronektin, Fibronektin, Fibrinogen, Laminin und Laktoferrin. Mittels ELISA wurde eine konzentrationsabhängige Bindung der oberflächenassoziierten Enzyme von M. pneumoniae mit Wirtsproteinen festgestellt, die hinsichtlich der Intensität jedoch Unterschiede aufwies. So konnten ausgeprägte Interaktionen aller Enzyme mit humanem Plasminogen und Vitronektin nachgewiesen werden. Die Bindung von Fibronektin und Laktoferrin ist dagegen nur für einen Teil der glykolytischen Enzyme zu bestätigen. Die Untersuchung verschiedener Einflussfaktoren ergab, dass alle Bindungen zwischen glykolytischen Enzymen und humanen Proteinen spezifisch durch die entsprechenden Antiseren gehemmt werden und dass der Großteil der Interaktionen ionischen Wechselwirkungen unterliegt. Die Bindung zu Plasminogen basiert überwiegend auf Lysin-Resten. Untersuchungen, ob sich die glykolytischen Enzyme gegenseitig in der Bindung zu Wirtsfaktoren beeinflussen, ergab ein komplexes Muster, das hinsichtlich Plasminogen, Fibronektin und Laminin für eine Überlagerung der für die Interaktion maßgeblichen Proteinbereiche spricht. Die Untersuchung einer möglichen Aktivierung von inaktivem Plasminogen zu proteolytisch aktivem Plasmin ergab, dass in Gegenwart aller oberflächenlokalisierten glykolytischen Enzyme von M. pneumoniae Plasmin gebildet wird. Es wurden jedoch Unterschiede im Aktivierungspotenzial nachgewiesen. Die Pyruvatdehydrogenase Untereinheit B zeigte die höchste, die Pyruvatdehydrogenase Untereinheit C die geringste Plasminproduktion. Die Verwendung des gewebespezifischen Plasminogenaktivators führte zu einer höheren Aktivierung als der Urokinase-Typ Plasminogenaktivator. Die Variabilität der Plasminproduktion kann mit der unterschiedlichen Bindungsaffinität der glykolytischen Enzyme zu Plasminogen begründet werden. So besitzt die Pyruvatdehydrogenase Untereinheit B im Vergleich mit der Pyruvatdehydrogenase Untereinheit C ein höheres Bindepotenzial, das sich in der gemessenen Aktivierung widerspiegelt. Die Bildung von Plasmin kann zum Abbau verschiedener extrazellulärer Matrix-Proteine führen. Diese Prozesse sind physiologisch, z. B. in der Fibrinolyse, von Bedeutung. Während in Gegenwart der glykolytischen Enzyme die humanen Proteine Laktoferrin, Laminin und Fibronektin nicht abgebaut wurde, konnte Fibrinogen in Gegenwart der Pyruvatdehydrogenase Untereinheit B bzw. der Phosphoglyceratmutase und Vitronektin durch alle glykolytischen Enzyme (bis auf die Pyruvatdehydrogenase Untereinheit C) degradiert werden. Mit der erstmals durchgeführten Analyse aller glykolytischen Enzyme eines Mikroorganismus hinsichtlich ihrer Lokalisation und der Bindung zu Komponenten der humanen extrazellulären Matrix wurde ein komplexes Netzwerk an Wirt-Erreger-Interaktionen nachgewiesen.
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Owen, Jo. "Structural and functional studies of fibulin-1 EGF domains." Thesis, University of Oxford, 2002. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.270656.

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López, Ceballos Pablo. "Elucidating how protein turnover in cell-ECM adhesion stabilizes tissue structure during development." Thesis, University of British Columbia, 2016. http://hdl.handle.net/2429/57622.

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Morphogenesis is the process by which cells rearrange to form complex three dimensional structures. Cell to extracellular matrix (ECM) adhesion, primarily mediated by Integrins, is essential for the formation and maintenance of tissue architecture. A critical way to regulate cell-ECM adhesion is by modulating the turnover of Integrins and their adhesion complex, and thereby modulating the stability of Integrin-based adhesions. We previously showed that mechanical force stabilizes Integrin-based adhesions during development by modulating Integrin turnover. Here, we extend our studies to understand how mechanical stress impacts the dynamics of the cytoplasmic adaptor protein Talin, a critical regulator of Integrin function. Using Fluorescence Recovery After Photobleaching (FRAP) analysis in combination with a newly developed mathematical model that encompasses the complexities of Talin turnover, we determined that mechanical force stabilizes cell-ECM adhesion by increasing the rate of assembly of Talin-mediated adhesion complexes. To dissect the mechanisms that regulate Talin turnover downstream of mechanical force, we used point mutations of Talin which abrogate specific functions of the Integrin adhesion complex and measured turnover kinetics. We found that the activation of Integrins, resulting in increased affinity for ECM ligands, is a crucial process to regulate adhesion complex turnover. To further investigate the role of Integrin activation in regulating adhesion stability, we introduced small molecules known to induce “outside-in activation” of Integrins in vitro into live, intact embryos. This approach revealed that outside-in activation stabilizes cell-ECM adhesion by decreasing Integrin endocytosis; similarly to what we have previously seen when mechanical force is increased. Based on this finding, we propose that mechanical force may induce changes in Integrin activation in order to stabilize cell-ECM adhesions. Overall, we show that Integrin activation is a key mechanism that regulates cell-ECM adhesion stabilization during embryogenesis.
Medicine, Faculty of
Graduate
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Osta, Muhammad Samir Ahmed. "Characterisation of ECM protein processing mechanisms underlying simple peritoneal sclerosis and encapsulating peritoneal sclerosis." Thesis, University of Sheffield, 2015. http://etheses.whiterose.ac.uk/11406/.

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Introduction and hypothesis: Peritoneal dialysis (PD) is an important option for renal replacement therapy. Peritoneal sclerosis (PS) limits PD duration due to loss of ultrafiltration (UF) capacity, while about 3% of PD patients experience a condition termed encapsulating peritoneal sclerosis (EPS). In many fibrotic diseases reduced Extracellular matrix (ECM) breakdown due to lowered matrix metalloproteinase (MMP) activity occurs, often from over-expression of tissue inhibitors of MMP (TIMPs) that underlie fibrotic remodeling. Furthermore, recent application of 2D gel proteomics on peritoneal dialysis effluent (PDE) samples has identified several proteins that are elevated in patients with membrane damage. These observations have led to the hypothesis that: changes in proteins in PDE samples, in particular those associated with ECM breakdown have value as non-invasive biomarkers of PS and the switch to EPS. To test this hypothesis, PDE samples from 3 patient cohorts was analysed for ECM proteolytic activity. A range of ECM processing proteins and 3 proteins identified from previous proteomic studies of patients developing EPS (intellectin-1, dermatopontin and collagen α1 (I)) were analysed in PDE samples. Methods: Three patient cohorts were studied: two were from Sheffield Kidney Institute (SKI) that consisted of 32 spot PDE samples (SKI-1) that included 1 EPS patient & 51 PDE & plasma samples collected during a peritoneal equilibrium test (PET) with multiple dwell times in patients who did not have EPS (SKI-2). The third cohort consisted of 209 samples from the Global Fluid Study (GFS) including sequential samples from 12 EPS & 42 matched controls patients. MMP activity was assessed using the ENZchek assay system. Plasmin activity was assessed by using cleavage of the V0882 substrate. TIMPs, MMPs, intelectin-1, dermatopontin, and collagen (α1) I were quantified by commercial ELISA in PDE and plasma samples. PDE cytology (macrophages, leukocytes, fibroblasts and mesothelial cells) was performed to determine if changes in any protein could be associated with changes in cell types. Clinical data were recovered from either the peritoneal dialysis database (PDDB) at Sheffield or the GFS archives. The analysis was performed using Microsoft Excel 2010 software, SPSS, and Graphpad prism (prism 5.01 for windows). Results: Plasmin activity in PDE samples decreases with long duration of PD therapy. Minimal MMP activity was found in all PDE samples. In the SKI-1 cohort, MMP-1, -9, & -13 were almost undetectable with only MMP-2 & -3 being measurable with levels of ((mean±SD) 46±37 & 2.1±2.2 ng/mL respectively). In contrast TIMP-1 and TIMP-2 and to lesser extent TIMP-3 had significant levels in PDE samples from commencing PD (109±88, 17±12, and 0.28±0.33 ng/mL respectively). All TIMPs & MMP-2 were raised in the single patient who had a diagnosis of EPS. In samples from the GFS cohort, there was a rapid 6 fold increases in TIMP-1 within 100 days of the diagnosis of EPS, which when normalised to TIMP-2 levels was a good predictor of EPS. Calculation of the plasma to dialysate transfer rate by reference to that of circulating proteins with no peritoneal production and of known molecular weight (albumin, beta2microglobulin (B2M), transferrin, IgG, and creatinine) demonstrated that TIMPs & MMPs (especially TIMP-1 and MMP-2) have significant peritoneal production. Plasma levels for TIMP-1,-2, MMP-2,-3, and intelectin-1 (mean±SD) were 121±27, 85±16, 176±35, 11±5, and 374±136 ng/mL in healthy individuals respectively. Plasma levels in PD patients for TIMP-1,-2, MMP-2,-3, and intelectin-1 (mean±SD) were 297±78, 158±33, 309±112, 42±28, and 749 ±722 ng/mL respectively. None of the proteins identified by proteomics as predictors of EPS were able to be validated by ELISA. However TIMP-1,-2, MMP-2, intelectin-1, and collagen (α1) I in PDE samples had significant correlations with the loss of ultrafiltration and thus membrane damage. PDE cytology showed that peritoneal fibroblast and leukocyte numbers increase with time on PD, while peritoneal macrophage decreases with time on PD. There were no significant changes in mesothelial cells. Conclusions: Negligible MMP activity in PDE samples results from high TIMP levels which could underlie the development of PS. The rapid increase in TIMP-1 within 100 days of EPS development offers value as a diagnostic tool or a late biomarker. Plasma levels of TIMP-1,2, MMP-2,3, and intelectin-1 are higher in patients on PD compare to healthy individuals. The increase in peritoneal fibroblasts may be a source of TIMP-1.
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Lundberg, Ida. "Fibroblasts and ECM in colorectal cancer : Analysis of subgroup specific protein expression and matrix arrangement." Thesis, Umeå universitet, Patologi, 2012. http://urn.kb.se/resolve?urn=urn:nbn:se:umu:diva-85606.

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The tumor microenvironment is important for tumor growth and progression, where the cancer associated fibroblast (CAF) is one central cell type. The CpG island methylator phenotype (CIMP) divides colorectal cancer (CRC) into three subgroups and in this study we investigate how the different CIMP-groups and adjacent fibroblasts affect each other. This was done with the aim of finding CIMP-specific markers and to see if different tumor-fibroblast interactions result in differently invasive tumors. Here we report that CIMP-negative tumors have increased expression of fibronectin, while CIMP-high tumors have reduced expression of E-cadherin, findings that were seen in both tumor tissue samples and tumor cell lines. We also show that CIMP-negative and CIMP-high cancer cells induce an alignment of the fibronectin fibers produced by the fibroblasts and that CIMP-high cancer cells migrate with directionality on these matrices. These findings indicate that the different tumor subgroups in fact induce different phenotypes in CAFs, resulting in CIMP-specific markers. They also indicate that CIMP-negative and CIMP-high tumors may induce an alignment of fibronectin in order to promote cancer cell migration and thereby also tumor invasion.
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Waters, Timothy Richard. "Studies on the Eco RV restriction endonuclease using oligodeoxynucleotides containing modified bases." Thesis, University of Southampton, 1992. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.385336.

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Chan, Ien. "The role of extracellular matrix protein 1 (ECM1) in human skin." Thesis, King's College London (University of London), 2006. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.423043.

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Tian, Wang, la Vega Montserrat Rojo de, Cody J. Schmidlin, Aikseng Ooi, and Donna D. Zhang. "Kelch-like ECH-associated protein 1 (KEAP1) differentially regulates nuclear factor erythroid-2–related factors 1 and 2 (NRF1 and NRF2)." AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC, 2018. http://hdl.handle.net/10150/627124.

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Nuclear factor erythroid-2-related factor 1 (NRF1) and NRF2 are essential for maintaining redox homeostasis and coordinating cellular stress responses. They are highly homologous transcription factors that regulate the expression of genes bearing antioxidant-response elements (AREs). Genetic ablation of NRF1 or NRF2 results in vastly different phenotypic outcomes, implying that they play different roles and may be differentially regulated. Kelch-like ECH-associated protein 1 (KEAP1) is the main negative regulator of NRF2 and mediates ubiquitylation and degradation of NRF2 through its NRF2-ECH homology-like domain 2 (Neh2). Here, we report that KEAP1 binds to the Neh2-like (Neh2L) domain of NRF1 and stabilizes it. Consistently, NRF1 is more stable in KEAP1(+/+) than in KEAP1(-/-) isogenic cell lines, whereas NRF2 is dramatically stabilized in KEAP1(-/-) cells. Replacing NRF1's Neh2L domain with NRF2's Neh2 domain renders NRF1 sensitive to KEAP1-mediated degradation, indicating that the amino acids between the DLG and ETGE motifs, not just the motifs themselves, are essential for KEAP1-mediated degradation. Systematic site-directed mutagenesis identified the core amino acid residues required for KEAP1-mediated degradation and further indicated that the DLG and ETGE motifs with correct spacing are insufficient as a KEAP1 degron. Our results offer critical insights into our understanding of the differential regulation of NRF1 and NRF2 by KEAP1 and their different physiological roles.
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Thorogood, Harry. "The Eco RV restriction endonuclease : an investigation using resonance raman spectroscopy and oligonucleotide phosphorothioates." Thesis, University of Newcastle Upon Tyne, 1996. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.361576.

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Books on the topic "ECM proteiny"

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Lennon, Rachel, and Neil Turner. The molecular basis of glomerular basement membrane disorders. Edited by Neil Turner. Oxford University Press, 2018. http://dx.doi.org/10.1093/med/9780199592548.003.0320_update_001.

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The glomerular basement membrane (GBM) is a condensed network of extracellular matrix molecules which provides a scaffold and niche to support the function of the overlying glomerular cells. Within the glomerulus, the GBM separates the fenestrated endothelial cells, which line capillary walls from the epithelial cells or podocytes, which cover the outer aspect of the capillaries. In common with basement membranes throughout the body, the GBM contains core components including collagen IV, laminins, nidogens, and heparan sulphate proteoglycans. However, specific isoforms of these proteins are required to maintain the integrity of the glomerular filtration barrier.Across the spectrum of glomerular disease there is alteration in glomerular extracellular matrix (ECM) and a number of histological patterns are recognized. The GBM can be thickened, expanded, split, and irregular; the mesangial matrix may be expanded and glomerulosclerosis represents a widespread accumulation of ECM proteins associated with loss of glomerular function. Whilst histological patterns may follow a sequence or provide diagnostic clues, there remains limited understanding about the mechanisms of ECM regulation and how this tight control is lost in glomerular disease. Monogenic disorders of the GBM including Alport and Pierson syndromes have highlighted the importance of both collagen IV and laminin isoforms and these observations provide important insights into mechanisms of glomerular disease.
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Zdeněk, Deyl, ed. Advanced chromatographic and electromigration methods in biosciences. Amsterdam: Elsevier, 1998.

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Book chapters on the topic "ECM proteiny"

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Brancaccio, Mara, Emila Turco, and Emilio Hirsch. "Tissue-Specific KO of ECM Proteins." In Methods in Molecular Biology, 15–50. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-413-1_2.

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Mould, Paul A. "Solid Phase Assays for Studying ECM Protein–Protein Interactions." In Methods in Molecular Biology, 195–200. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-413-1_13.

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Wang, Jiangxue, Ying Hou, and Jiawei Ma. "Titanium surfaces, biochemical modification by peptides and ECM proteins." In Encyclopedia of Metalloproteins, 2248. New York, NY: Springer New York, 2013. http://dx.doi.org/10.1007/978-1-4614-1533-6_200001.

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Paardekooper, E. J. C., and J. Bol. "Future protein foods." In Product Innovation and Eco-efficiency, 67–77. Dordrecht: Springer Netherlands, 1998. http://dx.doi.org/10.1007/978-94-015-8945-1_10.

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Elagamey, Eman, Kanika Narula, Niranjan Chakraborty, and Subhra Chakraborty. "Extracellular Matrix Proteome: Isolation of ECM Proteins for Proteomics Studies." In Nitrogen Metabolism in Plants, 155–72. New York, NY: Springer New York, 2019. http://dx.doi.org/10.1007/978-1-4939-9790-9_14.

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Ostuni, Emanuele, George M. Whitesides, Donald E. Ingber, and Christopher S. Chen. "Using Self-Assembled Monolayers to Pattern ECM Proteins and Cells on Substrates." In Methods in Molecular Biology, 183–94. Totowa, NJ: Humana Press, 2009. http://dx.doi.org/10.1007/978-1-59745-413-1_12.

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Schulze-Kremer, Steffen. "Genetic algorithms for protein tertiary structure prediction." In Machine Learning: ECML-93, 262–79. Berlin, Heidelberg: Springer Berlin Heidelberg, 1993. http://dx.doi.org/10.1007/3-540-56602-3_141.

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Okun, Oleg, Helen Priisalu, and Alexessander Alves. "Fast Non-negative Dimensionality Reduction for Protein Fold Recognition." In Machine Learning: ECML 2005, 665–72. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/11564096_67.

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van Haasterecht, L., Paul P. M. van Zuijlen, and ML Groot. "Structural Assessment of Scars Using Optical Techniques." In Textbook on Scar Management, 169–78. Cham: Springer International Publishing, 2020. http://dx.doi.org/10.1007/978-3-030-44766-3_19.

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AbstractThe evaluation of scar treatment benefits from exact structural measurements. Accurate assessment of thickness, surface area, and relief is crucial in routine clinical follow-up. From an experimental perspective, precise visualization of the microstructural organization is necessary for a better understanding of the mechanisms underlying pathological scarring. Structural proteins in scars differ from healthy skin in terms of amount, type, and importantly, organization. The precise quantification of this extracellular matrix (ECM) organization was, until recently, limited to two-dimensional images from fixated and stained tissue. Advances in optical techniques now allow high-resolution imaging of these structures, in some cases in vivo. The enormous potential of these techniques as objective assessment tools is illustrated by a substantial increase in available devices. This chapter describes currently used devices and techniques used in the clinical follow-up of scar progression from a volumetric standpoint. Furthermore, some of the most powerful techniques for microstructural research are described including optical coherence tomography, nonlinear optical techniques such as second harmonic generation microscopy, and confocal microscopy.
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Coste, François, and Goulven Kerbellec. "A Similar Fragments Merging Approach to Learn Automata on Proteins." In Machine Learning: ECML 2005, 522–29. Berlin, Heidelberg: Springer Berlin Heidelberg, 2005. http://dx.doi.org/10.1007/11564096_50.

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Conference papers on the topic "ECM proteiny"

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Lee, Hae-Jeong, Marvi A. Matos, Lisa Pakstis, Marcus T. Cicerone, and Joy P. Dunkers. "Quantitation of Laminin Adsorbed Onto Polydimethylsiloxane Surfaces Using Various Treatment Protocols." In ASME 2008 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2008. http://dx.doi.org/10.1115/sbc2008-192785.

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There is considerable interest in how cells respond to mechanical stimuli, from the ligands used to transmit the stimulus to the signaling pathways initiated and the proteins expressed upon phenotype change [1]. Previous work focused on the evaluation of the quality of the extracellular matrix (ECM) coating and cell proliferation [2]. Our focus is the characterization of a flexible polymeric substrate, treated with ECM, used to induce tensile strain on cells. In this work, we expand our physical characterization of the protein modified polydimethylsiloxane (PDMS) surface by quantifying the coverage of laminin on PDMS, plasma-treated PDMS, and PDMS treated with plasma and aminopropyltrimethoxysilane (APTMS) (Silane_70 protocol) using X-ray reflectivity.
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Wang, Yunjie, and Katherine Yanhang Zhang. "The Biomechanical Properties of Arterial Elastin With Glucose Effect." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14200.

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Elastin, as one of the major extracellular matrix (ECM) components, is essential to accommodate physiological deformation and provide elastic support for blood vessels. Elastin is a long-lived ECM protein and it can suffer from cumulative effects of exposure to chemical damage, which can greatly compromise its biomechanical properties. The mechanical properties of elastin are related to its microstructure and the chemical environment. Glucose is an important carbohydrate in human body. The effect of glucose on the mechanical properties of blood vessels is especially magnified in diabetic patients [1]. Glucose can directly condense with amino groups of proteins by nonenzymatic glycation, which is one of the main mechanisms of aging [2].
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Sewell-Loftin, M. K., and W. David Merryman. "The Role of SRC in Strain- and Ligand- Dependent Phenotypic Modulation of Mouse Embryonic Fibroblasts." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53604.

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Connective tissue fibrosis represents a significant portion of mortality and morbidity in our society. These diseases include many illnesses such as heart valve disease, atherosclerosis, macular degeneration, and cirrhosis, meaning that millions of lives are affected by these conditions each year. Fibrotic tissues form when quiescent fibroblasts activate becoming myofibroblasts, the phenotype of active tissue construction and fibrosis. During this process, the cells produce smooth muscle α-actin (αSMA), a contractile element considered to be the hallmark of cellular activation [1]. Following the production of αSMA, there is an increase in the synthesis of extracellular matrix (ECM) proteins, most notably type I collagen; this increase in ECM proteins causes the stiffening of the tissue characteristic of fibrotic disease. In non-disease states (such as wound healing or tissue development), the myofibroblasts will either deactivate, becoming fibroblasts again, or apoptose before tissue fibrosis occurs. However, when myofibroblasts persist, increased ECM protein deposition causes increased tissue stiffness and activates neighboring cells, causing the fibrosis to propagate. Currently there are no therapies to prevent or reverse fibrosis. Therefore a more thorough understanding of the dynamic mechanical environment and signaling pathways involved in the activation of fibroblasts is required to develop potential treatments.
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Freytes, Donald O., Samuel Kolman, Sachin S. Velankar, and Stephen F. Badylak. "Rheological Properties of Extracellular Matrix Derived Gels." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176537.

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Bioscaffolds composed of extracellular matrix (ECM) have been used for the repair of a variety of tissues often leading to tissue-specific constructive remodeling [1]. ECM scaffolds are typically prepared by decellularization of tissues and are composed of the structural proteins (e.g. collagen) and functional proteins (e.g. growth factors) that characterize the native ECM. However, for certain applications, the use of ECM scaffolds can be limited by the native two-dimensional sheet form in which they are harvested.
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Lai, Victor K., Edward A. Sander, Spencer P. Lake, Robert T. Tranquillo, and Victor H. Barocas. "Collagen Network Topology is Influenced by Collagen Concentration, But Not by Co-Gelation With Fibrin." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53239.

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Extracellular matrix (ECM) proteins (e.g. collagen, elastin) play an important role in biological tissues. In addition to conferring mechanical strength to a tissue, the ECM provides a biochemical environment essential for modulation of cellular responses such as growth and migration. Collagens are the dominant protein of the ECM, with collagen type I being most abundant. Our group and others have shown that the mechanical properties of a collagen I matrix change with collagen concentration, and when formed in the presence of a secondary fibril network such as fibrin [1]. We are interested in collagen-fibrin systems because our group uses fibrin as the starting scaffold material for cardiovascular tissue engineering, which produces interpenetrating collagen-fibrin matrices during the remodeling process as the fibrin network is degraded and replaced with cell-deposited collagen [2]. Fibrin and collagen networks are also present together around the thrombus during the wound healing process. Research has shown that ECM mechanical properties are correlated with their overall network structure characteristics such as fibril diameter [3]. Currently we have a modeling framework that generates an ECM microstructural network which can be used to predict the overall properties of a bioengineered tissue [4]. This framework allows exploration of the structure-function relation, but how the structure depends on composition remains poorly understood, especially in multi-component gels. Thus, the objective of this work was to quantify the collagen network architecture in pure collagen gels of different concentrations and in collagen-fibrin co-gels.
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Qiu, Weiguo, Arjun Stokes, Joseph Cappello, and Xiaoyi Wu. "Electrospinning of Recombinant Protein Polymer Nanofibers." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206352.

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Structural proteins often in the form of micro and nanofibers, constituting most of intra- and extracellular matrix (ECM), are the fundamental building blocks of life [1]. Recent efforts to replace diseased or damaged tissues and organs have resulted in the molecular design and genetic engineering of recombinant proteins, and the advent of new technology for fabricating structural proteins into micro-/nanofibrous scaffolds, hoping to resemble some or all the characteristics of ECM structure and function. The fabrication of such an ECM mimic may be an important step in engineering a functional tissue. To this end, we have produced a series of silk-elastin-like proteins (SELPs) [2]. Revealed by our subsequent studies, SELPs in the form of hydrogels, thin films, and microfibers, have displayed a set of outstanding biological and physical properties. In this study, electrospinning will be pursued as a mechanism for the formation of SELP nanofibers.
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Espinosa, Gabriela, Lisa Bennett, William Gardner, and Jessica Wagenseil. "The Effects of Extracellular Matrix Protein Insufficiency and Treatment on the Stiffness of Arterial Smooth Muscle Cells." In ASME 2013 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2013. http://dx.doi.org/10.1115/sbc2013-14131.

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Increased arterial stiffness is directly correlated with hypertension and cardiovascular disease. Stiffness of the conducting arteries is largely determined by the extracellular matrix (ECM) proteins in the wall, such as collagen and elastin, produced by the smooth muscle cells (SMCs) found in the medial layer. Elastin is deposited as soluble tropoelastin and is later crosslinked into elastin fibers. Newborn mice lacking the elastin protein ( Eln−/−) have increased arterial wall stiffness and SMCs with altered proliferation, migration and morphology [1]. Vessel elasticity is also mediated by other ECM proteins, such as fibulin-4. Elastic tissue, such as lung, skin, and arteries, from fibulin-4 deficient ( Fbln4−/−) mice show no decrease in elastin content, but have reduced elasticity due to disrupted elastin fibers [2]. Arteries from both elastin and fibulin-4 deficient mice have been previously studied, but the mechanical properties of their SMCs have not been investigated. Recent experiments comparing arterial SMCs from old and young animals suggest that mechanical properties of the SMCs themselves may contribute to changes in wall stiffness [3]. Hence, we investigated the stiffness of isolated arterial SMCs from elastin and fibulin-4 deficient mice using atomic force microscopy (AFM). In addition, we studied the effects of two elastin treatments on the mechanical properties of SMCs from Eln+/+ and Eln−/− mice. Differences between the treatments may elucidate the importance of soluble versus crosslinked elastin on single cell stiffness.
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Chan, Roger W., Thomas H. Siegmund, Kai Zhang, Neeraj Tirunagari, and Min Fu. "Structural Constitutive Characterization of the Vocal Fold: Modeling the Fibrous and the Interstitial Matrix Proteins." In ASME 2004 International Mechanical Engineering Congress and Exposition. ASMEDC, 2004. http://dx.doi.org/10.1115/imece2004-61298.

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The extracellular matrix (ECM) of the human vocal fold is a highly specialized soft connective tissue with a layered microstructure that is optimally tuned for vibration and sound production in response to a unique set of biomechanical stimuli in vivo, including oscillation at amplitudes up to 3–4 mm at magnitudes of acceleration &gt; 200g and at high frequencies (&gt; 100Hz). The vocal fold ECM, commonly called the lamina propria or mucosa, consists of biomacromolecules of two major classes distributed in different densities: (1) fibrous proteins including collagen and elastin fibers that are denser in the deep layers of the ECM, and (2) interstitial proteins like glycosaminoglycans and structural glycoproteins that are scattered throughout the entire ECM [1,2]. Nonlinear viscoelastic response of the vocal fold ECM under different loading conditions has been reported, including strain rate-dependence and hysteresis of tensile stress-strain curves, and nonlinear stress-strain behavior under large-strain shear [3,4].
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Cheng, Jeffrey K., Victoria Le, Robert P. Mecham, and Jessica E. Wagenseil. "Mechanics and Modeling of Postnatal Arterial Development in Wild-Type and Elastin-Insufficient Mice." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53140.

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Large arteries in vertebrates serve as elastic reservoirs that store a portion of the blood volume with systole and discharge it during diastole. This function is made possible by the combination of extracellular matrix (ECM) proteins deposited by the smooth muscle cells (SMCs) in the arterial wall. Elastin and collagen expression in mice is first detectable around embryonic day 14 and peaks around postnatal day (P) 14, returning to baseline levels by P30. During this time, pressure and cardiac output increase significantly before leveling off ∼P30 [1]. Hence, the protein amounts and consequent mechanical properties of the arterial wall change simultaneously with the applied hemodynamic loads in a complicated and unknown feedback loop.
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Bell, Brett J., and Sherry L. Voytik-Harbin. "Multiaxial Study of Fibroblast Biomechanics in a 3D Collagen Matrix." In ASME 2009 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2009. http://dx.doi.org/10.1115/sbc2009-206722.

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It is becoming increasingly evident, that of the signaling modalities relevant to the cell-extracellular matrix (ECM) microenvironment, the mechanical component is a very important mediator of cell behavior (reviewed in [1, 2]). Indeed, proliferation, ECM protein expression (collagen), matrix metalloproteinase (MMP) levels, migration, and stem cell differentiation, have all been shown to be affected by mechanical environmental cues [3, 4]. Although the importance of physical signaling mechanisms has been well established, the bulk of this work has yet to be translated to a more physiologic 3D microenvironment [1]. Self-assembling collagen matrices provide a biochemically, biophysically relevant 3D model of soft tissues in which biomechanical studies can be performed [5, 6]. It is with this 3D tissue model in mind, that a biaxial mechanical testing system (BMTS) was devised, built, tested, and applied to the study of cell-ECM biomechanics. The completion of this device has enabled us, to undertake a multi-scale, multidimensional study of cell-ECM mechanics. Hierarchical quantification of cell and ECM strains using digital image correlation (DIC) facilitate a more complete understanding of the mechanical response of cells to macroscopic loads and deformations. Furthermore, transfection of cells with GFP tagged actin binding protein utrophin (UTR-GFP) enables qualitative assessment of cytoskeletal deformations [7].
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