Relevant bibliographies by topics / Extracellular proteolysi

Academic literature on the topic 'Extracellular proteolysi'

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Published: 9 March 2023
Last updated: 10 March 2023

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Journal articles on the topic "Extracellular proteolysi"

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Kakurina, Gelena Valer'evna, Irina Viktorovna Kondakova, and Evgeniy Lkhamatsyrenovich Choynzonov. "Degradome Components in Progression of Squamous Cell Carcinoma of the Head and Neck." Annals of the Russian academy of medical sciences 70, no. 6 (December 6, 2015): 684–93. http://dx.doi.org/10.15690/vramn563.

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The process of tumor progression is closely related to the intracellular, extracellular and intramembranous proteolysis. Many studies indicate that the proteases function as part of an extensive multidirectional network of proteolytic interactions. Disturbance of strictly controlled equilibrium of the proteolytic system is described in a number of diseases, including cancer. The paper presents a review of the available data concerning the contribution of intracellular, extracellular and intramembrane proteolysis to the process of squamous cell head and neck carcinoma. Specific mechanisms of interaction of different proteolytic systems in cancer progression both in general and in squamous cell head and neck carcinoma remain underinvestigated. The versatility of functions and complexity of the relationships between proteolytic systems highlights the importance of studying the participation of all degradome components in tumor progression that may clarify the multi-link complex mechanisms of carcinogenesis of squamous cell head and neck carcinoma and to identify markers of progression and/or a targets for therapeutic intervention.
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Weaver, T. E., and J. A. Whitsett. "Processing of hydrophobic pulmonary surfactant protein B in rat type II cells." American Journal of Physiology-Lung Cellular and Molecular Physiology 257, no. 2 (August 1, 1989): L100—L108. http://dx.doi.org/10.1152/ajplung.1989.257.2.l100.

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The amino acid sequence of surfactant protein B (SP-B), derived from human genomic and cDNA sequences, indicates that the active polypeptide is contained within the sequence of a preproprotein of 381 residues. Synthesis of mature SP-B, which requires proteolytic processing at both the NH2- and COOH-termini of the proprotein, was studied in primary cultures of rat alveolar type II epithelial cells. Type II cells were pulse labeled with [35S]methionine-cysteine for 15-30 min and chased for 0-18 h. SP-B proprotein (Mr = 42,000) accumulated in the medium at early time points but declined at later time points suggesting extracellular proteolysis of the proprotein. In contrast, surfactant protein A (SP-A), another surfactant protein, continued to accumulate extracellularly during this time period. A proteolytic fragment of SP-B (Mr = 25,000) accumulated in the medium with a slightly slower time course, consistent with extracellular proteolysis of the proprotein. Intracellular processing of SP-B was also detected. SP-B polypeptides of Mr 8,000 and 12,000 were detected intracellularly and in the medium at late time points. These forms of SP-B (Mr = 8,000 and 12,000) comigrated in two-dimensional isoelectric-focusing sodium dodecyl sulfate-polyacrylamide gel electrophoresis with mature SP-B isolated from rat alveolar lavage fluid. The mature form of SP-B (Mr = 8,000), but not the Mr 42,000 and 25,000 SP-B precursors, was also detected in lamellar bodies isolated from rat lung homogenates. These experiments demonstrate complete proteolytic processing of prepro-SP-B to the alveolar Mr 8,000 form by type II epithelial cells in vitro.(ABSTRACT TRUNCATED AT 250 WORDS)
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Hintermann, Edith, Susan Kinder Haake, Urs Christen, Andrew Sharabi, and Vito Quaranta. "Discrete Proteolysis of Focal Contact and Adherens Junction Components in Porphyromonas gingivalis-Infected Oral Keratinocytes: a Strategy for Cell Adhesion and Migration Disabling." Infection and Immunity 70, no. 10 (October 2002): 5846–56. http://dx.doi.org/10.1128/iai.70.10.5846-5856.2002.

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ABSTRACT Adhesive interactions of cells are critical to tissue integrity. We show that infection with Porphyromonas gingivalis, a major pathogen in the periodontal disease periodontitis, interferes with both cell-matrix and cell-cell adhesion in the oral keratinocyte cell line HOK-16. Thus, infected cells showed reduced adhesion to extracellular matrix, changes in morphology from spread to rounded, and impaired motility on purified matrices in Transwell migration assays and scratch assays. Western blot analysis of P. gingivalis-challenged HOK-16 cells revealed proteolysis of focal contact components (e.g., focal adhesion kinase), adherens junction proteins (e.g., catenins), and adhesion signaling molecules (e.g., the tyrosine kinase SRC). Proteolysis was selective, since important components of adherens junctions (E-cadherin) or signaling molecules (extracellular signal-regulated kinases ERK1/2) were not degraded. The virulence factors gingipains, cysteine proteinases expressed by P. gingivalis, are likely responsible for this proteolytic attack, since they directly digested specific proteins in pull-down experiments, and their proteolytic activity was blocked by the cysteine proteinase inhibitor N-α-p-tosyl-l-lysine chloromethyl ketone and also by a caspase inhibitor. Proteolysis was strain dependent, such that ATCC 33277 and 381 had high proteolytic potential, whereas W50 showed almost no proteolytic activity. These findings may help explain the formation of gingival pockets between cementum and periodontal epithelium, a hallmark of periodontitis. Furthermore, they illustrate a new pathogenetic paradigm of infection whereby bacteria may disrupt the integrity of epithelia.
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Perregaux, David G., and Christopher A. Gabel. "Post-Translational Processing of Murine IL-1: Evidence that ATP-Induced Release of IL-1α and IL-1β Occurs via a Similar Mechanism." Journal of Immunology 160, no. 5 (March 1, 1998): 2469–77. http://dx.doi.org/10.4049/jimmunol.160.5.2469.

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Abstract In response to LPS, peritoneal macrophages produce IL-1, but, for the most part, newly synthesized cytokine molecules remain cell associated. Externalization and proteolytic processing of pro-IL-1β can be initiated by extracellular ATP. In this study, kinetics and inhibitor sensitivity of the stimulus-coupled mechanism were investigated with [35S]methionine-labeled macrophages. Optimal ATP concentrations required to promote cytokine post-translational processing suggest the involvement of a P2Z type of receptor. Proteolysis of pro-IL-1β initiates within 7.5 min of ATP addition; 17-kDa mature IL-1β is observed first intracellularly and subsequently extracellularly. In contrast, ATP-treated cells do not contain 17-kDa IL-1α. Macrophages exposed to ATP continuously or only for a 15-min pulse release IL-1α, IL-1β, and lactate dehydrogenase (LDH). Proteolytic maturation of IL-1β exceeds that of IL-1α in both formats, but pulsed cells process the externalized cytokines more efficiently. Ethacrynic acid and DIDS (4,4′-diisothiocyanato-stilbene-2,2′-disulfonic acid) block ATP-induced proteolysis of pro-IL-1β and prevent release of pro-IL-1α/β and LDH; they do not inhibit ATP-induced K+ (86Rb+) efflux. Ethacrynic acid inhibits release of both forms of IL-1 with a similar concentration dependence; within the arrested cells, procytokines accumulate in a Triton-insoluble fraction. An IL-1β-converting enzyme inhibitor blocks proteolysis of IL-1β, but it does not prevent release of pro-IL-1α, pro-IL-1β, or LDH. These results indicate that ATP stimulates externalization of both IL-1α and IL-1β. The ATP-induced cytokine release mechanism is accompanied by cell death and requires activity of an anion transport inhibitor-sensitive component, but this pathway operates independently of cytokine proteolytic processing.
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Petushkova, Anastasiia I., and Andrey A. Zamyatnin. "Redox-Mediated Post-Translational Modifications of Proteolytic Enzymes and Their Role in Protease Functioning." Biomolecules 10, no. 4 (April 23, 2020): 650. http://dx.doi.org/10.3390/biom10040650.

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Proteolytic enzymes play a crucial role in metabolic processes, providing the cell with amino acids through the hydrolysis of multiple endogenous and exogenous proteins. In addition to this function, proteases are involved in numerous protein cascades to maintain cellular and extracellular homeostasis. The redox regulation of proteolysis provides a flexible dose-dependent mechanism for proteolytic activity control. The excessive reactive oxygen species (ROS) and reactive nitrogen species (RNS) in living organisms indicate pathological conditions, so redox-sensitive proteases can swiftly induce pro-survival responses or regulated cell death (RCD). At the same time, severe protein oxidation can lead to the dysregulation of proteolysis, which induces either protein aggregation or superfluous protein hydrolysis. Therefore, oxidative stress contributes to the onset of age-related dysfunction. In the present review, we consider the post-translational modifications (PTMs) of proteolytic enzymes and their impact on homeostasis.
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Toe, Cui Jin, Hooi Ling Foo, Teck Chwen Loh, Rosfarizan Mohamad, Raha Abdul Rahim, and Zulkifli Idrus. "Extracellular Proteolytic Activity and Amino Acid Production by Lactic Acid Bacteria Isolated from Malaysian Foods." International Journal of Molecular Sciences 20, no. 7 (April 10, 2019): 1777. http://dx.doi.org/10.3390/ijms20071777.

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Amino acids (AAs) are vital elements for growth, reproduction, and maintenance of organisms. Current technology uses genetically engineered microorganisms for AAs production, which has urged the search for a safer food-grade AA producer strain. The extracellular proteolytic activities of lactic acid bacteria (LAB) can be a vital tool to hydrolyze extracellular protein molecules into free AAs, thereby exhibiting great potential for functional AA production. In this study, eight LAB isolated from Malaysian foods were determined for their extracellular proteolytic activities and their capability of producing AAs. All studied LAB exhibited versatile extracellular proteolytic activities from acidic to alkaline pH conditions. In comparison, Pediococcus pentosaceus UP-2 exhibited the highest ability to produce 15 AAs extracellularly, including aspartate, lysine, methionine, threonine, isoleucine, glutamate, proline, alanine, valine, leucine, tryptophan, tyrosine, serine, glycine, and cystine, followed by Pediococcus pentosaceus UL-2, Pediococcus acidilactici UB-6, and Pediococcus acidilactici UP-1 with 11 to 12 different AAs production detected extracellularly. Pediococcus pentosaceus UL-6 demonstrated the highest increment of proline production at 24 h of incubation. However, Pediococcus acidilactici UL-3 and Lactobacillus plantarum I-UL4 exhibited the greatest requirement for AA. The results of this study showed that different LAB possess different extracellular proteolytic activities and potentials as extracellular AA producers.
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Campbell, E. J., E. K. Silverman, and M. A. Campbell. "Elastase and cathepsin G of human monocytes. Quantification of cellular content, release in response to stimuli, and heterogeneity in elastase-mediated proteolytic activity." Journal of Immunology 143, no. 9 (November 1, 1989): 2961–68. http://dx.doi.org/10.4049/jimmunol.143.9.2961.

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Abstract Human peripheral blood monocytes contain human leukocyte elastase (HLE) and cathepsin G (CG), serine proteinases originally described in azurophil granules of polymorphonuclear neutrophils (PMN). Immunoreactive HLE and CG of freshly harvested monocytes have been quantified in this study; to begin to elucidate potential roles for these enzymes in extracellular events, release in response to stimuli has been measured, along with proteolytic activity of monocytes toward surface-bound proteins. Our results indicate that whole-cell extracts of monocytes contain approximately 6% of the amount of HLE as do extracts of comparable numbers of PMN. In response to PMA in vitro, monocytes released 39 to 53% of their content of HLE and CG within 60 min, a fractional release greater than that of PMN. Furthermore, when phorbol-stimulated monocytes were adherent to a fibronectin-coated surface, extensive HLE-mediated proteolysis of the surface-bound protein was observed. Proteolysis by such cells in the presence of proteinase inhibitors was of considerable interest, since a subpopulation (15 to 20% of the total) expressed marked but localized proteolytic activity, possibly escaping inhibition through contact-mediated mechanisms. These data indicate that a subpopulation of freshly harvested monocytes is rich in HLE and CG (serine proteinases traditionally associated with PMN), can promptly release HLE and CG in response to stimuli, and can utilize HLE for extracellular proteolysis. Monocyte-derived serine proteinases may participate in extracellular events formerly associated with PMN-derived HLE and CG.
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Lockwood, Thomas D. "Redox-dependent and redox-independent subcomponents of protein degradation in perfused myocardium." American Journal of Physiology-Endocrinology and Metabolism 276, no. 5 (May 1, 1999): E945—E954. http://dx.doi.org/10.1152/ajpendo.1999.276.5.e945.

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The integration of proteolytic pathways with metabolism was investigated in perfused rat myocardium. After a 10-min incorporation period, the minute-to-minute release of [3H]leucine from myocardial proteins was measured in nonrecirculating effluent perfusate. The nontoxic pro-oxidant probe diamide (100 μM) or a supraphysiological concentration of the endogenous oxidative metabolite dehydroascorbic acid (200 μM) reversibly inhibited 75% of myocardial proteolysis consisting of several known subcomponents (redox dependent); however, 25% of proteolysis was diamide insensitive (redox independent). Decrease in extracellular glucose concentration from 10 to 0.1 mM strongly increased the potencies of minimally effective concentrations of diamide (10 μM) or dehydroascorbic acid (15 μM) by ∼10-fold to the respective potencies maximally inhibiting proteolysis. The reversal of diamide action was also strongly dependent on the perfusate glucose concentration observed at 0.1, 0.2, 1.0 and 10 mM glucose. Proteolytic inhibition caused by diamide (100 μM) was not accompanied by change in basal tissue ATP content of 5 μmol/g wet wt. Conversely, nearly lethal 60% ATP depletion caused by sodium azide (0.4 mM) was not accompanied by change in total [3H]leucine release. Results indicate that a large proteolytic subcomponent (75%) is maintained by redox chains fed by glucose; however, there is no apparent linkage of this proteolysis to short-term ATP fluctuations. A distinct major proteolytic subcomponent (25%) does not vary in response to experimental intervention in either ATP content or redox chains.
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Chirkin, A. A., O. M. Balaeva-Tikhomirova, V. V. Dolmatova, and I. O. Semenov. "Molecular-structural homology of proteolytic enzymеs in the studying of proteolysis mechanism and its regulation." Proceedings of the National Academy of Sciences of Belarus, Chemical Series 57, no. 2 (June 3, 2021): 206–17. http://dx.doi.org/10.29235/1561-8331-2021-57-2-206-217.

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The actual problem of experimental medicine is the substantiation of new model organisms that meet modern requirements of bioethics, cost and conditions of detention. The aim of this work was a comparative analysis of the homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks. The homology of enzymes in nucleotide sequences in humans and pulmonary freshwater mollusks in the analysis of unregulated proteolysis is 66–68 %; regulated proteolysis – 69–76 %; ubiquitin-like modifiers – 78–83 %; extracellular enzymes – 67–76 %; and intracellular enzymes – 65–72 %. The evolutionary conservatism of proteolytic enzymes and the presence of an open blood circulation, which allows the substances under study to be delivered from the hemolymph directly to target cells, make it possible to use these animals as cheap and convenient test organisms. The practical importance of a sufficiently high homology degree of proteolytic enzymes in humans and pulmonary freshwater mollusks justifies the expediency of forming mollusk aquaculture to obtain proteolytic enzyme protein preparations from their tissues within the framework of the tasks of biopharmaceuticals, cosmetics and the food industry.
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Mineur, Pierre, Alain C. Colige, Christophe F. Deroanne, Johanne Dubail, Frédéric Kesteloot, Yvette Habraken, Agnès Noël, et al. "Newly identified biologically active and proteolysis-resistant VEGF-A isoform VEGF111 is induced by genotoxic agents." Journal of Cell Biology 179, no. 6 (December 17, 2007): 1261–73. http://dx.doi.org/10.1083/jcb.200703052.

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Ultraviolet B and genotoxic drugs induce the expression of a vascular endothelial growth factor A (VEGF-A) splice variant (VEGF111) encoded by exons 1–4 and 8 in many cultured cells. Although not detected in a series of normal human and mouse tissue, VEGF111 expression is induced in MCF-7 xenografts in nude mice upon treatment by camptothecin. The skipping of exons that contain proteolytic cleavage sites and extracellular matrix–binding domains makes VEGF111 diffusible and resistant to proteolysis. Recombinant VEGF111 activates VEGF receptor 2 (VEGF-R2) and extracellularly regulated kinase 1/2 in human umbilical vascular endothelial cells and porcine aortic endothelial cells expressing VEGF-R2. The mitogenic and chemotactic activity and VEGF111's ability to promote vascular network formation during embyonic stem cell differentiation are similar to those of VEGF121 and 165. Tumors in nude mice formed by HEK293 cells expressing VEGF111 develop a more widespread network of numerous small vessels in the peritumoral tissue than those expressing other isoforms. Its potent angiogenic activity and remarkable resistance to proteolysis makes VEGF111 a potential adverse factor during chemotherapy but a beneficial therapeutic tool for ischemic diseases.
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Dissertations / Theses on the topic "Extracellular proteolysi"

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LORENZI, V. DE. "CROSS-TALK BETWEEN THE PROTEOLYTIC AND NON-PROTEOLYTIC FUNCTIONS OF THE UROKINASE RECEPTOR." Doctoral thesis, Università degli Studi di Milano, 2015. http://hdl.handle.net/2434/265507.

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Urokinase (uPA) and its cell surface receptor (uPAR) have been implicated in a wide variety of biological processes related to tissue homeostasis. Moreover the uPA-system plays an important role in many pathological events, such as tumour cell migration and dissemination. On the one hand, the binding of uPA to uPAR favours extracellular proteolysis by enhancing cell surface plasminogen activation. On the other hand, it promotes cell adhesion and signalling through binding of the provisional matrix protein vitronectin (VN). Although the existence of feedback loops between the functions of uPAR in extracellular proteolysis, cell adhesion and signalling has been described, some aspects of this cross-talk are still poorly understood and not characterized experimentally. We here report that cell surface plasminogen activation induces a potent negative feedback on cell adhesion to VN. The feedback is predominantly caused by proteolytic cleavage of the RGD-motif in VN catalyzed by both uPA and plasmin. In this process the cell-adhesive properties of VN are impaired by disruption of the integrin binding site and release of the somatomedin B (SMB) domain responsible for binding of uPAR. Cleavage of VN by uPA displays a remarkable receptor-dependence and requires concomitant binding of both uPA and VN to uPAR suggesting that the hydrolysis is accelerated by a mechanism of substrate presentation. VN represents the first described uPAR-dependent substrate of uPA and our findings therefore identify a potential novel function of uPAR in focusing the proteolytic activity of the plasminogen activation system onto extracellular matrix-associated VN. Additionally, SMB-containing N-terminal VN fragments are released by several cancer cell lines in vitro and are detectable in human urines samples. We have thus developed a clinical grade immunoassay for the detection and quantification of such fragments in urine samples with the aim of using the levels of urinary VN fragments as a novel cancer biomarker. Our working hypothesis is that this biomarker may be used as an indirect functional measurement of the uPA-system activity in the tumour tissue. Finally, we show that the specific urokinase inhibitor, plasminogen activator inhibitor 1 (PAI-1), blocks the negative feedback mediated by uPA and behaves as a potent uPA-dependent agonist of the interaction between uPAR and VN. Indeed, we report for the first time that the covalent complex between uPA and PAI-1 is endowed with higher agonistic activity compared to uPA. Taken together, these data might represent a molecular explanation of the poor clinical outcome observed in cancer patients with high levels of uPA and PAI-1.
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Slimani, Lamia. "Mécanismes impliqués dans l'atrophie et la récupération musculaire après immobilisation chez le rat. : Rôle des altérations de la matrice extracellulaire." Thesis, Clermont-Ferrand 1, 2012. http://www.theses.fr/2012CLF1MM21/document.

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Le muscle squelettique est le réservoir principal d’acides aminés libres de l’organisme. Ainsi, l’atrophie musculaire induite par l’immobilisation peut entraîner un affaiblissement et un allongement des périodes de récupération générant des coûts de santé publique élevés. Une aggravation de l’atrophie caractérise de façon surprenante le muscle tibialis anterior (TA) après le déplâtrage, retardant la récupération. Mon objectif a été de comprendre les mécanismes à l’origine de l’aggravation de l’atrophie du TA pendant les phases précoces de récupération en étudiant i) la structure et le phénotype des muscles, ii) la composition de la matrice extracellulaire (MEC), iii) la protéolyse et l’apoptose, et iv) les processus de signalisation via les intégrines. Des rats ont été soumis à une immobilisation par plâtrage pendant 8 jours d’une des deux pattes arrière, l’autre servant de témoin, et placés en récupération pendant 10 jours. L’aggravation de l’atrophie du TA apparaît dès déplâtrage, corrélée avec i) une baisse de l’aire des fibres associée à leur déformation, ii) une redistribution des isoformes des chaines lourdes de myosines, iii) une augmentation de l’apoptose localisée dans le tissu conjonctif, iv) un épaississement de l’endomysium pendant la remobilisation, v) des adaptations au niveau des processus de remodelage des collagènes, et vi) une activation prononcée et persistante du système protéolytique ubiquitine-protéasome (UPS) et de l’apoptosome. Nous montrons également une élévation des niveaux ARNm dans le TA remobilisé vii) de la ténascine-C et de Sparc dès le déplâtrage, et viii) de marqueurs de l’autophagie à partir du moment où l’atrophie se stabilise. Enfin, nous montrons également une élévation des ARNm dans le TA immobilisé ix) des facteurs myogéniques, et x) des intégrines membranaires et de leurs partenaires pendant l’immobilisation et après le déplâtrage. En conclusion, mon travail de thèse a permis de montrer que l'aggravation de l’atrophie du TA est précoce, associée à un remodelage important de la structure et de la composition de la MEC et du phénotype des fibres musculaires, et pourrait résulter de l’augmentation persistante et prononcée de la voie UPS et de l’apoptose. Ce travail suggère que des modifications au niveau des molécules matricielles pendant la remobilisation pourraient influencer la signalisation dépendante des intégrines et la régénération musculaire
Skeletal muscle is the main reservoir of body amino acids. Thus, muscle atrophy induced by immobilization can lead to a weakening and to a lengthening of recovery periods, leading to elevated healthcare costs. Surprisingly, a worsening of tibialis anterior (TA) muscle atrophy prevailed after cast removal and thus delayed recovery. The aim of my Ph.D was to understand mechanisms underlying the worsening of TA atrophy during early recovery by studying i) the muscle structure and phenotype, ii) the composition of the extracellular matrix (ECM), iii) proteolysis and apoptosis, and iv) the signaling pathways via integrins. Rats were subjected to hindlimb casting for 8 days of one hindllimb, the other leg served as control, and then were allowed to recover for 10 days. The worsening of TA atrophy appeared immediately after cast removal and correlated with i) a decrease in fiber crosssection area associated to fiber deformation, ii) a redistribution of myosin heavy chain isoforms, iii) an increase in apoptosis localized in the connective tissue, iv) a thickening of the endomysium during remobilization, v) some adaptations in collagen remodeling processes, and vi) a pronounced and sustained activation of the ubiquitin-proteasome proteolytic system (UPS) and of the apoptosome. We also showed an increase in the remobilized TA of mRNA levels vii) of tenascin-C and Sparc immediately after cast removal, and viii) of some autophagy markers, when atrophy stabilized. Finally, we showed an elevation of mRNA levels encoding ix) myogenic factors, and x) transmembrane integrins and their partners during TA immobilization and after cast removal. In conclusion, my Ph.D project showed that the worsening of the TA atrophy occurred early after cast removal, was associated with a significant remodeling of the structure and composition of the ECM and of the phenotype of muscle fibers, and may result from pronounced and sustained increase in the UPS and apoptosis. This work suggests that changes in the matricellular matrix molecules during remobilization could influence integrin-dependent signaling and muscle regeneration
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Brown, Geraldine Marie. "Extracellular matrix proteolysis by bronchoalveolar leukocytes in experimental pneumoconiosis." Thesis, University of Edinburgh, 1990. http://hdl.handle.net/1842/19447.

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Neutral proteinases, released by inflammatory leukocytes, have been implicated in the pathogenesis of pneumoconiosis but there has been no systematic study of the proteolytic acitivty of leukocytes from dust-exposed lung. The aim of the present study was, therefore, to assess the bronchoalveolar leukocyte profile and proteolytic activity of the leukocytes in a rat model of pneumoconiosis. An assay, based on the breakdown of [125I] fibronectin, that would measure the overall proteolytic activity of the bronchoalveolar leukocytes and indicate their potential to damage the connective tissue of the alveolar septum was developed and validated. Increased proteolytic activity was found in the inflammatory bronchoalveolar leukocyte populations and so the relative role of macrophages and neutrophils was assessed by separation into distinct populations; both inflammatory macrophages and neutrophils had increased proteolytic activity. The important features governing the inflammogenicity of particles were addressed by measuring the inflammation-generating properties of a variety of fibrogenic and non-fibrogenic particles in rats exposed by intratracheal instillation or inhalation. The number of leukocytes recruited to the alveolar region was measured by bronchoalveolar lavage. Only fibrogenic mineral dusts had the ability to produce a sustained alveolitis in which the proteolytic activity of the bronchoalveolar leukocytes remained elevated. The pathogenicity of fibrogenic particles is likely, therefore, to be related to their ability to evoke and sustain an increased lung proteinase burden. The sustained alveolitis with fibrogenic particles was not related to lack of clearance of dust from the lung. Both quartz and coalmine dust elicited persistent alveolitis, but titanium dioxide, which is no more readily cleared than silica or coalmine dust, failed to sustain the inflammation. Properties of the particle surface, at least in the case of quartz, appear to play a part in their inflammogenicity. Altering the surface of quartz particles by coating them with aluminium lactate reduced their ability to recruit inflammatory leukocytes but did not alter the proteolytic activity of the leukocytes. The tissue response to the aluminium-coated quartz particles was also less than that elicited by native quartz with fewer and less-severe lesions. The foregoing serve to substantiate the role of inflammatory leukocytes in the pathogenesis of pneumoconiosis. Only when there is a sustained alveolitis with an overall increased proteinase burden, does pathological change occur in the lung. Reducing the magnitude and/or the duration of the alveolitis markedly suppresses the development of the tissue lesions.
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Deane, Shelly May. "Molecular biology studies on the extracellular serine proteases of Vibrio alginolyticus." Doctoral thesis, University of Cape Town, 1989. http://hdl.handle.net/11427/21895.

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Bibliography: pages 161-176.
Vibrio alginolyticus is a gram-negative aerobic bacterium that produces several extracellular serine proteases and a collagenase during the stationary growth phase. The aim of this study was to investigate alkaline serine protease production by this organism, and to attempt the cloning and expression of a V.alginolyticus protease gene in Escherichia coli.
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Mayer, Joanne. "Modulation of adult neural plasticity by proteolytic catabolism of lecticans." [Tampa, Fla] : University of South Florida, 2007. http://purl.fcla.edu/usf/dc/et/SFE0001927.

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Wallace, Andrew. "Design and synthesis of peptide derivatives as potential modulators of cellular chemotaxis and extracellular proteolysis." Thesis, Queen's University Belfast, 1987. http://ethos.bl.uk/OrderDetails.do?uin=uk.bl.ethos.317072.

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Okuyama, Hiroaki. "Regulation of cell growth by redox-mediated extracellular proteolysis of platelet-derived growth factor receptor β." Kyoto University, 2003. http://hdl.handle.net/2433/148682.

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Ein-Eli, Noémie. "Migration de cellules tumorales mammaire sur réseau en 3 Dimension et Mécanismes physiques de la protéolyse matricielle." Thesis, Cergy-Pontoise, 2014. http://www.theses.fr/2014CERG0688/document.

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Nous étudions la migration et la protéolyse de la matrice extracellulaire dans le cancer du sein. Pour cela, nous avons mis en place deux systèmes modèles. Le premier, se base sur une lame basale reconstituée et permet d'évaluer le potentiel invasif de lignées cellulaires tumorales. Nous montrons que les cellules cancéreuses migrent différemment à travers un gel pour former des amas de taille variable directement corrélé à leur pouvoir invasif. Dans notre système, seule la migration de type mésenchymateuse est utilisée par les cellules. Ce type de mouvement est directement dépendant de protéases sécrétées par les cellules. Nous avons, donc mesurée la synthèse au niveau transcriptionnel de la classe d'enzyme majoritairement impliquée dans la dissémination tumorale, les matrice métalloprotéases (MMPs). Nous avons ainsi pu montrer que l'expression de 3 MMPs est corrélée aux capacités migratoires des cellules donc à leur potentiel invasif. Le processus physique par lequel les enzymes dégradent les matrices est très peu étudié au niveau expérimental. Le second système que nous utilisons se base sur un modèle de matrice conjonctive majoritairement composer de collagène de type I. Nous utilisons la gélatine, pour étudier la protéolyse de gels protéiques par différentes classes de protéases. A partirdes études sur la solubilisation enzymatique des gels par l'-chymotrypsine, la protéinase K et la papaïne, nous montrons qu'il existe des mécanismes de dégradation distincts. Le premier est un mécanisme anormal dont la cinétique est limitée par la diffusion de l'enzyme, le second est brownien et la cinétique est limitée par la réaction. Ce second mécanisme dépend directement d'interactions eléctrostatiques entre l'enzyme et le gel. Nous observons pour deux des enzymes que l'évolution des temps de dégradation mais également la cinétique dépendent de la concentration en protéine dans les gels
We study the migration and proteolysis of the extracellular matrix in breast cancer. For this, we set up two model systems. The first is based on a reconstituted basement membrane and allows the evaluation of invasive potential tumor cell lines. We show that cancer cells migrate differently across the gel to form clusters of variable size directly correlates with their invasiveness. In our system, only the migration of mesenchymal type is used by the cells. This type of movement is directly dependent proteases secreted by the cells. We therefore measured the synthesis at the transcriptional level of the enzyme class mainly involved in tumor dissemination, the matrix metalloproteases (MMPs). We were able to show that the expression of 3 MMPs is correlated with migratory capacity of cells, therefore their invasive potential. The physical process by which enzymes degrade the matrix is very little studied at the experimental level. The second system we use is based on a model of connective matrix mainly composed of collagen type I. We use gelatin for the study of protein gels proteolysis by different classes of proteases. Based on the study of gels enzymatic solubilization by a- chymotrypsin, proteinase K and papain, we show that there are distinct mechanisms of degradation. The first mechanism is abnormal whose kinetic is limited by enzyme diffusion, and the second is Brownian and the kinetic is reaction limited. The second mechanism depends directly on electrostatic interactions between enzyme and gel. We observe for two enzymes that the evolution of degradation time but also the degradation kinetics depend on the concentration of protein in gels
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MONACO, SUSANNA. "Basement membrane and cellular migration: role of Gelatinases (MMP-2, MMP-9) on proteolysis of type IV collagen." Doctoral thesis, Università degli Studi di Roma "Tor Vergata", 2007. http://hdl.handle.net/2108/372.

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In condizioni patologiche le gelatinasi o meglio la MMP-2 e la MMP-9 vengono espresse dalle cellule in quantità più elevate rispetto alle normali condizioni fisiologiche. Ne sono un esempio i processi infiammatori e la progressione tumorale, dove queste endopeptidasi Ca+2 e Zn+2 dipendenti sono attivamente coinvolte nel processamento delle membrane basali cellulari; infatti la loro azione permette alle cellule tumorali la loro progressione all’interno di nuovi tessuti, dando origine alla formazione di metastasi. Le gelatinasi influenzano la progressione tumorale in quanto intervengono in un processo che prende il nome di “angiogenic switch”, che consiste nella formazione di una nuova vascolarizzazione in grado di alimentare le cellule in attiva proliferazione. L’ ”angiogenic switch” inizia con la degradazione da parte delle gelatinasi del collagene IV, componente fondamentale della membrana basale vascolare. Esso, una volta processato, libera fattori (quali il VEGF) che stimolano le cellule endoteliali a migrare all’interno di una matrice provvisoria dove si formeranno i nuovi vasi sanguigni. Se da un lato le gelatinasi aumentano l’attività proliferativa delle cellule tumorali, dall’altra sono in grado di inibirla. Sembra infatti che la MMP-2, degradando il collagene di tipo IV, produca dei frammenti con attività anti-angiogenica in grado di bloccare la proliferazione tumorale. Ai fini di una miglior comprensione del ruolo delle Gelatinasi durante la progressione tumorale, abbiamo analizzato l’efficienza delle due metalloproteinasi verso il collagene di tipo IV; e nel caso della MMP-2 abbiamo caratterizzato il ruolo dei suoi diversi domini verso questo substrato naturale. Inoltre è stata effettuata una analisi basata sulla capacità dei neutrofili di migrare attraverso una membrana ricoperta di collagene di tipo IV in presenza di (i) una quantità esogena crescente di MMP-2 (ii) frammenti di arrestina derivanti dal processamento della catene  del collagene IV, (iii) MMP-2 mutata, ossia priva del suo dominio catalitico, (iv) del dominio ricombinante fibronectinico della MMP-2 o rCBD e (v) la MMP-2 inattiva o pro-MMP-2.Per finire abbiamo studiato l’esistenza di una possibile interazione tra le due gelatinasi nel processare il collagene di tipo IV sia in vitro che in condizioni ex vivo.I nostri risultati dimostrano come entrambe le gelatinasi processano il componente fondamentale delle membrane basale vascolare in condizioni fisiologiche, 37°C e pH 7,2. Inoltre l’MMP-2 interagisce con la MMP-9 aumentandone l’efficienza di processamento verso il collagene di tipo IV, per effetto di un controllo allosterico dovuto al semplice legame dell’enzima con il substrato. Quando la MMP-2 si lega al collagene IV per opera del suo dominio fibronectinico (CBD) , la MMP-9 processa il substrato con maggiore efficienza rispetto all’ azione quando è prsente da sola. Il fenomeno varia a seconda della concentrazione della MMP-2 che possiede due siti di legame per questo tipo di collagene: uno ad alta affinità ed un secondo sito con una scarsa affinità di legame. A bassa concentrazione di MMP-2 viene legato solo il sito del substrato per cui l’enzima posside una maggior affinità e di conseguenza la MMP-9 legandosi allo stesso substrato lo processa con maggior efficienza. Al contrario, ad alte concentrazioni di MMP-2, l’enzima si lega ad ambedue i siti di attacco che possiede nel collagene IV diminuendo la capacità della MMP-9 di processarlo, a causa di una probabile sovrapposizione del sito di attacco dei due enzimi.L’attività sinergica delle due gelatinasi viene riscontrata anche ex vivo, ossia mediante esperimenti di migrazione cellulare attraverso un coating di collagene IV. Le cellule utilizzate sono neutrofili, cellule in grado di esprimere vari enzimi proteolitici tra cui metalloproteinasi come la MMP-8 e la MMP-9 e proteasi a serina come l’elastasi del neutrofili. Risultano invece non produrre livelli apprezzabili di MMP-2, come dimostrato dalle zimografie delle Figure 10 e 11. I neutrofili, grazie alla MMP-9, sono quindi in grado di oltrepassare la barriera di collagene IV, che viene processato con maggior attività in presenza di quantità esogene di MMP-2 priva del dominio catalitico o in aggiunta del suo dominio di legame al substrato, il dominio ricombinante rCBD.
Proteolytic degradation of basement memnbrane influences the cell behaviour during important processes, such as inflammations, tumorigenesis, angiogenesis and allergic diseases. In this study, we have investigated the action of gelatinase A (MMP-2) and B (MMP-9) on collagen IV, the major constituent of the basement membrane. We have compared quantitatively their actions on the soluble forms of collagen IV extracted with or without pepsin (from human placenta and from Engelbreth-Holm-Swarm (EHS) murine sarcoma, respectively). The catalytic efficiency of MMP-2, and also MMP-9, is dramatically reduced in the case of the EHS murine sarcoma with respect to the human placenta, probably due to the much tighter packing of the network which renders very slow the speed of the rate-limiting step. We have also enquired on the role of MMP-2 domains in processing collagen IV. The removal of the hemopexin-like domain, using only the catalytic domain of MMP-2, has only a limited effect on the catalytic efficiency toward collagen IV, indicating that the missing domain has not a great relevance for the overall mechanism. Instead, the addition of the isolated collagen binding domain, corresponding to the fibronectin-like domain of whole MMP-2, greatly inhibits the cleavage process, demonstrating that MMP-2 interacts with collagen type IV preferentially through its fibronectin-like domain. Finally, we have investigated the effect of MMP-2 proteolytic activity ex vivo. MMP-2 action negatively affects the neutrophil cells migration across type IV coated membranes and this is likely related to the production of lower molecular weight fragments which impair the cellular migration.However, for both types of collagen IV the enzymatic processing by MMP-9 is dramatically enhanced in the presence of the Collagen Binding Domain of Gelatinase A (CBD). This effect, clearly indicates that the fibronectin-like domain of MMP-2 and MMP-9 bind to topologically distinct sites on type IV collagen, bringing about a conformational change of the collagen IV molecule. This allows the two enzymes to cooperate with each other through a ligand-linked mechanism, which does not necessarily require the enzymatic action. Therefore, fibronectin-like domains not only increase the affinity between enzyme and substrate to enhance the catalysis, they also act as allosteric third party elements in the MMP action. This synergistic action between MMP-2 and MMP-9 on collagen IV has been tested also with an ex vivo eperiment. The MMP-2 without the catalytic domain, the rCBD and the pro-MMP-2 increase the neutrophil cells migration across collagen IV coated membranesand this is related to the growth of the catalytic activity of MMP-9.
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Wolf, Katarina. "Migration of tumor cells and leukocytes in extracellular matrix proteolytic and nonproteolytic strategies for overcoming tissue barriers /." [S.l.] : [s.n.], 2003. http://deposit.ddb.de/cgi-bin/dokserv?idn=971018243.

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Books on the topic "Extracellular proteolysi"

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P, Mecham Robert, and SpringerLink (Online service), eds. Extracellular Matrix Degradation. Berlin, Heidelberg: Springer-Verlag Berlin Heidelberg, 2011.

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Matrix metalloproteinase protocols. 2nd ed. New York, N.Y: Humana Press, 2010.

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Mozrzymas, Jerzy W., and Leszek Kaczmarek, eds. Neuroplasticity and Extracellular Proteolysis. Frontiers Media SA, 2016. http://dx.doi.org/10.3389/978-2-88919-851-1.

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Parks, William C., and Robert Mecham. Extracellular Matrix Degradation. Springer, 2011.

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Parks, William C., and Robert Mecham. Extracellular Matrix Degradation. Springer, 2013.

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Behrendt, Niels. Matrix Proteases in Health and Disease. Wiley & Sons, Incorporated, John, 2012.

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Behrendt, Niels. Matrix Proteases in Health and Disease. Wiley & Sons, Incorporated, John, 2012.

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Behrendt, Niels. Matrix Proteases in Health and Disease. Wiley & Sons, Limited, John, 2012.

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Behrendt, Niels. Matrix Proteases in Health and Disease. Wiley & Sons, Limited, John, 2012.

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Behrendt, Niels. Matrix Proteases in Health and Disease. Wiley & Sons, Incorporated, John, 2012.

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Book chapters on the topic "Extracellular proteolysi"

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Bond, Judith S., Timothy R. Keiffer, and Qi Sun. "Pericellular Proteolysis." In Extracellular Matrix Degradation, 75–94. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16861-1_4.

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Brömme, Dieter, and Susan Wilson. "Role of Cysteine Cathepsins in Extracellular Proteolysis." In Extracellular Matrix Degradation, 23–51. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16861-1_2.

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Bugge, Thomas H., and Niels Behrendt. "Cooperation Between Proteolysis and Endocytosis in Collagen Turnover." In Extracellular Matrix Degradation, 53–74. Berlin, Heidelberg: Springer Berlin Heidelberg, 2011. http://dx.doi.org/10.1007/978-3-642-16861-1_3.

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Niedbala, Michael J. "Cytokine Regulation of Endothelial Cell Extracellular Proteolysis." In Proteases, Protease Inhibitors and Protease-Derived Peptides, 179–93. Basel: Birkhäuser Basel, 1993. http://dx.doi.org/10.1007/978-3-0348-7397-0_15.

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Baronas-Lowell, Diane, Janelle L. Lauer-Fields, Mohammad Al-Ghoul, and Gregg B. Fields. "Proteolytic Profiling of the Extracellular Matrix Degradome." In Peptide Characterization and Application Protocols, 167–202. Totowa, NJ: Humana Press, 2007. http://dx.doi.org/10.1007/978-1-59745-430-8_6.

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Werner, Fee, Kathrin Sachse, and Thomas Reinheckel. "Secreted Cysteine Cathepsins - Versatile Players in Extracellular Proteolysis." In Matrix Proteases in Health and Disease, 283–97. Weinheim, Germany: Wiley-VCH Verlag GmbH & Co. KGaA, 2012. http://dx.doi.org/10.1002/9783527649327.ch11.

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Pepper, Michael S., Jean-Dominique Vassalli, Lelio Orci, and Roberto Montesano. "Angiogenesis in Vitro: Cytokine Interactions and Balanced Extracellular Proteolysis." In Angiogenesis, 149–70. Boston, MA: Springer US, 1994. http://dx.doi.org/10.1007/978-1-4757-9188-4_19.

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Kramer, M. D., R. Batrla, G. M. Hänsch, and J. Reinartz. "Plasmin-Mediated Pericellular Proteolysis by Keratinocytes: Extracellular Matrix Reorganization vs Tissue Damage." In Wound Healing and Skin Physiology, 201–11. Berlin, Heidelberg: Springer Berlin Heidelberg, 1995. http://dx.doi.org/10.1007/978-3-642-77882-7_17.

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Goldfarb, Ronald H. "Proteolytic Enzymes in Tumor Invasion and Degradation of Host Extracellular Matrices." In Mechanisms of Cancer Metastasis, 341–75. Boston, MA: Springer US, 1986. http://dx.doi.org/10.1007/978-1-4613-2635-9_21.

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Anderson, M. John, Lauren E. Swenarchuk, and Shasikant Champaneria. "Localized Extracellular Proteolysis May Convey Inductive Signals Between Nerve and Muscle Cells During Synaptogenesis." In Serine Proteases and Their Serpin Inhibitors in the Nervous System, 255–73. Boston, MA: Springer New York, 1990. http://dx.doi.org/10.1007/978-1-4684-8357-4_23.

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Conference papers on the topic "Extracellular proteolysi"

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Wallace, Robert W., E. Ann Tallant, and Lynn M. Brumley. "POSSIBLE ROLE FOR THE CA2+-DEPENDENT PROTEASE (CALPAIN I) AS AN IRREVERSIBLE ACTIVATOR OF CA2+/CALMODULIN-MEDIATED REACTIONS IN THE HUMAN PLATELET." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644528.

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Calmodulin (CaM)-binding proteins have been identified in human platelets using Western blotting techniques and 125I-CaM. Ten proteins of 245, 225. 175, 150, 90. 82(2), 60 and 41(2) kilodaltons (kDa) bind 125I-CaM in a Ca2+-dependent manner; the binding is blocked by both trifluoperazine and nonradiolabeled CaM. The 225 and 90 kDa proteins are labeled by antisera against myosin light chain kinase (MLCK); the 60 kDa and one of the 82 kDa proteins have been identified as the CaM-dependent phosphatase (calcineurin) and caldesmon. The other proteins are presumed to be other Ca2+/CaM regulated enzymes and proteins which may be important in platelet function. Most of the CaM-binding proteins are degraded upon addition of Ca2+ to a platelet homogenate; the degradation may be blocked by either EGTA, leupeptin or N-ethylmaleimide which suggests that the degradation is due to a Ca2+-dependent protease. Activation of intact platelets under conditions which promote platelet aggregation (i.e. stirring with extracellular Ca2+) also results in limited proteolysis of CaM-binding proteins including those labeled with anti sera against MLCK and the phosphatase. In vitro studies utilizing purified phosphatase and calpain I indicate that the phosphatase is irreversibly activated upon Ca2+-dependent proteolysis. The proteolytically-activated enzyme is insensitive to either Ca2+ or Ca2+/CaM; in addition, its activity in the absence of Ca2+ is even greater than the activity of the unproteolyzed enzyme in the presence of Ca2+ and CaM. Proteolytic stimulation of the phosphatase is accompanied by degradation of the 60 kDa subunit of the enzyme (subunit A) to 56, 52 and 45 kDa fragments, sequentially; proteolysis results in the loss of CaM binding to the enzyme. These results suggest that the Ca2+-dependent protease may have a physiological role in platelet activation as an irreversible activator of Ca2+/ CaM-dependent reactions. Supported by NIH grant HL29766.
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Tanner, L., C. Andersson, J. Ljungberg, R. K. V. Bhongir, A. Egesten, and A. B. Single. "Citrullination of Extracellular Histone H3.1 Reduces Antibacterial Activity and Enhances Proteolytic Degradation by Neutrophil Elastase." In American Thoracic Society 2020 International Conference, May 15-20, 2020 - Philadelphia, PA. American Thoracic Society, 2020. http://dx.doi.org/10.1164/ajrccm-conference.2020.201.1_meetingabstracts.a7446.

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Wilson, Christopher G., and Marc E. Levenston. "Chondrocytes and Fibrochondrocytes Differentially Process Aggrecan During De Novo Extracellular Matrix Assembly." In ASME 2007 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2007. http://dx.doi.org/10.1115/sbc2007-176669.

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The material properties of articular cartilage and meniscal fibrocartilage depend on the composition and ultrastructure of the extracellular matrix (ECM). Aggrecan is the predominant large proteoglycan in these tissues, and confers compressive stiffness through immobilization of negatively charged sulfated glycosaminoglycans (sGAG). The abundance of sGAG is in part regulated by cell-mediated proteolysis of the aggrecan core protein, and transforming growth factor-β (TGF-β) family cytokines upregulate aggrecan synthesis in chondrocytes and fibrochondrocytes. The function(s) of aggrecan and mechanisms of aggrecan processing in the meniscus, however, are not well understood. The objective of this study was to examine tissue-specific kinetics and mechanisms of TGF-β-induced aggrecan turnover using the cell-agarose culture system. In addition, the tissue-specific functional implications of increased proteoglycan production were evaluated in terms of construct material properties.
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Ghilardi, Carmen, Figini Sara, Monica Lupi, Alessia Anastasia, Raffaella Giavazzi, and Mariarosa Bani. "Abstract 4169: Tumor endothelium regulates microenvironment-mediated migration via the proteolysis of extracellular TFPI-2 by trypsinogen 4." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-4169.

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Lam, My-Hanh, Judy Lucas, Andreas Maderna, Hallie Wald, Megan Wojciechowicz, Russell Dushin, Bryan Peano, et al. "Abstract 4837: Extracellular proteolytic cleavage of peptide-linked antibody-drug conjugates promotes bystander killing of cancer cells." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4837.

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Wagner, D. D., P. J. Fay, L. A. Sporn, S. Sinha, S. O. Lawrence, and V. J. Marder. "DIVERGENT PATES OF VON WILLEBRAND FACTOR AND ITS PROPOLYPEPTIDE (VON WILLEBRAND ANTIGEN II) AFTER SECRETION FROM ENDOTHELIAL CELLS." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642832.

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The intracellular site of cleavage of pro-von Willebrand factor subunit and the subsequent fate of the propolypeptide (von Willebrand antigen II) and of the mature von Willebrand factor (vWf) were investigated. Both the propolypeptide, which was found to be a homodimer of non-covalently linked subunits, and mature vWf were released from Weibel-Palade bodies of endothelial cells following stimulation with secretagogues. The stoichiometry of the two proteins in the releasate was essentially equimolar. This indicates that vWf and the propolypeptide were packaged into the Weibel-Palade bodies as one unit, pro-vWf, and that the proteolytic cleavage of pro-vWf is likely to be a post-Golgi event. The association of prosequences into dimers provides support for their hypothetical role in the multimerization process. After secretion, the two proteins were distributed differently, as based on the following observations. The propolypeptide did not associate with vWf in the culture medium, did not co-distribute with vWf in the extracellular "patches of release" on stimulated endothelial cells, and was not detected in the endothelial cell extracellular matrix, which did contain vWf. Additionally, in contrast to vWf, the propolypeptide did not bind to matrix of human foreskin fibroblasts. Since the propolypeptide does not associate with vWf and does not interact witji extracellular matrices in vitro, it is highly unlikely that it would promote platelet adhesion to subendothelium in vivo.
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Wasi, S., S. Juodvalkis, P. Alles, and J. E. Aubin. "STUDIES ON THE DIRECT PROTEOLYTIC ACTION OF HUMAN TISSUE PLASMINOGEN ACTIVATOR ON HUMAN FIBRONECTIN AND VITRONECTIN." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1644376.

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The ability of cells to make or break specific attachments to extracellular matrix (ECM) and other cells is important in cell migration, proliferation and wound repair. Specific attachment proteins believed to be involved in mediating these interactions comprise functional domains joined by protease sensitive segments. Proteases can conceivably modulate cellular interactions by releasing functional domains from parent molecules. Tissue plasminogen activator (t-pA) is known to participate in various pathophysiological processes. That t-pA may also act directly on structural proteins has not been investigated. We have studied the direct proteolytic action of melanoma t-pA on fibronectin (FN), vitronectin (VN) and laminin (LN). These were incubated with t-pA for 0 to 48 h in 50 mM Tris HCi, pH 7.4. The cleavage products were separated on polyacrylamide slab gels and blotted onto nitrocellulose strips. FN and VN fragments with cell attachment properties were identified by incubating the strips with human gingiva fibroblasts and staining with Amido black. Monoclonal antibodies to FN were used to identify heparin, cell and gelatin binding fragments. VN was converted to a major 55 Kd product as a function of time. Lower molecular weight species migrating at 45 Kd, 30 Kd and 15 Kd positions were also identified. Most of these fragments possessed cell attachment properties. LN became susceptible to t-pA digestion after dénaturation with H2O2. The catalytic activity of t-pA could be inhibited in the presence of nitrophenyl-p-guinidino benzoate (a synthetic inhibitor of plasminogen activator), whereas O-phenanthroline (a metalloprotease inhibitor), α 2-antiplasmin and trasylol had no effect. A monoclonal IgG preparation (HI 72 A1, kindly provided by Dr. David J. Loskutoff) that specifically inhibits t-pA also inhibited the protelyotic action of t-pA on FN. These data suggest that direct proteolytic action of t-pA on adhesive proteins may modulate cellular behaviour in various normal and pathological conditions which involve dynamic interactions between cells and ECM and where plasminogen activator levels are elevated either transiently or permanently, for example during tissue remodelling, wound-related repair and thrombolytic therapy.
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Hatton, Mark W. C., Susan Moar, and Mary Richardson. "THE BEHAVIOUR OF RABBIT PLASMINOGEN AT THE LUMINAL SURFACE OF RABBIT AORTA IN VIVO BEFORE AND AFTER BALLOON-CATHETER INJURY." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1643578.

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A previous study from this laboratory has identified the susceptibility of the de-endothelialised aorta, particularly the proteoglycan (PG) components of the extracellular matrix (ECM), to proteolytic damage if exposed to plasmin in vitro. To explore the possiblity that this occurs in vivo, a possible association between 125I-plasminogen (PLG) binding to the arterial wall, its activation to plasmin (PLN) and, subsequently, proteolytic damage to the intimal ECM has been studied. Intravenous injection of 125I-PLG in healthy N.Z. white male rabbits showed that PLG associated minimally (<0.01% of circulating PLG/cm2 /ml blood at 1 h) with the thoracic aorta endothelium, measured after Hautchen preparation from 1-cm vessel segments. Trans endothelial passage, measured as 125I-PLG associated with thg subendothelium (intima-media), progressed to 0.015%/cm2 /ml blood at 1 h. In contrast, the process of de-endothelialisation by balloon catheter led to a rapid uptake of bI-PLG by the denuded vessel surface. At saturation (approx. 10 min after injury), 0.7 - 0.8% of circulating PLG/cm2/ml blood was adsorbed by the entire de-endothelialised intima-media: Of the adsorbed PLG, 2-3% was associated with the platelet layer. Uptake was not inhibited by eACA (dose: 200 mg/kg) given i.v. before I-PLG. Adsorbed PLG was not released significantly from segments incubated in MEM containing 4% (w/v) RSA in vitro PLN activity was not detected. Furthermore, assessment of the ECM by transmission electron microscopy, after ruthenium red staining, showed that uptake of PLG by the de-endothelialised vessel in vivo was not associated with obvious damage to the PG components. Supported by the Heart and Stroke Foundation of Ontario.
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Hurley, Jennifer R., Abdul Q. Sheikh, Meredith Beckenhaupt, Cameron Ingram, Andrew Mutchler, and Daria A. Narmoneva. "Self-Assembling Peptide Nanofibers for MMP Delivery and Cardiac Regeneration in Diabetes." In ASME 2011 Summer Bioengineering Conference. American Society of Mechanical Engineers, 2011. http://dx.doi.org/10.1115/sbc2011-53761.

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Diabetes is a serious problem in the United States, afflicting 7.8% of the population with annual medical costs estimated at $116B in 2007 (1). Diabetic cardiomyopathy (DCM) is a cardiovascular complication of diabetes resulting in pathological alterations to the myocardium including circulatory defects, impaired heart muscle contraction, and progressive fibrosis. Cardiac fibrosis is associated with an imbalance between the deposition of the extracellular matrix (ECM) proteins by cardiac fibroblasts and the ECM proteolytic degradation via matrix metalloproteinases (MMPs). Recent studies have demonstrated that in the diabetic heart, expression and activity of MMP-2 are reduced, resulting in increased collagen accumulation and cardiac dysfunction (2). These observations suggest that a MMP-related mechanism may contribute to cardiac fibrosis, and that it may be attenuated through stimulation of native MMP-2 expression or delivery of exogenous MMP-2. Therefore, reduced MMP-2 activity in DCM may represent a novel target for therapeutic treatment (3). To achieve this, a special proteolytically-stable delivery scaffold would be needed, because native ECM is rapidly degraded by MMPs. The goal of this study is to determine if self-assembling peptide nanofibers can be used for long-term (several weeks) MMP delivery and enhancement of cardiac remodeling. This study tests the hypothesis that increased MMP-2 concentration (native or exogenous) in the nanofiber environment will promote matrix remodeling in diabetic cardiac fibroblasts in vitro.
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Andreasen, P. A., A. Riccio, L. R. Lund, K. G. Welinder, F. Blasi, and K. Danø. "PLASMINOGEN ACTIVATOR INHIBITOR TYPE 1: STUDIES ON STRUCTURE AND REGULATION." In XIth International Congress on Thrombosis and Haemostasis. Schattauer GmbH, 1987. http://dx.doi.org/10.1055/s-0038-1642810.

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Abstract:
Human plasminogen activator inhibitor type-1 is an Mr∼54,000 protein which specifically inhibits urokinase-type (u-PA) and tissue-type (t-PA) plasminogen activators. During inhibition, u-PA and t-PA convert PAI-1 to an inactive form with Mr∼50,000. We have determined the amino-terminal amino acid sequence of native and converted PAI-1, and isolated and partly sequenced PAI-1 cDNA. The data show that the conversion of PAI-1 consists of cleavage of an Arg-Met bond 33 residues from the carboxy-terminus, thus localizing the reactive center of the inhibitor to that position, and identifying PAI-1 as an "arg-serpin". PAI-1 activity is known to be influenced by a number of agents; we have studied the mechanisms of the stimulation of PAI-1 activity by transforming growth factor-β (TGF-β) and the synthetic glucocorticoid dexame-thasone in human WI-38 lung fibroblasts and HT-1080 fibrosarcoma cells. Bytheuse of PAI-1 cDNA, TGF-β was found to course a rapid increase in PAI-1 mRNA level in WI-38 cells, reaching a maximal 50-fold enhancement after 8 hours. Dexamethasone caused a 10-fold increase in PAI-1 mRNA in HT-1080 cells, which was detectable after 4 hours and became maximal after 16 hours. In both cases, the 3.4 as well as the 2.4 Kb-PAI-1-mRNA species were increased. Quantitative studies on the effect of these agents on PAI-1 protein levels in cell extracts and culture media by ELISA gave results consistent with the effects on PAI-1 mRNA. These studies suggest that TGF-β and glucocorticoids may exert important controls over plasminogen activation-mediated extracellular proteolysis through an enhancement of PAI-1 gene transcription.
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