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In animal models, unaccustomed eccentric exercise (EE) has been widely related to muscle fiber membrane (sarcolemma) damage. On the contrary, studies in humans reported that sarcolemma was not susceptible to damage following a single bout of EE. We hypothesized that the single bout of EE used by those studies was not sufficient to induce sarcolemma damage, in humans. In this study we examined muscle biopsies from untrained males who either performed six sets of 15 reps of maximum voluntary eccentric contractions (n=9), for six consecutive days, or served as control-group (n=6). Blood and biopsy samples were obtained one week prior to exercise, immediately after bout 3, and 24h after the last training session. In addition to standard haematoxylin-eosin staining, all biopsies were stained immunohistochemically using antibodies specific for fibronectin and desmin antigens. In the exercise-group, no biopsies taken at pre-exercise or post-exercise level showed evidence of sarcolemma damage as stained by anti-fibronectin antibody in eight of nine subjects. Serum creatine kinase (CK) and lactate dehydrogenase (LDH) activities increased significantly throughout the study despite the lack of sarcolemma damage.We suggest that in humans, repeated bouts of EE do not cause gross sarcolemma damage in the mid-belly of Vastus Lateralis.

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1980 19 517 525 Grinnell, F., Billingham, R. E., Burgess, L.: Distribution of fibronectin during wound

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.: Distribution of fibronectin during wound healing in vivo. J. Invest. Dermatol., 1981, 76 , 181–189. Burgess L. Distribution of fibronectin during wound healing in vivo

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European Journal of Microbiology and Immunology
Authors: Manja Boehm, Daniel Simson, Ulrike Escher, Anna-Maria Schmidt, Stefan Bereswill, Nicole Tegtmeyer, Steffen Backert and Markus M. Heimesaat

adhesion to fibronectin (CadF) [ 23 , 24 ], major outer membrane protein (MOMP) [ 25 ], periplasmic binding protein (PEB1) [ 26 ], P95 [ 27 ], jejuni lipoprotein A (JlpA) [ 28 , 29 ], Campylobacter autotransporter protein A (CapA) [ 30 ], and

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Magyar Onkológia
Authors: Miklós Petrás, Gábor Hutóczki, Imre Varga, György Vereb, János Szöllősi, László Bognár, Péter Ruszthi, Annamária Kenyeres, Judit Tóth, Zoltán Hanzély, Beáta Scholtz and Álmos Klekner

. 5. EHJ Danen KM Yamada 2001 Fibronectin, integrins, and growth control J Cell Physiol

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European Journal of Microbiology and Immunology
Authors: Jana Niemz, Stefanie Kliche, Marina C. Pils, Eliot Morrison, Annika Manns, Christian Freund, Jill R. Crittenden, Ann M. Graybiel, Melanie Galla, Lothar Jänsch and Jochen Huehn

Using quantitative phosphopeptide sequencing of unstimulated versus stimulated primary murine Foxp3+ regulatory and Foxp3 conventional T cells (Tregs and Tconv, respectively), we detected a novel and differentially regulated tyrosine phosphorylation site within the C1 domain of the guanine-nucleotide exchange factor CalDAG GEFI. We hypothesized that the Treg-specific and activation-dependent reduced phosphorylation at Y523 allows binding of CalDAG GEFI to diacylglycerol, thereby impacting the formation of a Treg-specific immunological synapse. However, diacylglycerol binding assays of phosphomutant C1 domains of CalDAG GEFI could not confirm this hypothesis. Moreover, CalDAG GEFI−/− mice displayed normal Treg numbers in thymus and secondary lymphoid organs, and CalDAG GEFI−/− Tregs showed unaltered in vitro suppressive capacity when compared to CalDAG GEFI+/+ Tregs. Interestingly, when tested in vivo, CalDAG GEFI−/− Tregs displayed a slightly reduced suppressive ability in the transfer colitis model when compared to CalDAG GEFI+/+ Tregs. Additionally, CRISPR-Cas9-generated CalDAG GEFI−/− Jurkat T cell clones showed reduced adhesion to ICAM-1 and fibronectin when compared to CalDAG GEFI-competent Jurkat T cells. Therefore, we speculate that deficiency in CalDAG GEFI impairs adherence of Tregs to antigen-presenting cells, thereby impeding formation of a fully functional immunological synapse, which finally results in a reduced suppressive potential.

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A Toll-like receptor-4 a természetes immunválasz egyik központi mediátora. Fő ligandja a Gram-negatív baktériumok lipopoliszacharidja, de emellett más molekulák is kötődnek a receptorhoz, mint például a hősokkprotein-60, az oxidált alacsony denzitású lipoprotein és a fibronektin. A receptor aktivációja a proinflammatorikuscitokin-szint növekedésével jár. Az elmúlt évek kutatási eredményei kimutatták, hogy a Toll-like receptor-4 a fertőző ágensek elleni immunválaszon kívül olyan krónikus gyulladásos reakcióval járó egyéb betegségekben is részt vehet, mint például az atherosclerosis, a diabetes mellitus vagy a gyulladásos bélbetegségek. A közlemény bemutatja a receptorral kapcsolatos újabb ismereteket, a receptor gyakori koszegregációs polimorfizmusait, valamint a polimorfizmusok különböző megbetegedésekre gyakorolt hatását.

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C.R. Young 1999 The absence of cecal colonization of chicks by a mutant of Campylobacter jejuni not expressing bacterial fibronectin-binding protein Avian Dis

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Acta Microbiologica et Immunologica Hungarica
Authors: N. Regéczy, L. Kormos, Cs. M. Szigetvári, É. Torbágyi, M. Hajdu, L. Gopcsa, A. Bányai and K. Pálóczi

the immunoglobulin superfamily with binding domains similar to fibronectin. Nature 334 , 701 (1988). Neural adhesion molecule L 1 as a member of the immunoglobulin superfamily with binding domains similar to fibronectin

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931 Euker TP, Konkel ME: The cooperative action of bacterial fibronectin-binding proteins and secreted proteins promote maximal Campylobacter jejuni invasion of host cells by stimulating

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