Integrin αVβ3 can substitute for collagen‐binding β1‐integrins in vivo to maintain a homeostatic interstitial fluid pressure

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Fältnamn	Indikatorer	Metadata
000		05055naa a2200505 4500
001		oai:DiVA.org:uu-356075
003		SwePub
008		180713s2018 \| \|\|\|\|\|\|\|\|\|\|\|000 \|\|eng\|
009		oai:lup.lub.lu.se:7815ff2c-86b0-4f68-b201-de7db8f98ffe
024	7	a https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-3560752 URI
024	7	a https://doi.org/10.1113/EP0869022 DOI
024	7	a https://lup.lub.lu.se/record/7815ff2c-86b0-4f68-b201-de7db8f98ffe2 URI
040		a (SwePub)uud (SwePub)lu
041		a engb eng
042		9 SwePub
072	7	a ref2 swepub-contenttype
072	7	a art2 swepub-publicationtype
100	1	a Liden, Åsau Univ Bergen, Dept Biomed, Bergen, Norway,University of Bergen4 aut
245	1 0	a Integrin αVβ3 can substitute for collagen‐binding β1‐integrins in vivo to maintain a homeostatic interstitial fluid pressure
264	1	c 2018
338		a electronic2 rdacarrier
500		a WoS title: Integrin alpha(V)beta(3) can substitute for collagen-binding beta(1)-integrins in vivo to maintain a homeostatic interstitial fluid pressurel
520		a Accumulated data indicate that cell‐mediated contraction of reconstituted collagenous gels in vitro can serve as a model for cell‐mediated control of interstitial fluid pressure (PIF) in vivo. A central role for collagen‐binding β1‐integrins in both processes has been established. Furthermore, integrin αVβ3 takes over the role of collagen‐binding β1‐integrins in mediating contraction after perturbations of collagen‐binding β1‐integrins in vitro. Integrin αVβ3 is also instrumental for normalization of dermal PIF that has been lowered due to mast cell degranulation with compound 48/80 (C48/80) in vivo. Here we demonstrate a role of integrin αVβ3 in maintaining a long term homeostatic dermal PIF in mice lacking the collagen‐binding integrin α11β1 (α11−/− mice). Measurements of PIF were performed after circulatory arrest. Furthermore, cell‐mediated integrin αVβ3‐directed contraction of collagenous gels in vitro depends on free access to a collagen site known to bind several extracellular matrix (ECM) proteins that form substrates for αVβ3‐directed cell attachment, such as fibronectin and fibrin. A streptococcal collagen‐binding protein, CNE, specifically binds to and blocks this site on the collagen triple helix. Here we show that whereas CNE perturbed αVβ3‐directed and platelet‐derived growth factor BB‐induced normalization of dermal PIF after C48/80, it did not affect αVβ3‐dependent maintenance of a homeostatic dermal PIF. These data imply that dynamic modification of the ECM structure is needed during acute patho‐physiological modulations of PIF but not for long‐term maintenance of a homeostatic PIF. Our data thus show that collagen‐binding β1‐integrins, integrin αVβ3 and ECM structure are potential targets for novel therapy aimed at modulating oedema formation and hypovolemic shock during anaphylaxis.
650	7	a NATURVETENSKAPx Biologix Biokemi och molekylärbiologi0 (SwePub)106022 hsv//swe
650	7	a NATURAL SCIENCESx Biological Sciencesx Biochemistry and Molecular Biology0 (SwePub)106022 hsv//eng
650	7	a MEDICIN OCH HÄLSOVETENSKAPx Medicinska och farmaceutiska grundvetenskaperx Cell- och molekylärbiologi0 (SwePub)301082 hsv//swe
650	7	a MEDICAL AND HEALTH SCIENCESx Basic Medicinex Cell and Molecular Biology0 (SwePub)301082 hsv//eng
653		a contraction
653		a extracellular matrix
653		a microcirculation
653		a contraction
653		a extracellular matrix
653		a microcirculation
700	1	a Karlsen, Tine Veronikau Univ Bergen, Dept Biomed, Bergen, Norway,University of Bergen4 aut
700	1	a Guss, Bengtu Swedish University of Agricultural Sciences4 aut
700	1	a Reed, Rolf K.u Univ Bergen, Dept Biomed, Bergen, Norway; Univ Bergen, Ctr Canc Biomarkers CCBIO, Bergen, Norway,University of Bergen4 aut
700	1	a Rubin, Kristoferu Uppsala University,Lund University,Lunds universitet,Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi,Lund Univ, Dept Lab Med, Translat Canc Res, Sweden,Avdelningen för translationell cancerforskning,Institutionen för laboratoriemedicin,Medicinska fakulteten,Division of Translational Cancer Research,Department of Laboratory Medicine,Faculty of Medicine4 aut0 (Swepub:lu)med-krn
710	2	a Univ Bergen, Dept Biomed, Bergen, Norwayb University of Bergen4 org
773	0	t Experimental Physiologyg 103:5, s. 629-634q 103:5<629-634x 0958-0670x 1469-445X
856	4	u https://doi.org/10.1113/EP086902y Fulltext
856	4	u https://uu.diva-portal.org/smash/get/diva2:1232959/FULLTEXT01.pdfx primaryx Raw objecty fulltext:print
856	4	u http://dx.doi.org/10.1113/EP086902x freey FULLTEXT
856	4 8	u https://urn.kb.se/resolve?urn=urn:nbn:se:uu:diva-356075
856	4 8	u https://doi.org/10.1113/EP086902
856	4 8	u https://lup.lub.lu.se/record/7815ff2c-86b0-4f68-b201-de7db8f98ffe

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Av författaren/redakt...: Liden, Åsa; Karlsen, Tine Ve ...; Guss, Bengt; Reed, Rolf K.; Rubin, Kristofer

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NATURVETENSKAP: NATURVETENSKAP; och Biologi; och Biokemi och mole ...

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