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The streptococcal c...
The streptococcal collagen-binding protein CNE specifically interferes with {alpha}V{beta}3-mediated cellular interactions with triple helical collagen
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- van Wieringen, Tijs (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Kalamajski, Sebastian (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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- Lidén, Åsa (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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Bihan, Dominique (author)
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- Guss, Bengt (author)
- Swedish University of Agricultural Sciences,Sveriges lantbruksuniversitet,Institutionen för mikrobiologi,Department of Microbiology
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- Heinegård, Dick (author)
- Lund University,Lunds universitet,Reumatologi och molekylär skelettbiologi,Sektion III,Institutionen för kliniska vetenskaper, Lund,Medicinska fakulteten,Rheumatology,Section III,Department of Clinical Sciences, Lund,Faculty of Medicine
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Farndale, Richard W. (author)
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- Rubin, Kristofer (author)
- Uppsala universitet,Institutionen för medicinsk biokemi och mikrobiologi
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(creator_code:org_t)
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- 2010
- 2010
- English.
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In: Journal of Biological Chemistry. - 0021-9258 .- 1083-351X. ; 285:46, s. 35803-35813
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Abstract
Subject headings
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- Collagen fibers expose distinct domains allowing for specific interactions with other extracellular matrix proteins and cells. To investigate putative collagen domains that govern integrin α(V)β(3)-mediated cellular interactions with native collagen fibers we took advantage of the streptococcal protein CNE that bound native fibrillar collagens. CNE specifically inhibited α(V)β(3)-dependent cell-mediated collagen gel contraction, PDGF BB-induced and α(V)β(3)-mediated adhesion of cells, and binding of fibronectin to native collagen. Using a Toolkit composed of overlapping, 27-residue triple helical segments of collagen type II, two CNE-binding sites present in peptides II-1 and II-44 were identified. These peptides lack the major binding site for collagen-binding β(1) integrins, defined by the peptide GFOGER. Peptide II-44 corresponds to a region of collagen known to bind collagenases, discoidin domain receptor 2, SPARC (osteonectin), and fibronectin. In addition to binding fibronectin, peptide II-44 but not II-1 inhibited α(V)β(3)-mediated collagen gel contraction and, when immobilized on plastic, supported adhesion of cells. Reduction of fibronectin expression by siRNA reduced PDGF BB-induced α(V)β(3)-mediated contraction. Reconstitution of collagen types I and II gels in the presence of CNE reduced collagen fibril diameters and fibril melting temperatures. Our data indicate that contraction proceeded through an indirect mechanism involving binding of cell-produced fibronectin to the collagen fibers. Furthermore, our data show that cell-mediated collagen gel contraction does not directly depend on the process of fibril formation.
Subject headings
- LANTBRUKSVETENSKAPER -- Husdjursvetenskap (hsv//swe)
- AGRICULTURAL SCIENCES -- Animal and Dairy Sience (hsv//eng)
- LANTBRUKSVETENSKAPER -- Veterinärmedicin (hsv//swe)
- AGRICULTURAL SCIENCES -- Veterinary Science (hsv//eng)
- MEDICIN OCH HÄLSOVETENSKAP -- Klinisk medicin -- Reumatologi och inflammation (hsv//swe)
- MEDICAL AND HEALTH SCIENCES -- Clinical Medicine -- Rheumatology and Autoimmunity (hsv//eng)
Keyword
- MEDICINE
- MEDICIN
Publication and Content Type
- ref (subject category)
- art (subject category)
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