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Träfflista för sökning "WFRF:(Heinegård Dick) ;pers:(Franzén Ahnders)"

Sökning: WFRF:(Heinegård Dick) > Franzén Ahnders

  • Resultat 1-7 av 7
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  • Franzén, Ahnders, et al. (författare)
  • Altered osteoclast development and function in osteopontin deficient mice.
  • 2008
  • Ingår i: Journal of Orthopaedic Research. - : Wiley. - 1554-527X .- 0736-0266. ; 26:5, s. 721-728
  • Tidskriftsartikel (refereegranskat)abstract
    • The role of osteopontin in bone resorption was elucidated by studies of mice with knock out of the osteopontin gene generated by a different approach compared to previous models. Thus, a targeting vector with the promoter region as well as exons 1, 2, and 3 of the osteopontin gene was replaced by a loxP-flanked Neo-TK cassette, and this cassette was eliminated through transient expression of Cre recombinase. The recombined ES cells were used to create mice lacking expression of the osteopontin gene. Tissues from these mice were subjected structural and molecular analyses including morphometry and proteomics. The bone of the null mice contained no osteopontin but showed no significant alterations with regard to other bone proteins. The bone volume was normal in young null animals but in the lower metaphysis, the volume and number of osteoclasts were increased. Notably, the volume and length of the osteoclast ruffled border was several folds lower, indicating a lower resorptive capacity. The null mice did not develop the bone loss characteristic for osteoporosis demonstrated in old wild-type female animals. This quantitative study demonstrates a bone phenotype in the osteopontin null mice of all ages. The data provides further evidence for a role of osteopontin in osteoclast activity. (c) 2007 Orthopaedic Research Society. Published by Wiley Periodicals, Inc. J Orthop Res.
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  • Heinegård, Dick, et al. (författare)
  • Glycosylated matrix protein
  • 2002
  • Ingår i: Connective tissue and its heritable disorders: molecular, genetic, and medical aspects, 2nd edition. - Hoboken, NJ, USA : John Wiley & Sons, Inc.. - 9780471251859 ; , s. 271-291
  • Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
    • Connective tissues have many features in common, including resisting and dissipating mechanical load and providing shape, as well as acting to provide barriers regulating water flow and diffusibility of macromolecules. In this chapter we have chosen to focus on cartilage and bone, covering many aspects of connective tissues. We give special focus to the noncollagenous proteins in their matrices.
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4.
  • Heinegård, Dick, et al. (författare)
  • Glycosylated Matrix Proteins
  • 2002
  • Ingår i: Connective Tissue and Its Heritable Disorders: Molecular, Genetic and Medical Aspects. - Hoboken, NJ, USA : John Wiley & Sons, Inc.. - 9780471251859 - 9780471221920 ; , s. 271-291
  • Bokkapitel (övrigt vetenskapligt/konstnärligt)abstract
    • Connective tissues have many features in common, including resisting and dissipating mechanical load and providing shape, as well as acting to provide barriers regulating water flow and diffusibility of macromolecules. In this chapter we have chosen to focus on cartilage and bone, covering many aspects of connective tissues. We give special focus to the noncollagenous proteins in their matrices.
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5.
  • Ramstad, VE, et al. (författare)
  • Ultrastructural distribution of osteoadherin in rat bone shows a pattern similar to that of bone sialoprotein
  • 2003
  • Ingår i: Calcified Tissue International. - : Springer Science and Business Media LLC. - 1432-0827 .- 0171-967X. ; 72:1, s. 57-64
  • Tidskriftsartikel (refereegranskat)abstract
    • Osteoadherin (OSAD) is a keratan sulfate proteoglycan recently isolated from bovine and rat bone. Based on results obtained from in vitro experiments, the protein was shown to bind osteoblasts via the integrin receptor alpha(v)beta(3). Due to OSAD's capacity to bind hydroxyapatite crystals, a role for the protein in the mineralization process has also been suggested. To test these hypotheses in an in vivo model, the ultrastructural localization of OSAD in bone, tibial (metaphyses and diaphyses). and calvarial samples from normal 10 to 12-day-old rats were examined by immunohistochemical techniques at the ultrastructural level. In addition to the qualitative studies, quantitative measurements of OSAD marker density were performed in relevant compartments. Immunolabeling for OSAD was located to the mineralized bone matrix, with highest concentration of marker at the border between bone and cartilage remnants in the metaphyseal trabeculi. Intracellular labeling was low and no systemic accumulation of OSAD markers was observed at the cell-matrix interface. The observed distribution pattern of OSAD is strikingly similar to that of bone sialoprotein (BSP), confirmed by double labeling. The results of the current study support a role for OSAD in the mineralization process. In this process BSP is assumed to be a nucleator of hydroxyapatite crystals, and OSAD could work in concert with BSP to regulate nucleation. However, the mechanisms involved remain to be elucidated.
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6.
  • Ström, Åsa, et al. (författare)
  • Altered Vascular Remodeling in Osteopontin-Deficient Atherosclerotic Mice.
  • 2004
  • Ingår i: Journal of Vascular Research. - : S. Karger AG. - 1423-0135 .- 1018-1172. ; 41:4, s. 314-322
  • Tidskriftsartikel (refereegranskat)abstract
    • <i>Background:</i> Osteopontin (OPN) is a cell-binding phosphoprotein with proposed functions in atherosclerosis. The aim of this study was to examine how OPN deficiency affects the atherosclerotic process. <i>Methods:</i> ApoE/LDL receptor/OPN triple knockout (ALO) mice were generated by crossing OPN null mice with ApoE/LDL receptor-deficient (AL) mice. Analysis were made on tissue sections from the aortic arch of 8-, 20- and 34-week female AL and ALO mice and included morphometric measurements, collagen staining, TUNEL staining and immunohistochemistry with antibodies to OPN, macrophages and proliferating cellular nuclear antigen (PCNA). <i>Results:</i> Lesion and media areas were significantly smaller and collagen accumulation in lesions was significantly reduced in 34-week-old ALO mice compared with AL mice. The numbers of proliferating and apoptotic cells were increased in lesions of 34 weeks old ALO mice. Furthermore, the plasma levels of SAA and total cholesterol were significantly decreased in 34 weeks old ALO mice. <i>Conclusions:</i> The present study shows that OPN deficiency reduces atherogenesis in atherosclerotic mice. The results corroborate and extend recently published findings and also include novel data on the role of OPN in the process of remodeling, inflammation and lipid metabolism.
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  • Resultat 1-7 av 7

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