| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
Regular Articles |
1ß1 Integrin-Deficient Mice during Bone Fracture Healing
From the Departments of Medical Biochemistry and Molecular Biology,*Surgery,and the MediCity Research Laboratory,University of Turku, Turku, Finland; Biogen Limited,¶Cambridge, Massachusetts; and the Orthopaedic Research Laboratories,University of Michigan, Ann Arbor, Michigan
Integrins mediate cell adhesion to extracellular matrix components. Integrin 
1ß1 is a collagen receptor expressed on many mesenchymal cells, but mice deficient in 1 integrin (1-KO) have no gross structural defects. Here, the regeneration of a fractured long bone was studied in 1-KO mice. These mice developed significantly less callus tissue than the wild-type (WT) mice, and safranin staining revealed a defect in cartilage formation. The mRNA levels of nine extracellular matrix genes in calluses were evaluated by Northern blotting. During the first 9 days the mRNA levels of cartilage-related genes, including type II collagen, type IX collagen, and type X collagen, were lower in 1-KO mice than in WT mice, consistent with the reduced synthesis of cartilaginous matrix appreciated in tissue sections. Histological observations also suggested a diminished number of chondrocytes in the 1-KO callus. Proliferating cell nuclear antigen staining revealed a reduction of mesenchymal progenitors at the callus site. Although, the number of mesenchymal stem cells (MSCs) obtained from WT and 1-KO whole marrow was equal, in cell culture the proliferation rate of the MSCs of 1-KO mice was slower, recapitulating the in vivo observation of reduced callus cell proliferation. The results demonstrate the importance of proper collagen-integrin interaction in fracture healing and suggest that 1 integrin plays an essential role in the regulation of MSC proliferation and cartilage production.
This article has been cited by other articles:
 |
|
 |
|
  H. Yamazaki, M. Tsuneto, M. Yoshino, K.-I. Yamamura, and S.-I. Hayashi Potential of Dental Mesenchymal Cells in Developing Teeth Stem Cells, January 1, 2007; 25(1): 78 - 87. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 T. Kuorilehto, E. Ekholm, M. Nissinen, K. Hietaniemi, A. Hiltunen, P. Paavolainen, R. Penttinen, and J. Peltonen NF1 Gene Expression in Mouse Fracture Healing and in Experimental Rat Pseudarthrosis J. Histochem. Cytochem., March 1, 2006; 54(3): 363 - 370. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 D. Davidson, A. Blanc, D. Filion, H. Wang, P. Plut, G. Pfeffer, M. D. Buschmann, and J. E. Henderson Fibroblast Growth Factor (FGF) 18 Signals through FGF Receptor 3 to Promote Chondrogenesis J. Biol. Chem., May 27, 2005; 280(21): 20509 - 20515. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Kapyla, J. Jaalinoja, M. Tulla, J. Ylostalo, L. Nissinen, T. Viitasalo, P. Vehvilainen, V. Marjomaki, P. Nykvist, A.-M. Saamanen, et al. The Fibril-associated Collagen IX Provides a Novel Mechanism for Cell Adhesion to Cartilaginous Matrix J. Biol. Chem., December 3, 2004; 279(49): 51677 - 51687. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 X. Chen, G. Moeckel, J. D. Morrow, D. Cosgrove, R. C. Harris, A. B. Fogo, R. Zent, and A. Pozzi Lack of Integrin {alpha}1{beta}1 Leads to Severe Glomerulosclerosis after Glomerular Injury Am. J. Pathol., August 1, 2004; 165(2): 617 - 630. [Abstract] [Full Text] [PDF]
|
|
|
|
|
|
J. Jokinen, E. Dadu, P. Nykvist, J. Kapyla, D. J. White, J. Ivaska, P. Vehvilainen, H. Reunanen, H. Larjava, L. Hakkinen, et al. Integrin-mediated Cell Adhesion to Type I Collagen Fibrils J. Biol. Chem., July 23, 2004; 279(30): 31956 - 31963. [Abstract] [Full Text] [PDF]
|
|
|
|
 |
|
 C. Colnot, Z. Thompson, T. Miclau, Z. Werb, and J. A. Helms Altered fracture repair in the absence of MMP9 Development, September 1, 2003; 130(17): 4123 - 4133. [Abstract] [Full Text] [PDF]
|
|
| HOME | HELP | FEEDBACK | SUBSCRIPTIONS | ARCHIVE | SEARCH | TABLE OF CONTENTS |
