Abstract:
:The fibroblast integrin alpha11beta1 is a key receptor for fibrillar collagens. To study the potential function of alpha11 in vivo, we generated a null allele of the alpha11 gene. Integrin alpha11(-/-) mice are viable and fertile but display dwarfism with increased mortality, most probably due to severely defective incisors. Mutant incisors are characterized by disorganized periodontal ligaments, whereas molar ligaments appear normal. The primary defect in the incisor ligament leads to halted tooth eruption. alpha11beta1-defective embryonic fibroblasts displayed severe defects in vitro, characterized by (i) greatly reduced cell adhesion and spreading on collagen I, (ii) reduced ability to retract collagen lattices, and (iii) reduced cell proliferation. Analysis of matrix metalloproteinase in vitro and in vivo revealed disturbed MMP13 and MMP14 synthesis in alpha11(-/-) cells. We show that alpha11beta1 is the major receptor for collagen I on mouse embryonic fibroblasts and suggest that alpha11beta1 integrin is specifically required on periodontal ligament fibroblasts for cell migration and collagen reorganization to help generate the forces needed for axial tooth movement. Our data show a unique role for alpha11beta1 integrin during tooth eruption.
journal_name
Mol Cell Bioljournal_title
Molecular and cellular biologyauthors
Popova SN,Barczyk M,Tiger CF,Beertsen W,Zigrino P,Aszodi A,Miosge N,Forsberg E,Gullberg Ddoi
10.1128/MCB.00041-07subject
Has Abstractpub_date
2007-06-01 00:00:00pages
4306-16issue
12eissn
0270-7306issn
1098-5549pii
MCB.00041-07journal_volume
27pub_type
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