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Tissue Inhibitors of Metalloproteinases (TIMPs): Their Biological Functions and Involvement in Oral Disease

Department of Orthodontics and Oral Biology, Radboud University Nijmegen Medical Centre, P.O. Box 9101, 6500 HB Nijmegen, The Netherlands

View larger version (44K): [in this window] [in a new window]   Figure 1. The primary protein structure of TIMPs. In each TIMP, 6 pairs of cysteines are linked to each other to form 6 disulfide bridges. The arrows indicate the junctions between the N- and the C-terminal domains of the proteins. The conserved VIRAK sequence is indicated in yellow. Reprinted from Critical Reviews in Oncology/Hematology, 49, Lambert E, Dassé E, Haye B, Petitfrère E, TIMPs as multifacial proteins, 187–198, Copyright (2004), with permission from Elsevier.

View larger version (21K): [in this window] [in a new window]   Figure 2. Schematic representation of pro-MMP-2 activation by MT1-MMP and TIMP-1. MT1-MMP is bound at the cell surface (A). TIMP-1 binds to MT1-MMP (B). Pro-MMP-2 binds to this complex, and becomes activated. Uncomplexed MT1-MMPs may be recruited and aid in the activation of pro-MMP-2 (C). Subsequently, the complex dissociates (D). The binding sites for the formation of this complex are found in the N-terminal and C-terminal domains of TIMP-2, the hemopexin-like domain of pro-MMP-2, and the active site of MT1-MMP, as described in the text.

View larger version (14K): [in this window] [in a new window]   Figure 3. Palatal fusion during embryonic development. Initially, the palatal shelves (ps) are positioned next to the developing tongue (A). Subsequently, the tongue descends, and the palatal shelves rotate toward each other (B). Finally, the palatal shelves fuse, and the midline seam (ms) is degraded by MMPs (C). The nasal septum (ns) simultanously merges with the secondary palate.

Journal of Dental Research, Vol. 85, No. 12, 1074-1084 (2006)
DOI: 10.1177/154405910608501202


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