Biomedical Engineering Reference
In-Depth Information
2.11
Summary
Tissue-implant interactions are well documented in the last decade, especially those
regarding mobile cells in the blood, vascular endothelial cells, and cells of various
connective tissues. All types of implantation, especially for non-resorptive materials
(metallic, hard insoluble polymers) involve tissue trauma, which induces an
inflammatory response, followed by wound healing reaction (angiogenesis,
fibroblast activation) and ECM remodeling. All high performance implanted mate-
rials should limit the extension of inflammatory reactions and also should promote
tissue remodeling toward a functional status. Matrix tailoring supposes not only
pure ECM dissection and cleavage for its main molecules but also subtle changes in
ECM composition, which may alter the activity of the growth factors or of cells'
surface receptors. In order for the essential biological processes to develop, ECM
must be degraded in a controlled manner in order to allow cell displacement during
embryonic development, tissue remodeling, and tissue repair. These processes are
directly mediated by Matrix Metalloproteinases (MMPs), that we may consider to
act as true molecular scissors for ECM. Modulation of MMP activity appears to
become essential in remodeling control, even in implant adaptation to host.
Modulation of MMP activity depends directly on the specific inhibition or modula-
tion of the catalytic domain. This inhibition depends on the intimate structure of the
catalytic domain of the MMPs (which is common to almost all metalloproteinases).
Our group has performed various tests in order to detect the presence of some MMPs
(as gelatinases) in periimplant tissues, including molecular modeling studies
together with immunohistochemical investigations.
References
1. Abreu T, Silva G (2009) Cell movement: new research trends. Nova Biomedical topics, New
York
2. Agren MS, Jorgensen LN, Andersen M, Viljanto J, Gottrup F (1998) Matrix metalloproteinase
9 level predicts optimal collagen deposition during early wound repair in humans. Br J Surg
85(1):68-71
3. Arumugam S, Jang YC, Chen-Jensen C, Gibran NS, Isik FF (1999) Temporal activity of
plasminogen activators and matrix metalloproteinases during cutaneous wound repair. Surgery
125(6):587-593
4. Aschi M, Bozzi A, Di Bartolomeo R, Petruzzelli R (2010) The role of disulfide bonds and
N-terminus in the structural properties of hepcidins: insights from molecular dynamics simula-
tions. Biopolymers 93(10):917-926
5. Atassi F (2002) Periimplant probing: positives and negatives. Implant Dent 11(4):356-362
6. Baier RE, Meenaghan MA, Hartman LC, Wirth JE, Flynn HE, Meyer AE et al (1988) Implant
surface characteristics and tissue interaction. J Oral Implantol 13(4):594-606
7. Banyai L, Tordai H, Patthy L (1994) The gelatin-binding site of human 72 kDa type IV colla-
genase (gelatinase A). Biochem J 298(Pt 2):403-407
8. Baramova E, Foidart JM (1995) Matrix metalloproteinase family. Cell Biol Int 19(3):239-242
Search WWH ::




Custom Search