Search PubMed⌕ Search

PubMed · 11099555

Matrix turnover.

Abstract

This review concentrates on how the major component of extracellular matrix, collagen, is catabolized. This process is important in a number of aspects of orthodontics since matrix is constantly turning over, the rate of which differs in embryogenesis, ageing, disease, and physiological processes, such as orthodontic tooth movement. It is not the purpose of this review to consider each process in detail. The aim is to give a clear account of the matrix metalloproteinases (a major family of proteinases) including their classification, properties, and functions.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J J Kerrigan, J P Mansell, J R Sandy. 2000. Matrix turnover.. https://doi.org/10.1179/ortho.27.3.227

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

Surface organization and nanopatterning of collagen by dip-pen nanolithography.

Collagen is a key fibrous protein in biological systems, characterized by a complex structural hierarchy as well as the ability to self-assemble into liquid crystalline mesophases. The structural features of collagen influence cellular responses and material properties, with importance for a wide range of biomaterials and tissue architectures. The mechanism by which fibrillar collagen structures form from liquid crystalline mesophases is not well characterized. We report positive printing of collagen and a collagen-like peptide down to 30-50-nm line widths, using the atomic force microscopy technique of dip-pen nanolithography. The method preserved the triple-helical structure and biological activity of collagen and even fostered the formation of characteristic higher levels of structural organization. The "direct-write" capability of biologically relevant molecules, while preserving their structure and functionality, provides tremendous flexibility in future biological device applications and in proteomics arrays, as well as a new strategy to study the important hierarchical assembly processes of biological systems.

Collagen↗

Diffusion characteristics of collagen film.

Collagen films prepared by treating collagen gel solutions with different concentrations of glutaraldehyde were evaluated as a biodegradable and biocompatible drug carrier for cosmetically effective agents in this study. The influences of concentration of glutaraldehyde (0, 0.05, 0.075, 0.1, 0.2, 0.25, and 0.3%, v/w) with a fixed concentration (1%, w/w) of collagen on the crosslinking rate of collagen gel solutions and on the crosslinking extent of the collagen contained within were examined by monitoring changes in viscosity. In addition, the influences of the addition of different model drugs (retinoic acid, retinol palmitate, ascorbic acid 6-palmitate, and tocopherol acetate) on viscosity changes of collagen gel solutions were compared. The results demonstrate that the maximal viscosity of collagen gel solutions increases with increasing concentrations of glutaraldehyde. When the concentration of glutaraldehyde exceeds 0.2%, the maximal viscosity of collagen gel solutions reaches a plateau. However, model drugs showed insignificant effects on viscosity changes of collagen gel solutions. The diffusion characteristics of collagen films prepared from those gel solutions crosslinked with different concentrations of glutaraldehyde were assessed using two different matrix forms of solution or gel for the model drugs in a flow-through diffusion system. The matrix effect on the flux of model drugs from both solution and gel matrix through collagen films was inconclusive. However, both fluxes show the same tendency to decrease when the concentration of glutaraldehyde used for crosslinking is increased. However, when the concentration of glutaraldehyde exceeds 0.2%, these model drugs, except retinoic acid, show similar diffusion characteristics across the collagen films.

Collagen↗