Crosslinked type II collagen matrices: preparation, characterization, and potential for cartilage engineering.

Abstract:

:The limited intrinsic repair capacity of articular cartilage has stimulated continuing efforts to develop tissue engineered analogues. Matrices composed of type II collagen and chondroitin sulfate (CS), the major constituents of hyaline cartilage, may create an appropriate environment for the generation of cartilage-like tissue. In this study, we prepared, characterized, and evaluated type 11 collagen matrices with and without CS. Type II collagen matrices were prepared using purified, pepsin-treated, type II collagen. Techniques applied to prepare type I collagen matrices were found unsuitable for type II collagen. Crosslinking of collagen and covalent attachment of CS was performed using 1-ethyl-3-(3-dimethyl aminopropyl)carbodiimide. Porous matrices were prepared by freezing and lyophilization, and their physico-chemical characteristics (degree of crosslinking, denaturing temperature, collagenase-resistance, amount of CS incorporated) established. Matrices were evaluated for their capacity to sustain chondrocyte proliferation and differentiation in vitro. After 7 d of culture, chondrocytes were mainly located at the periphery of the matrices. In contrast to type I collagen, type II collagen supported the distribution of cells throughout the matrix. After 14 d of culture, matrices were surfaced with a cartilagenous-like layer, and occasionally clusters of chondrocytes were present inside the matrix. Chondrocytes proliferated and differentiated as indicated by biochemical analyses, ultrastructural observations, and reverse transcriptase PCR for collagen types I, II and X. No major differences were observed with respect to the presence or absence of CS in the matrices.

journal_name

Biomaterials

journal_title

Biomaterials

authors

Pieper JS,van der Kraan PM,Hafmans T,Kamp J,Buma P,van Susante JL,van den Berg WB,Veerkamp JH,van Kuppevelt TH

doi

10.1016/s0142-9612(02)00067-4

keywords:

subject

Has Abstract

pub_date

2002-08-01 00:00:00

pages

3183-92

issue

15

eissn

0142-9612

issn

1878-5905

pii

S0142-9612(02)00067-4

journal_volume

23

pub_type

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