Biomedical Engineering Reference
In-Depth Information
(a)
(b)
A C
D A
Biglycan
(i)
∆
DiHA
(ii)
Decorin
∆
Di4S
(iii)
Versican
10.4
AlloDerm retains proteoglycan content and glycosylation pattern.
(a) Proteoglycans were extracted from AlloDerm RTM (A) and control
dermis (D) using 4 M guanidine hydrochloride. Glycosaminoglycan
chains were then removed by digestion with chondroitinase ABC. The
resulting core proteins were fractionated on a 10% polyacrylamide gel,
transferred to nitrocellulose and identified by western blot for decorin,
biglycan or versican. (b) AlloDerm RTM was digested with proteinase K
and the resulting glycosaminoglycans precipitated with ethanol.
Disaccharides were obtained following digestion of the glycosamino-
glycans with chondroitinase ABC and hyaluronidase, labeled with
2-aminoacridone and analyzed by fluorophore-assisted carbohydrate
eletrophoresis (FACE). Control AlloDerm samples (C) were not treated
with chondroitinase ABC or hyaluronidase and show the migration of
an irrelevant band not representative of dermal-derived disaccharides.
(Danielson
et al
., 1997; Young
et al
., 2002). In addition to their structural role,
these molecules have recently been shown to regulate cellular activities through
direct interactions with growth factors such as TGF-
and PDGF, as well
as the cell surface receptors EGFR (epidermal growth factor receptor) and ILGFR
(insulin-like growth factor receptor) (Csordás
et al
., 2000; Nili
et al
., 2003;
Schönherr
et al
., 2005; Tufvesson and Westergren-Thorsson, 2002; Yamaguchi,
et
al.
, 1990). In particular, the presence of decorin in ECM scaffolds has been shown
to reduce contracture in cutaneous wound healing (Shafritz
et al.
, 1994) presum-
ably by binding and neutralizing TGF-
β
, TNF-
α
. Theses findings correlate with analysis of
hypertrophic scars showing 75% reductions in decorin content and irregular
collagen organization (Sayani
et al
., 2000; Scott
et al
., 1996).
The glycosaminoglycan component of AlloDerm RTM exhibits normal
β
