Biomedical Engineering Reference
In-Depth Information
(a)
M I
III
IV
V D
A
[
α
1(IV)]
2
[
α
2(IV)]
[
1(III)]
3
α
kDa
173
α
1(I)
α
2(I)
114
79.6
61.3
49.0
(b)
A D M
CNBr peptides
α
2(I) CB 3.5
α
1(I) CB 7.6
α
1(I) CB 8.3
α
1(I) CB 3.7
α
2(I) CB 4
α
1(I) CB 7
α
1(I) CB 8
α
1(III) CB 5
α
1(I) CB 6
α
1(I) CB 3
α
1(III) CB 8
10.3
Collagen type distribution in AlloDerm RTM. (a) AlloDerm RTM
was digested with pepsin and the solublized collagen analyzed follow-
ing electrophoresis on an 8% polyacrylamide gel. (b) Pepsin insoluble
collagen was cleaved using cyanogen bromide and the resulting
collagen peptides analyzed following electrophoresis on 4-20%
polyacrylamide gradient gel. Dermal samples that were not subjected
to the decellularization process were analyzed in parallel and shown
for comparative purposes. Lane headings: M = Marker; A = AlloDerm;
D = Dermis; I, III, IV, V = purified collagen of the indicated type.
biglycan and versican (
Fig. 10.4(a
)). In particular, decorin and biglycan have been
described as possessing a broad range of functional activities responsible for cell
growth regulation, growth factor binding and immunoregulation. Additionally,
they both bind collagen and regulate the formation of collagen fibrils. Mutant mice
lacking these proteoglycans produce phenotypes with connective tissue disorders
