Biomedical Engineering Reference
In-Depth Information
Abbreviations
2-D two-dimensional
3-D three-dimensional
BMP bone morphogenetic protein
ECM extracellular matrix
FGF basic fibroblast growth factor
FN fibronectin
MW molecular weight
MMP matrix metalloproteinase
PEG poly(ethylene glycol)
PEMA poly(ethylene-
alt
-maleic anhydride)
POMA poly(octadecene-
alt
-maleic anhydride)
PPMA
poly(propene-
alt
-maleic anhydride)
RGD
arginine-glycine-aspartic acid
SDF-1
stromal cell-derived factor-1
VEGF
vascular endothelial growth factor
1
Introduction
The extracellular matrix (ECM) is a highly orchestrated ensemble of proteins,
proteoglycans, and glycosaminoglycans arranged in tissue specific three-
dimensional structures [1-4]. ECM plays a key role in tissue architecture
and homeostasis by providing structural support and tensile strength, at-
tachment sites for cell surface receptors, and feedback-controlled reservoirs
for signalling factors related to a wide variety of processes related to cell
differentiation, tissue formation, homeostasis, and regeneration. Thus, the
“nonliving” material of the ECM biopolymers has to be considered to cre-
ate the base for multicellular tissues and their dedicated functions in living
organisms.
The principal proteinaceous components of the ECM are collagens which
are secreted by a variety of stromal cells. Other proteins involved in different
specialized matrix assemblies, such as the basement membrane [5], include
fibronectin, laminin, collagen IV, and various growth factors and proteases.
A second class of molecules that play an essential role in the ECM are pro-
teoglycans whose protein core is covalently bound to high-molecular-weight
glycosaminoglycans, including chondroitin and heparan sulfate. Proteogly-
cans support cell adhesion and bind various growth factors [6]. The ECM also
contains hyaluronan, a glycosaminoglycan not linked to a core protein, which
regulates adhesion, trafficking, and signalling of cells.
Asurveyofsomeofthemost-abundantECMbiopolymersandtheir
known functions is given in Table 1; for more details the reader is referred
to [2].
