Biomedical Engineering Reference
In-Depth Information
also recognised by galectin-1, showing the function of galectin-1 in immune response and
inflammation (Liu, 2005; Nishi et al., 2008; Pace et al., 1999; Rabinovich et al., 2002a;
Rabinovich et al., 2002b).
Binding partner
Gal
Cell type
Process
Reference
Skeletal muscle
cells;
Myoblasts
Influences integrin-
laminin interaction
(Gu et al.,
1994)
Integrin α7β1
1
Vascular smooth
muscle cells
Influences adhesion
and migration
(Moiseeva et
al., 1999)
Integrin α1β1
1
Influences cell
adhesion and
survival by
modulating integrin-
ECM interaction
e.g. endothelial
cells
(Hadari et al.,
2000)
Integrin α3β1
8
Cell recognition
molecule L1;
Myelin associated
glycoprotein
(MAG)
Neural cell
adhesion molecule
(NCAM)
Likely influences cell
adhesion and
signalling processes
(Probstmeier
et al., 1995)
3
Neural tissue
Influences
endothelial cell
motility and
morphogenesis
Microvascular
pericytes
(Wen et al.,
2006)
NG2 proteoglycan
3
Table 2. Examples of cell-surface-glycoproteins interacting with galectins
This does not constitute a comprehensive list of cell-bound galectin-binding-glycoproteins,
but just intends to show some examples which might be interesting for tissue engineering.
Immune and tumor cells are not included in the list.
Similarly galectin-3 binds to CD98 on macrophages, CD66 on neutrophils and the T-cell
receptor also showing functions in immune response and inflammation (Demetriou et al.,
2001; Dong & Hughes, 1997; Dumic et al., 2006; Hughes, 2001). Other cell surface markers
involved in cell-adhesion processes such as CD44 are bound by galectin-8 in a glycan-
dependent manner underlining the importance of galectin-8 as matricellular protein
involved in the regulation of cell-adhesion (Sebban et al., 2007).
All three galectins mentioned in this review are able to bind different integrin subunits. All
bind to β1-integrins (Dumic et al., 2006; Furtak et al., 2001; Hughes, 2001; Sakaguchi et al.,
2010; Zick et al., 2004). In this context galectin-3 binding to β1-integrins leads to an
internalisation signal, regulating receptor amount on the cell surface and thereby
influencing cell signalling aspects (Furtak et al., 2001). Other integrins such as αvβ3 integrin
on endothelial cells or the αM subunit on macrophages are also bound by galectin-3 (Dong
& Hughes, 1997; Markowska et al., 2010). Galectin-8 is known to have a major function in
integrin-binding and integrin-mediated signalling (Zick et al., 2004). The binding of
galectin-8 N-CRD to the β1-integrin-sunbunit is especially good as high affinity α2-3-
