Biomedical Engineering Reference
In-Depth Information
signii cantly induces the expression of ICAM-1 and VCAM-1 (Cominacini
et al
. 1997b). Other investigators maintain that only LDL oxidized with 1 μM
Cu
2+
, but not LDL oxidized with 5 or 2.5 μM Cu
2+
, will signii cantly induce
the expression of these adhesion molecules (Cominacini
et al
. 1997a). Another
study has demonstrated that highly oxidized Ox-LDL may not have the ability to
stimulate ICAM-1 expression in HUVECs possibly due to LDL aggregation (Takei
et al
. 2001). HUVEC-oxidized LDL and MM-LDL cause a signii cant increase of
ICAM-1 and VCAM-1 in HUVECs
(Cominacini
et al
. 1997a).
Cu-LDL causes the PKC pathway to induce the ICAM-1 expression on
HUVECs (Mason
et al
. 1997),
but Cu-LDL does not induce PKC-mediated
ICAM-1 expression on glomerular endothelial cells
(Kamanna
et al
. 1999).
Lysophosphatidylcholine induces ICAM-1 and VCAM-1 in human iliac artery
endothelial cells, whereas only ICAM-1 is upregulated in HUVECs (Kume
et al
.
1992). h e augmented expression of ICAM-1 by lysophosphatidylcholine is not
mediated by the PKC pathway (Ochi
et al
. 1995). HDMECs stimulated with
X-LDL show an enhanced expression of VCAM-1, but not ICAM-1
(Matsumoto
et al
. 2003).
h e VCAM-1 expression is mediated by a tyrosine kinase-related
pathway, but not a G
i
-protein or PKC pathway
(Matsumoto
et al
. 2003).
Cu-
LDL induces the ICAM-1 and VCAM-1 expression on HDMECs (Matsumoto
et al
. 2003). h e ICAM-1 expression is mediated by a G
i
-protein pathway, but
not a tyrosine kinase-related pathway or a PKC pathway. h e Cu-LDL-induced
VCAM-1 expression might be mediated by not only a G
i
-protein pathway but
also other pathways (except a tyrosine kinase-related pathway or a PKC pathway).
Cu-LDL increases ICAM-1 expression on HDMECs depending on the degree of
LDL oxidation. In contrast, X-LDL does not signii cantly upregulate the ICAM-1
expression even if X-LDL receives more extensive oxidation (longer incubation of
LDL with xanthoma tissues).
MONOCYTE-BINDING TO ENDOTHELIAL CELLS
Ox-LDL increases the expression of P-selectin and ICAM-1 on HCAECs, and
therefore enhances the adhesion of monocytes to the endothelial cells (Chen
et al
. 2003). h e process of Ox-LDL-mediated monocyte adhesion to HCAECs
is associated with phosphorylation at Tyr
204
of ERK via LOX-1 (Li and Mehta
2000). MM-LDL induces monocyte binding to endothelial cells (Berliner
et al
.
1990).
Oxidized 1-palmitoyl-2-arachidonoyl-
sn
-glycero-3-phosphorylcholine
(Ox-PAPC), a component of MM-LDL, induces endothelial/monocyte
interactions (Watson
et al
. 1997). 1-palmitoyl-2-(5-oxovaleroyl)-
sn
-glycero-3-
phosphorylcholine and 1-palmitoyl-2-(5-hydroxy-8-oxooct-6-enoyl)-
sn
-glycero-
3-phosphocholine in Ox-PAPC induce monocyte-binding to HAECs (Leitinger
et al
. 1997).
