Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 209.6 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Deprecated: Implicit conversion from float 243.2 to int loses precision in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 534
Warning: imagejpeg(C:\Inetpub\vhosts\kidney.de\httpdocs\phplern\27242953
.jpg): Failed to open stream: No such file or directory in C:\Inetpub\vhosts\kidney.de\httpdocs\pget.php on line 117 Front+Oncol
2016 ; 6
(ä): 109
Nephropedia Template TP
gab.com Text
Twit Text FOAVip
Twit Text #
English Wikipedia
Turning-Off Signaling by Siglecs, Selectins, and Galectins: Chemical Inhibition
of Glycan-Dependent Interactions in Cancer
#MMPMID27242953
Cagnoni AJ
; Pérez Sáez JM
; Rabinovich GA
; Mariño KV
Front Oncol
2016[]; 6
(ä): 109
PMID27242953
show ga
Aberrant glycosylation, a common feature associated with malignancy, has been
implicated in important events during cancer progression. Our understanding of
the role of glycans in cancer has grown exponentially in the last few years,
concurrent with important advances in glycomics and glycoproteomic technologies,
paving the way for the validation of a number of glycan structures as potential
glycobiomarkers. However, the molecular bases underlying cancer-associated glycan
modifications are still far from understood. Glycans exhibit a natural
heterogeneity, crucial for their diverse functional roles as specific carriers of
biologically relevant information. This information is decoded by families of
proteins named lectins, including sialic acid-binding immunoglobulin (Ig)-like
lectins (siglecs), C-type lectin receptors (CLRs), and galectins. Siglecs are
primarily expressed on the surface of immune cells and differentially control
innate and adaptive immune responses. Among CLRs, selectins are a family of cell
adhesion molecules that mediate interactions between cancer cells and platelets,
leukocytes, and endothelial cells, thus facilitating tumor cell invasion and
metastasis. Galectins, a family of soluble proteins that bind
?-galactoside-containing glycans, have been implicated in diverse events
associated with cancer biology such as apoptosis, homotypic cell aggregation,
angiogenesis, cell migration, and tumor-immune escape. Consequently, individual
members of these lectin families have become promising targets for the design of
novel anticancer therapies. During the past decade, a number of inhibitors of
lectin-glycan interactions have been developed including small-molecule
inhibitors, multivalent saccharide ligands, and more recently peptides and
peptidomimetics have offered alternatives for tackling tumor progression. In this
article, we review the current status of the discovery and development of
chemical lectin inhibitors and discuss novel strategies to limit cancer
progression by targeting lectin-glycan interactions.
free
free
free
