الفهرس 
JUVENILE RHEUMATOID ARTHRITISOnly 14 pages are availabe for public view
 |  | from | 106 |  |  |
| | | from | 106 | | |
Abstract
Galectins are a family of carbohydrate-binding proteins with specificity
for N-acetyl-lactosamine-containing glycoproteins. At least 14 mammalian
galectins share structural similarities in their carbohydrate recognition
domains. Galectin-3, also known as Mac-2 and previously as L29, CBP35, or
eBP, is the only known Galectin with one carbohydrate recognition domains
and a unique N-terminus. It is often termed a chimeric Galectin. Galectins
lack classical signal peptides but are present and active both within and
outside of the cell. They are involved in cell adhesion, migration, survival,
and apoptosis and are often up- or down-regulated in cancer. Increased serum
Galectin-3 has been noted in rheumatoid arthritis (also in synovial fluid),
Behçet’s disease, and a variety of cancers, especially when they are
metastatic.