Figure 1
From: Heparanase upregulation by colonic epithelium in inflammatory bowel disease
Heparanase primary structure, critical amino acids and antibody specificity. (a) Primary structure. Pre-proheparanase harbors a signal peptide (SP, Met1-Ala35) which is removed upon entering the ER. The protein is then subjected to glycosylation at six N-glycosylation sites () and secreted as a latent ∼65 kDa protein (upper panel). Proteolytic processing removes the linker domain (Ser110–Gln157), resulting in 8 kDa (Gln36–Glu109) and 50 kDa (Lys158–Ile543) subunits (middle panel) that heterodimerize to yield an active enzyme. (b) Antibody specificity. Total cell lysate of heparanase-transfected 293 cells was subjected to immunoblotting applying antibody 1453 (left panel), antibody 733 (right panel) and antibody 810 (middle panel). Note that antibodies 733 and 810 preferentially recognize the 50 and 8 kDa heparanase subunits, respectively, vs the latent 65 kDa protein.
