Glypican-1 (GPC1), a member of the glycosylphosphatidilinositol anchored cell surface heparan sulfate proteoglycans, is involved with cell adhesion and migration, lipoprotein metabolism, modulation of growth factor activites and anticoagulation. Glypican-1 binds to and modulates the activity of several fibroblast growth factors (FGFs) including FGF-1, FGF-2 and FGF-7. Glypican-1 acts as an extracellular chaperone for VEGF165 to help restore receptor binding ability after oxidation. The heparan sulfate chains of glypican-1 mediate specific binding of glypican-1 to VEGF165. When present on the surface of marrow stromal cells, glypican-1 may aid in the maintenance and development of hematopoietic stem and progenitor cells. Human pancreatic cancer cells express a large amount of glypican-1 when compared to glypican-1 levels in normal pancreatic cells. Glypican-1 may play an important role in the response of pancreatic cancer cells to mitogenic stimuli, such as FGF-2. The gene encoding human glypican-1 maps to chromosome 2q37.3.
Background References
1. Cave C et al. GDE2 is essential for neuronal survival in the postnatal mammalian spinal cord. Mol Neurodegener 12:8 (2017).
2. Sharma P et al. Evolutionarily conserved intercalated disc protein Tmem65 regulates cardiac conduction and connexin 43 function. Nat Commun 6:8391 (2015).
Sequence Similarity
Belongs to the glypican family.
Post-translational Modification
S-nitrosylated in a Cu(2+)-dependent manner. Nitric acid (NO) is released from the nitrosylated cysteines by ascorbate or by some other reducing agent, in a Cu(2+) or Zn(2+) dependent manner. This free nitric oxide is then capable of cleaving the heparan sulfate side chains.; N- and O-glycosylated. N-glycosylation is mainly of the complex type containing sialic acid. O-glycosylated with heparan sulfate. The heparan sulfate chains can be cleaved either by the action of heparanase or, degraded by a deaminative process that uses nitric oxide (NO) released from the S-nitrosylated cysteines. This process is triggered by ascorbate, or by some other reducing agent, in a Cu(2+)- or Zn(2+) dependent manner. Cu(2+) ions are provided by ceruloproteins such as APP, PRNP or CP which associate with GCP1 in intracellular compartments or lipid rafts.; This cell-associated glypican is further processed to give rise to a medium-released species.
Western blot analysis of GPC1 on MCF7cell lysate with Rabbit anti-GPC1 antibody (R1512-15) at 1/1,000 dilution.
Exposure time: 20 seconds; ECL: K1801
Blocking: 5% NFDM/TBST, 1 hour at room temperature Primary antibody: R1512-15, 1/1,000 in primary antibody dilution buffer (K1803), overnight at 4 ℃ Secondary antibody: Goat anti-Rabbit IgG-HRP (HA1001), 1/50,000 in 5% NFDM/TBST, 1 hour at room temperature
Predicted band size: 61.7 kDa Observed band size: 61.7 kDa
ICC staining Glypican-1 in Hela cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
ICC staining Glypican-1 in MCF-7 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
ICC staining Glypican-1 in PANC-1 cells (green). The nuclear counter stain is DAPI (blue). Cells were fixed in paraformaldehyde, permeabilised with 0.25% Triton X100/PBS.
Immunohistochemical analysis of paraffin-embedded human breast tissue using anti- Glypican-1 antibody. Counter stained with hematoxylin.
Immunohistochemical analysis of paraffin-embedded human breast cancer tissue using anti- Glypican-1 antibody. Counter stained with hematoxylin.
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