Glypican-4 is a protein that in humans is encoded by the GPC4gene.[1][2]
Cell surface heparan sulfate proteoglycans are composed of a membrane-associated protein core substituted with a variable number of heparan sulfate chains. Members of the glypican-related integral membrane proteoglycan family (GRIPS) contain a core protein anchored to the cytoplasmic membrane via a glycosyl phosphatidylinositol linkage. These proteins may play a role in the control of cell division and growth regulation. The GPC4 gene is adjacent to the 3' end of GPC3 and may also play a role in Simpson-Golabi-Behmel syndrome.[2]
↑Veugelers M, Vermeesch J, Watanabe K, Yamaguchi Y, Marynen P, David G (Dec 1998). "GPC4, the gene for human K-glypican, flanks GPC3 on xq26: deletion of the GPC3-GPC4 gene cluster in one family with Simpson-Golabi-Behmel syndrome". Genomics. 53 (1): 1–11. doi:10.1006/geno.1998.5465. PMID9787072.
Sheu TJ, Schwarz EM, O'Keefe RJ, et al. (2002). "Use of a phage display technique to identify potential osteoblast binding sites within osteoclast lacunae". J. Bone Miner. Res. 17 (5): 915–22. doi:10.1359/jbmr.2002.17.5.915. PMID12009023.
Karumanchi SA, Jha V, Ramchandran R, et al. (2001). "Cell surface glypicans are low-affinity endostatin receptors". Mol. Cell. 7 (4): 811–22. doi:10.1016/S1097-2765(01)00225-8. PMID11336704.
Veugelers M, Cat BD, Muyldermans SY, et al. (2000). "Mutational analysis of the GPC3/GPC4 glypican gene cluster on Xq26 in patients with Simpson-Golabi-Behmel syndrome: identification of loss-of-function mutations in the GPC3 gene". Hum. Mol. Genet. 9 (9): 1321–8. doi:10.1093/hmg/9.9.1321. PMID10814714.