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Glypican Edit Wikipedia article
C-terminally truncated human glypican-1. PDB
Glypicans constitute one of the two major families of heparin sulfate proteoglycans, with the other major family being syndecans. Six glypicans have been identified in mammals, and are referred to as GPC1 through GPC6. In Drosophila two glypicans have been identified, and these are referred to as dally (division abnormally delayed) and dally-like. One additional glypican has been identified in C. elegans. Glypicans seem to play a vital role in developmental morphogenesis, and have been suggested as regulators for the Wnt and Hedgehog cell signaling pathways. They have additionally been suggested as regulators for fibroblast growth factor and bone morphogenic protein signaling.
While six glypicans have been identified in mammals, several characteristics remain consistent between these different proteins. First, the core protein of all glypicans is similar in size, approximately ranging between 60 and 70 kDa. Additionally, in terms of amino acid sequence, the location of fourteen cysteine residues is conserved; however, researchers describe glypicans as having moderate similarity in amino acid sequence overall. Nevertheless, it is thought that the fourteen conserved cysteine residues play a vital role in determining three-dimensional shape, thus suggesting the existence of a highly similar three-dimensional structure. Overall, GPC3 and GPC5 have very similar primary structures with 43% sequence similarity. On the other hand, GPC1, GPC2, GPC4, and GPC6 have between 35% and 63% sequence similarity. Thus, GPC3 and GPC5 are often referred to as one subfamily of glypicans, with GPC1, GPC2, GPC4, and GPC6 constituting the other group. Between the subfamilies of glypicans, there is about 25% sequence similarity. Furthermore, the amino acid sequence and structure of each glypican is well-conserved between species; all vertebrate glypicans are more than 90% similar regardless of the species.
For all members of the glypican family, the C-terminus of the protein is attached to the cell membrane covalently via a glycosylphosphatidylinositol (GPI) anchor. To allow for the addition of the GPI anchor, glypicans have a hydrophobic domain at the C-terminus of the protein. Within 50 amino acids of this GPI anchor, the heparan sulfate chains attach to the protein core. Therefore, unlike syndecans the heparan sulfate glycosaminoglycan chains attached to glypicans are located rather close to the cell-membrane. The glypicans found in vertebrates, Drosophila, and C. elegans all have an N-terminal signal sequence.
Glypicans are critically involved in developmental morphogenesis, and have been implicated as regulators in several cell signaling pathways. These include the Wnt and Hedgehog signaling pathways, as well as signaling of fibroblast growth factors and bone morphogenic proteins. The regulating processes performed by glypicans can either stimulate or inhibit specific cellular processes. The mechanisms by which glypicans regulate cellular pathways are not entirely elucidated. One commonly proposed mechanism suggests that glypicans behave as co-receptors which bind both the ligand and the receptor. Glypicans are expressed in various different amounts depending on the tissue, and they also are expressed to different degrees during the different stages of development. Drosophila Dally mutants have irregular wing, antenna, genitalia, and brain development.
GPC5 and GPC6 are next to one another on chromosome 13q32 (in humans). GPC3 and GPC4 are also found next to one another, and are located on the human chromosome Xq26. Some suggest that this implies that these glypicans arose because of a gene duplication event. The gene for GPC1 is found on chromosome 2q36. Nearby genes include ZIC2, ZIC3, COL4A1/2, and COL4A3/4.
Since 1996, it has been known that patients with Simpson-Golabi-Behmel Syndrome (SGBS) have mutations in GPC3. Because this is an X-linked syndrome, it appears to affect males more significantly than females. While the phenotype associated with this condition can vary from mild to lethal, common symptoms include macroglossia, cleft palate, syndactyly, polydactyly, cystic and dysplastic kidneys, congenital heart defects, and a distinct facial appearance. Additional symptoms/characteristics have also been noted. Overall, these symptoms/characteristics are distinguished by prenatal and post-natal overgrowth. Typically, patients identified with SGBS have point mutations or microdeletions in the gene encoding GPC3, and the mutations can occur in multiple different locations of the gene. No correlation has been noticed between the location of the GPC3 mutation and the phenotypic manifestation of this disease. therefore, it is inferred that SGBS results due to a nonfunctional GPC3 protein. Researchers currently speculate that GPC3 is a negative regulator of cell proliferation, and this would explain why patients with SGBS experience overgrowth.
Implications in Cancer
Abnormal expression of glypicans has been noted in multiple types of cancer, including human hepatocellular carcinoma, ovarian cancer, mesothelioma, pancreatic cancer, glioma, breast cancer and recently GCP2 in neuroblastoma. Most research involving the relationship between glypicans and cancer has focused on GPC1 and GPC3
A correlation between GPC3 expression levels and various types of cancer. To summarize these findings, it can be generally said that tissues which normally express GPC3 exhibit down-regulation of GPC3 expression during tumor progression. Similarly, the corresponding cancers of tissues which normally do not exhibit GPC3 expression often express GPC3. Furthermore, oftentimes GPC3 expression occurs during embryonic development in these tissues, and is subsequently re-expressed during tumor progression. GPC3 expression can be detected in normal ovarian cells; however, several ovarian cancer cell lines do not express GPC3. On the other hand, GPC3 expression is undetectable in healthy adult liver cells, while GPC3 expression occurs in the majority of human hepatocellular carcinomas. A similar correlation has been found in colorectal tumors. GPC3 is an oncofetal protein in both liver and intestine, as GPC3 is typically only expressed during embryonic development but also found in cancerous tumors.
GPC3 mutations do not occur in the coding sequence of this protein. Ovarian cancer cell lines do not express GPC3 due to hypermethylation of the GPC3 promoter. After removing these methyl groups, the authors restored expression of GPC3. Mesothelioma cell lines contain a GPC3 promoter which is incorrectly methylated. Re-establishing expression of GPC3 prevented colony-forming by cancerous cells.
GPC1 Implications in Cancer
In addition to GPC3, GPC1 has also been implicated in tumor progression, especially in pancreatic cancer, glioma, and breast cancer. GPC1 expression is severely high in pancreatic ductal adenocarcinoma cells, and results indicate that GPC1 expression is linked to cancer progression, including tumor growth, angiogenesis and metastasis. In addition to overexpression of GPC1 on the plasma membrane of pancreatic ductal adenocarcinoma cells. GPC1 is released into the tumor microenvironment by these cells. Because glypicans play a role in growth factor binding, researchers have speculated that increased levels of GPC1 in the tumor microenvironment may function to store growth factors for cancerous cells. By reducing the level of GCP1 in pancreatic adenocarcinoma cells, the growth of these cells was hindered. By reducing the levels of expressed GCP1 immunocompromised mice, slowed the growth tumors and reduced angiogenesis and metastases when compared with control GCP1 mice. GPC1 is highly expressed in human glioma blood vessel endothelial cells. Furthermore, increasing the level of GPC1 in mouse brain endothelial cells results in cell growth and stimulates mitosis in response to the angiogenic factor, FGF2. This suggests that GPC1 acts as a regulator for cell cycle progression. GPC1 expression is well-above normal in human breast cancers, while expression of GPC1 is low in healthy breast tissue. Furthermore, expression was not significantly increased for any other glypican. GPC1 plays a role in heparin-binding and cell cycle progression in the breast tissue.
GPC2 Implications in Cancer
Glypican-2 (GPC2) is a cell surface heparan sulfate proteoglycan that is important for neuronal cell adhesion and neurite outgrowth. GPC2 protein is highly expressed in about half of neuroblastoma cases and that high GPC2 expression correlates with poor overall survival compared with patients with low GPC2 expression, suggesting GPC2 as a therapeutic target in neuroblastoma. Silencing of GPC2 by CRISPR/Cas9 results in the inhibition of neuroblastoma tumor cell growth. GPC2 silencing inactivates Wnt/β-catenin signaling and reduces the expression of the target gene N-Myc, an oncogenic driver of neuroblastoma tumorigenesis. Immunotoxins and chimeric antigen receptor (CAR) T cells targeting GPC2 have been made. Immunotoxin treatment inhibits neuroblastoma growth in mice. CAR T cells targeting GPC2 can eliminate tumors in a neuroblastoma mouse model.
Glypicans can modify cell signaling pathways and contribute to cellular proliferation and tissue growth. In Drosophila, the glypican dally assists diffusion of the BMP-family growth-promoting morphogen Decapentaplegic in the developing wing, while the developing haltere lacks dally and remains small. Extracellular localization of the other glypican in Drosophila, dally-like, is also required for the proper level of Hedgehog signaling in the developing wing.
- De Cat B, David G (April 2001). "Developmental roles of the glypicans". Seminars in Cell & Developmental Biology. 12 (2): 117–25. doi:10.1006/scdb.2000.0240. PMID 11292377.
- Filmus J, Capurro M, Rast J (2008). "Glypicans". Genome Biology. 9 (5): 224. doi:10.1186/gb-2008-9-5-224. PMC . PMID 18505598.
- Filmus J, Selleck SB (2001). "Glypicans: proteoglycans with a surprise". The Journal of Clinical Investigation. 108 (4): 497–501. doi:10.1172/JCI13712. PMC . PMID 11518720.
- Filmus J (March 2001). "Glypicans in growth control and cancer". Glycobiology. 11 (3): 19R–23R. doi:10.1093/glycob/11.3.19r. PMID 11320054.
- Li N, Fu H, Hewitt SM, Dimitrov DS, Ho M (August 2017). "Therapeutically targeting glypican-2 via single-domain antibody-based chimeric antigen receptors and immunotoxins in neuroblastoma". Proceedings of the National Academy of Sciences of the United States of America. 114 (32): E6623–E6631. doi:10.1073/pnas.1706055114. PMC . PMID 28739923.
- Lin H, Huber R, Schlessinger D, Morin PJ (February 1999). "Frequent silencing of the GPC3 gene in ovarian cancer cell lines". Cancer Research. 59 (4): 807–10. PMID 10029067.
- Murthy SS, Shen T, De Rienzo A, Lee WC, Ferriola PC, Jhanwar SC, Mossman BT, Filmus J, Testa JR (January 2000). "Expression of GPC3, an X-linked recessive overgrowth gene, is silenced in malignant mesothelioma". Oncogene. 19 (3): 410–6. doi:10.1038/sj.onc.1203322. PMID 10656689.
- Ho M, Kim H (February 2011). "Glypican-3: a new target for cancer immunotherapy". European Journal of Cancer. 47 (3): 333–8. doi:10.1016/j.ejca.2010.10.024. PMC . PMID 21112773.
- Qiao D, Yang X, Meyer K, Friedl A (July 2008). "Glypican-1 regulates anaphase promoting complex/cyclosome substrates and cell cycle progression in endothelial cells". Molecular Biology of the Cell. 19 (7): 2789–801. doi:10.1091/mbc.E07-10-1025. PMC . PMID 18417614.
- Matsuda K, Maruyama H, Guo F, Kleeff J, Itakura J, Matsumoto Y, Lander AD, Korc M (July 2001). "Glypican-1 is overexpressed in human breast cancer and modulates the mitogenic effects of multiple heparin-binding growth factors in breast cancer cells". Cancer Research. 61 (14): 5562–9. PMID 11454708.
- Crickmore MA, Mann RS (January 2007). "Hox control of morphogen mobility and organ development through regulation of glypican expression". Development. 134 (2): 327–34. doi:10.1242/dev.02737. PMID 17166918.
- Gallet A, Staccini-Lavenant L, Thérond PP (May 2008). "Cellular trafficking of the glypican Dally-like is required for full-strength Hedgehog signaling and wingless transcytosis". Developmental Cell. 14 (5): 712–25. doi:10.1016/j.devcel.2008.03.001. PMID 18477454.
- Su G, Meyer K, Nandini CD, Qiao D, Salamat S, Friedl A (June 2006). "Glypican-1 is frequently overexpressed in human gliomas and enhances FGF-2 signaling in glioma cells". The American Journal of Pathology. 168 (6): 2014–26. doi:10.2353/ajpath.2006.050800. PMC . PMID 16723715.
- Pang RW, Joh JW, Johnson PJ, Monden M, Pawlik TM, Poon RT (April 2008). "Biology of hepatocellular carcinoma". Annals of Surgical Oncology. 15 (4): 962–71. doi:10.1245/s10434-007-9730-z. PMID 18236113.
- Cui S, Leyva-Vega M, Tsai EA, EauClaire SF, Glessner JT, Hakonarson H, Devoto M, Haber BA, Spinner NB, Matthews RP (May 2013). "Evidence from human and zebrafish that GPC1 is a biliary atresia susceptibility gene". Gastroenterology. 144 (5): 1107–1115.e3. doi:10.1053/j.gastro.2013.01.022. PMC . PMID 23336978.
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External database links
This tab holds annotation information from the InterPro database.
InterPro entry IPR001863
Glypicans [PUBMED:8589707, PUBMED:7657705] are a family of heparan sulphate proteoglycans which are anchored to cell membranes by a glycosylphosphatidylinositol (GPI) linkage. Six members (GPC1-6) are known in vertebrates [PUBMED:11474185]. The main function of glypicans is to regulate several signaling pathways, including those of Wnts, Hedgehogs, fibroblast growth factors and bone morphogenetic proteins (BMPs) [PUBMED:18505598, PUBMED:24412155].
Structurally, these proteins consist of three separate domains:
- A signal sequence;
- An extracellular domain of about 500 residues that contains 12 conserved cysteines probably involved in disulphide bonds and which also contains the sites of attachment of the heparan sulphate glycosaminoglycan side chains;
- A C-terminal hydrophobic region which is post-translationally removed after formation of the GPI-anchor.
The mapping between Pfam and Gene Ontology is provided by InterPro. If you use this data please cite InterPro.
|Cellular component||anchored component of plasma membrane (GO:0046658)|
|Biological process||regulation of signal transduction (GO:0009966)|
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1Cannot generate PP/Heatmap alignments for seeds; no PP data available
Key: available, not generated, — not available.
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|Author:||Finn RD , Bateman A|
|Number in seed:||16|
|Number in full:||1519|
|Average length of the domain:||355.90 aa|
|Average identity of full alignment:||24 %|
|Average coverage of the sequence by the domain:||86.76 %|
|HMM build commands:||
build method: hmmbuild -o /dev/null HMM SEED
search method: hmmsearch -Z 45638612 -E 1000 --cpu 4 HMM pfamseq
|Family (HMM) version:||19|
|Download:||download the raw HMM for this family|
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Unmapped species names
The tree is built by looking at each sequence in the full alignment for the family. We take the name of the species given by UniProt and try to map that to the full taxonomic tree from NCBI. In some cases, the name chosen by UniProt does not map to any node in the NCBI tree, perhaps because the chosen name is listed as a synonym or a misspelling in the NCBI taxonomy.
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The tree shows the occurrence of this domain across different species. More...
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For all of the domain matches in a full alignment, we count the number that are found on all sequences in the alignment. This total is shown in the purple box.
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There is 1 interaction for this family. More...
We determine these interactions using iPfam, which considers the interactions between residues in three-dimensional protein structures and maps those interactions back to Pfam families. You can find more information about the iPfam algorithm in the journal article that accompanies the website.
For those sequences which have a structure in the Protein DataBank, we use the mapping between UniProt, PDB and Pfam coordinate systems from the PDBe group, to allow us to map Pfam domains onto UniProt sequences and three-dimensional protein structures. The table below shows the structures on which the Glypican domain has been found. There are 18 instances of this domain found in the PDB. Note that there may be multiple copies of the domain in a single PDB structure, since many structures contain multiple copies of the same protein sequence.
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