| Agrin NtA domain | |||||||||
|---|---|---|---|---|---|---|---|---|---|
| Identifiers | |||||||||
| Symbol | NtA | ||||||||
| Pfam | PF03146 | ||||||||
| InterPro | IPR004850 | ||||||||
| SCOP2 | 1jc7 / SCOPe / SUPFAM | ||||||||
| |||||||||
Agrin is a large proteoglycan whose best-characterised role is in the development of the neuromuscular junction during embryogenesis. Agrin is named based on its involvement in the aggregation of acetylcholine receptors during synaptogenesis. In humans, this protein is encoded by the AGRN gene.[5][6][7]
This protein has nine domains homologous to protease inhibitors.[8] It may also have functions in other tissues and during other stages of development. It is a major proteoglycan component in the glomerular basement membrane and may play a role in the renal filtration and cell-matrix interactions.[9]
Agrin functions by activating the MuSK protein (for Muscle-Specific Kinase), [10] which is a receptor tyrosine kinase required for the formation and maintenance of the neuromuscular junction.[11] Agrin is required to activate MuSK.[12] Agrin is also required for neuromuscular junction formation.[13]
- ^ a b c GRCh38: Ensembl release 89: ENSG00000188157 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000041936 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Rupp F, Payan DG, Magill-Solc C, Cowan DM, Scheller RH (May 1991). "Structure and expression of a rat agrin". Neuron. 6 (5): 811–823. doi:10.1016/0896-6273(91)90177-2. PMID 1851019. S2CID 44440186.
- ^ Kröger S, Schröder JE (October 2002). "Agrin in the developing CNS: new roles for a synapse organizer". News in Physiological Sciences. 17 (5): 207–212. doi:10.1152/nips.01390.2002. PMID 12270958. S2CID 2988918.
- ^ Groffen AJ, Buskens CA, van Kuppevelt TH, Veerkamp JH, Monnens LA, van den Heuvel LP (May 1998). "Primary structure and high expression of human agrin in basement membranes of adult lung and kidney". European Journal of Biochemistry. 254 (1): 123–128. doi:10.1046/j.1432-1327.1998.2540123.x. PMID 9652404.
- ^ Tsen G, Halfter W, Kröger S, Cole GJ (February 1995). "Agrin is a heparan sulfate proteoglycan". The Journal of Biological Chemistry. 270 (7): 3392–3399. doi:10.1074/jbc.270.7.3392. PMID 7852425.
- ^ Groffen AJ, Ruegg MA, Dijkman H, van de Velden TJ, Buskens CA, van den Born J, et al. (January 1998). "Agrin is a major heparan sulfate proteoglycan in the human glomerular basement membrane". The Journal of Histochemistry and Cytochemistry. 46 (1): 19–27. doi:10.1177/002215549804600104. PMID 9405491. S2CID 24353753.
- ^ Valenzuela DM, Stitt TN, DiStefano PS, Rojas E, Mattsson K, Compton DL, Nunez L, Park JS, Stark JL, Gies DR, Thomas S, LeBeau MM, Fernald AA, Copeland NG, Jenkins NA, Burden SJ, Glass DJ, Yancopoulos GD (Sep 1995). "Receptor tyrosine kinase specific for the skeletal muscle lineage: expression in embryonic muscle, at the neuromuscular junction, and after injury". Neuron. 15 (3): 573–584. doi:10.1016/0896-6273(95)90146-9. PMID 7546737.
- ^ DeChiara TM, Bowen DC, Valenzuela DM, Simmons MV, Poueymirou WT, Thomas S, Kinetz E, Compton DL, Rojas E, Park JS, Smith C, DiStefano PS, Glass DJ, Burden SJ, Yancopoulos GD (May 1996). "The receptor tyrosine kinase MuSK is required for neuromuscular junction formation in vivo". Cell. 85 (4): 501–512. doi:10.1016/s0092-8674(00)81251-9. PMID 8653786.
- ^ Glass DJ, Bowen DC, Stitt TN, Radziejewski C, Bruno J, Ryan TE, Gies DR, Shah S, Mattson K, Burden SJ, DiStefano PS, Valenzuela DM, DeChiara TM, Yancopoulos GD (May 1996). "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513–523. doi:10.1016/s0092-8674(00)81252-0. PMID 8653787.
- ^ Gautam M, Noakes PG, Moscoso L, Rupp F, Scheller RH, Merlie JP, Sanes JR (May 1996). "Defective neuromuscular synaptogenesis in agrin-deficient mutant mice". Cell. 85 (4): 525–535. doi:10.1016/s0092-8674(00)81253-2. PMID 8653788.