Mouse Agrin(AGRN) ELISA kit

heparan sulfate basal lamina glycoprotein that plays a central role in the formation and the maintenance of the neuromuscular junction (NMJ) and directs key events in postsynaptic differentiation. This neuron-specific (z+) isoform is a component of the AGRN-LRP4 receptor complex that induces the phosphorylation and activation of MUSK. The activation of MUSK in myotubes induces the formation of NMJ by regulating different processes including the transcription of specific genes and the clustering of AChR in the postsynaptic membrane. Calcium ions are required for maximal AChR clustering. AGRN function in neurons is highly regulated by alternative splicing, glycan binding and proteolytic processing. Modulates calcium ion homeostasis in neurons, specifically by inducing an increase in cytoplasmic calcium ions. Functions differentially in the central nervous system (CNS) by inhibiting the alpha(3)-subtype of Na+/K+-ATPase and evoking depolarization at CNS synapses. This transmembrane agrin (TM-agrin) isoform, the predominate form in neurons of the brain, induces dendritic filopodia and synapse formation in mature hippocampal neurons in large part due to the attached glycosaminoglycan chains and the action of Rho-family GTPases.; Isoform 2 and isoform 3: these isoforms lacking the 'z' insert (z0) are muscle-specific, have no AChR clustering ability and may be involved in nervous system endothelial cell differentiation.; involved in regulation of neurite outgrowth probably due to the presence of the glycosaminoglcan (GAG) side chains of heparan and chondroitin sulfate attached to the Ser/Thr- and Gly/Ser-rich regions. Also involved in modulation of growth factor signaling.; this released fragment is important for agrin signaling and to exert a maximal dendritic filopodia-inducing effect. All 'z' splice variants (z+) of this fragment also show an increase in the number of filopodia.

1. The presence of agrin at locations with particular importance for the growth and stability of atherosclerotic plaques renders this molecule strategically positioned to influence plaque development and vulnerability PMID: 29405249
2. Agrin induces clustering and activation of EphB1 receptors on developing erythroblasts, leading to the activation of alpha5beta1 integrins. PMID: 26990660
3. identificaton of agrin, a component of neonatal extracellular matrix, as required for the full regenerative capacity of neonatal mouse hearts PMID: 28581497
4. The presence of C-terminal fragment of agrin (CAF) in urine suggests either glomerular filtration or secretion into urine. PMID: 27380275
5. Agrin strongly promotes chondrocyte differentiation and cartilage formation in vivo. PMID: 26290588
6. Reveal novel roles for APP in regulating neuromuscular synapse formation through hetero-oligomeric interaction with LRP4 and agrin and thereby provide new insights into the molecular mechanisms that govern NMJ formation and maintenance. PMID: 23986861
7. Agrin is frequently upregulated and important for oncogenic property of hepatocellular carcinoma. PMID: 25630468
8. agrin contributes to barrier characteristics of brain endothelium. PMID: 25107608
9. NMJs in agrin-deficient mice rapidly disappear after birth. Agrin is essential for postnatal NMJ maintenance, but not for their embryonic formation, and also for the postnatal, but not prenatal, midmuscle localization of postsynaptic specializations. PMID: 25368159
10. reviews the evidence that agrin regulates synapse development, plasticity and signaling in the brain and discusses the evidence for the proposed mechanisms PMID: 22414531
11. Using gamma-secretase drug inhibitors and presenilin mutants in embryonic fibroblasts, we found that a mature gamma-secretase complex was required to repress neurotrypsin expression and agrin cleavage. PMID: 24145027
12. Neural agrin slows the degradation of surface AChR in cultured muscle cellsb via phosphorylation of the AChR beta subunit at Y390, stabilizing AChR at developing synapses & adult neuromuscular junctions. PMID: 23325468
13. Agrin is Required for Maintenance of the Postsynaptic Apparatus. Agrin Loss Disrupts Nerve Terminal Organization PMID: 23056392
14. Two classic synaptic signalling systems (neural agrin and neuregulin-1) converge upon MuSK to regulate postsynaptic differentiation. PMID: 22328506
15. Agrin induces association of Chrna1 mRNA and nicotinic acetylcholine receptor in C2C12 myotubes. PMID: 22884571
16. The suppression of agrin reduced hyperambulation and holeboard exploration, restored anxiety-like behavior (or reduced risk-taking behavior), improved prepulse inhibition, shortened the circadian period and increased brain Na(+) ,K(+) -ATPase activity. PMID: 22520507
17. the cascade linking agrin to CLASP2-mediated microtubule capturing at the synaptic membrane is essential for the maintenance of a normal neuromuscular phenotype PMID: 22851317
18. Agrin deficiency impairs monocytic cell maturation. PMID: 22517892
19. Studies of neurotrypsin-deficient and agrin-overexpressing mice revealed that old-age sarcopenia also develops without neurotrypsin and is not prevented by elevated levels of agrin. Define neurotrypsin- and age-dependent sarcopenia as 2 distinct entities. PMID: 21885656
20. The Agrn point mutation is a model for congenital myasthenic syndromes caused by Agrn mutations and potentially other related neuromuscular diseases. PMID: 21890498
21. These results indicate that AGRIN is important for maintaining blood-brain barrier composition and that changes in Agrn expression (particularly vessel-associated AGRIN) influence Abeta homeostasis in mouse models of Alzheimer disease. PMID: 22082664
22. Many clusters of acetylcholine receptors are observed in nestin/agrin double knockout-out mutants compared to significantly fewer in agrin single knockouts. PMID: 21832185
23. The results support influence of agrin on AQP4, orthogonal arrays of particles and volume regulation. PMID: 20920487
24. The agrin C22 construct, constitutes a well-folded, stable domain, while the deletion of 48 residues that correspond to strands beta1-beta4 of the agrin laminin G3 domain imposed by the agrin C15 construct leads to a misfolded protein. PMID: 21037280
25. A role is proposed for agrin and laminin binding to alpha-dystrogycan at sensory synapses that places this activity upstream of neuregulin-ErbB signaling. PMID: 20213761
26. the N-terminal half of agrin is involved in agrin's ability to inhibit neurite outgrowth. PMID: 11793362
27. regulates neuronal responses to excitatory neurotransmitters PMID: 11817901
28. Agrin plays an organizing role in the formation of sympathetic synapses PMID: 12221070
29. Structures required for agrin signaling in CNS neurons are contained within a 20-kD COOH-terminal fragment of the protein. Distinct regions within agrin are responsible for receptor binding and activation. PMID: 12796478
30. Expression of agrin in non-synaptic region varies greatly between different muscles in wild-type mice and its levels are altered in dystrophic muscle. PMID: 12798796
31. Agrn becomes concentrated at neuroeffector and neuromuscular junctions in developing urinary bladder. PMID: 15711988
32. agrin and perlecan cluster with laminin-2 to contribute to assembly of aneural AChR clusters that precede neural agrin release as well as affect later NMJ development PMID: 16219760
33. agrin is able to rapidly and fully negate the laminin substrate clustering effect while inducing the rapid formation of new clusters. Acetylcholine receptor (AChR) half-life is not affected by agrin despite its role in inducing aggregation of AChRs. PMID: 16256100
34. These data provide the first evidence for a specific role of TM-agrin in shaping the cytoskeleton of neurites in the developing nervous system. PMID: 16364653
35. findings strongly indicate that agrin and alpha-dystroglycan mediate lymphocyte activation; furthermore, agrin-involved lymphocyte activation is mediated by alpha-dystroglycan PMID: 16394267
36. These data demonstrate that, through its interaction with the alpha3 sodium-potassium ATPase, agrin regulates activity-dependent processes in neurons, providing a molecular framework for agrin action in the CNS. PMID: 16630822
37. agrin likely triggers AChR clustering or maintains clusters through the coalescence of lipid rafts which play a pivotal role in the assembly of the postsynaptic membrane at the neuromuscular junction upon agrin signaling PMID: 16816402
38. Data show that agrin is highly expressed by chondrocytes and localizes to the growth plate in wild-type mice and plays a critical role in normal skeletal growth. PMID: 17186266
39. Transgenic mice overexpressing the heparan sulfate proteoglycan agrin have severe ocular dysgenesis. PMID: 17196957
40. agrin is required for proper structural and functional development of an interneuronal synapse in vivo PMID: 17443806
41. dysregulation of agrin processing is a good candidate for a pathogenetic mechanism underlying mental retardation PMID: 17586728
42. Although agrin contributes significantly to the anionic charge to the GBM, both it and its charge are not needed for glomerular permselectivity. PMID: 17591961
43. Agrin plays an important role in the formation and/or the maintenance of excitatory synapses in the brain. PMID: 17611272
44. The acetylcholine receptor-associated protein rapsyn interacted with calpain in an agrin-dependent manner, and this interaction inhibited the protease activity of calpain. PMID: 17640526
45. neurotrypsin exclusively cleaves glycanated variants of agrin; neurotrypsin-dependent cleavage of agrin was concentrated at synapses, where the most heavily glycanated variants of agrin predominate PMID: 18230682
46. Our study reveals a potentially novel mechanism that regulates agrin/MuSK signaling cascade. PMID: 18272689
47. At the postnatal neuromuscular synapse agrin signaling elevates the expression and targeting of rapsyn to the postsynaptic membrane, thereby packing more AChRs into stable, functionally-important AChR aggregates. PMID: 18506821
48. Muscle-wide secretion of a miniaturized form of neural agrin rescues focal neuromuscular innervation in agrin mutant mice. PMID: 18685098
49. These data are consistent with a role for Pofut1 in AChR aggregation during synaptogenesis via the regulation of the synaptogenic activity of muscle agrin. PMID: 18775496
50. These experiments indicate that Lrp4 is the long-sought and elusive receptor for Agrin and has a critical role in activating MuSK and stimulating neuromuscular synapse formation. PMID: 18848351

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Cell junction, synapse. Cell membrane; Single-pass type II membrane protein.

Expressed in central nervous system (CNS) synapses such as in the cerebral cortex and hippocampus. Localizes to basal lamina of hippocampal blood vessels. Both (z+) and (z-) isoforms found in kidney, heart and cerebral vasculature.

STRING: 10090.ENSMUSP00000137931

UniGene: Mm.273098