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anti-Mouse (Murine) Antibodies:
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Rat (Rattus) Monoclonal AGRN Primary Antibody for WB - ABIN446630
Clapcote, Duffy, Xie, Kirshenbaum, Bechard, Rodacker Schack, Petersen, Sinai, Saab, Lerch, Minassian, Ackerley, Sled, Cortez, Henderson, Vilsen, Roder: Mutation I810N in the alpha3 isoform of Na+,K+-ATPase causes impairments in the sodium pump and hyperexcitability in the CNS. in Proceedings of the National Academy of Sciences of the United States of America 2009
MYO9A deficiency in motor neurons is associated with reduced neuromuscular agrin secretion.
These studies provide evidence that a signaling pathway involving agrin, Fgfs and Shh may be a critical target of ethanol exposure during zebrafish embryogenesis.
Agrin expression and function may be a target of ethanol exposure during embryogenesis.
Agrin plays an important role in both peripheral and CNS development and also modulates posterior development in zebrafish.
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
Agrin induces clustering and activation of EphB1 receptors on developing erythroblasts, leading to the activation of alpha5beta1 integrins.
identificaton of agrin, a component of neonatal extracellular matrix, as required for the full regenerative capacity of neonatal mouse hearts
The presence of C-terminal fragment of agrin (CAF) in urine suggests either glomerular filtration or secretion into urine.
Agrin strongly promotes chondrocyte differentiation and cartilage formation in vivo.
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.
Agrin is frequently upregulated and important for oncogenic property of hepatocellular carcinoma.
agrin contributes to barrier characteristics of brain endothelium.
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.
reviews the evidence that agrin regulates synapse development, plasticity and signaling in the brain and discusses the evidence for the proposed mechanisms
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.
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.
Agrin is Required for Maintenance of the Postsynaptic Apparatus. Agrin Loss Disrupts Nerve Terminal Organization
Two classic synaptic signalling systems (neural agrin and neuregulin-1) converge upon MuSK to regulate postsynaptic differentiation.
Agrin induces association of Chrna1 mRNA and nicotinic acetylcholine receptor in C2C12 myotubes.
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.
the cascade linking agrin to CLASP2-mediated microtubule capturing at the synaptic membrane is essential for the maintenance of a normal neuromuscular phenotype
Agrin deficiency impairs monocytic cell maturation.
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.
agrin is highly expressed in nuclei of lung adenocarcinoma tissues and is strongly correlated with lymph node metastasis, clinical stage, and poor differentiation
High Agrin expression is associated with Chronic obstructive pulmonary disease.
C-terminal agrin fragment levels predict acute kidney injury after acute myocardial infarction.
Agrin promotes oncogenesis through YAP-dependent transcription.
Knockdown of agrin and perlecan promoted a decrease on cell migration and adhesion, and on resistance of cells to cisplatin.
Among 42 hip fractured patients (age 83.7+/-8.6 years, 76.2% women), sarcopenia was diagnosed in 7 individuals (16.7%). Serum C-terminal agrin fragment (CAF) levels were significantly higher in sarcopenic relative to non-sarcopenic patients.
In patients suffering from severe sepsis and septic shock, serum levels of C-terminal agrin fragment were significantly associated with kidney function and the need for renal replacement therapy and were not influenced by severe septic conditions.
MuSK myasthenia gravis IgG4 disrupts the interaction of LRP4 with MuSK but both IgG4 and IgG1-3 can disperse preformed agrin-independent AChR clusters
these observations indicate that agrin is another autoantigen in patients with MG and agrin autoantibodies may be pathogenic through inhibition of agrin/LRP4/MuSK signaling at the NMJ.
Five new recessive mutations in the gene encoding agrin are identified in patients with congenital myasthenic syndrome.
study identifies a spontaneous agrin mutation that reduces the ability of z+ agrin to activate MuSK and induce AChR clustering; this results in a severe congenital myasthenic syndrome in the patient, with both pre- and postsynaptic defects at the neuromuscular junction
Dynamics of expression patterns of agrin in human glioblastoma
In contrast to wild-type neurons which form synapses and survive for prolonged periods, agrin-deficient neurons do not mature and are rapidly eliminated in the transgenic olfactory bulb.
Agrin immunohistochemistry may facilitate determination of primary versus metastatic origin in problematic liver cancer cases.
different regions within the agrin protein are responsible for synapse formation at the neuromuscular junction and for process formation in central nervous system neurons
Agrin, a heparan sulfate proteoglycan, is a component of the basal lamina of BBB microvessels, and growing evidence suggests that it may be important for the maintenance of the BBB.
acts at the nerve-muscle synapse in the glomerular basal membrane and on T-lymphocytes
evidence for additional functions of agrin during axonal growth, establishment of the blood-brain barrier, and Alzheimer's disease is accumulating--REVIEW
This gene encodes one of several proteins that are critical in the development of the neuromuscular junction (NMJ), as identified in mouse knock-out studies. The encoded protein contains several laminin G, Kazal type serine protease inhibitor, and epidermal growth factor domains. Additional post-translational modifications occur to add glycosaminoglycans and disulfide bonds. In one family with congenital myasthenic syndrome affecting limb-girdle muscles, a mutation in this gene was found.
, agrin proteoglycan
, heparan sulfate proteoglycan