A protein component of the synaptic basal lamina. It has been shown to induce clustering of acetylcholine receptors on the surface of muscle fibers and other synaptic molecules in both synapse regeneration and development.
Cell surface proteins that bind acetylcholine with high affinity and trigger intracellular changes influencing the behavior of cells. Cholinergic receptors are divided into two major classes, muscarinic and nicotinic, based originally on their affinity for nicotine and muscarine. Each group is further subdivided based on pharmacology, location, mode of action, and/or molecular biology.
Chemically stimulated aggregation of cell surface receptors, which potentiates the action of the effector cell.
Dystrophin-associated proteins that play role in the formation of a transmembrane link between laminin-2 and DYSTROPHIN. Both the alpha and the beta subtypes of dystroglycan originate via POST-TRANSLATIONAL PROTEIN PROCESSING of a single precursor protein.
The synapse between a neuron and a muscle.
Cell membranes associated with synapses. Both presynaptic and postsynaptic membranes are included along with their integral or tightly associated specializations for the release or reception of transmitters.
Large, multinucleate single cells, either cylindrical or prismatic in shape, that form the basic unit of SKELETAL MUSCLE. They consist of MYOFIBRILS enclosed within and attached to the SARCOLEMMA. They are derived from the fusion of skeletal myoblasts (MYOBLASTS, SKELETAL) into a syncytium, followed by differentiation.

Globular domains of agrin are functional units that collaborate to induce acetylcholine receptor clustering. (1/304)

Agrin, an extracellular matrix protein involved in neuromuscular junction formation, directs clustering of postsynaptic molecules, including acetylcholine receptors (AChRs). This activity resides entirely in the C-terminal portion of the protein, which consists of three laminin-like globular domains (G-domains: G1, G2 and G3) and four EGF-like repeats. Additionally, alternate mRNA splicing yields G-domain variants G2(0,4) with 0- or 4-amino-acid inserts, and G3(0, 8,11,19) with 0-, 8-, 11- or 19-amino-acid inserts. In order to better understand the contributions of individual domains and alternate splicing to agrin activity, single G-domains and covalently linked pairs of G-domains were expressed as soluble proteins and their AChR clustering activity measured on cultured C2 myotubes. These analyses reveal the following: (1) While only G3(8) exhibits detectable activity by itself, all G-domains studied (G1, G2(0), G2(4), G3(0) and G3(8)) enhance G3(8) activity when physically linked to G3(8). This effect is most pronounced when G2(4) is linked to G3(8) and is independent of the order of the G-domains. (2) The deletion of EGF-like repeats enhances activity. (3) Increasing the physical separation between linked G1 and G3(8) domains produces a significant increase in activity; similar alterations to linked G2 and G3(8) domains are without effect. (4) Clusters induced by two concatenated G3(8) domains are significantly smaller than all other agrin forms studied. These data suggest that agrin G-domains are the functional units which interact independently of their specific organization to yield AChR clustering. G-domain synergism resulting in biological output could be due to physical interactions between G-domains or, alternatively, independent interactions of G-domains with cell surface receptors which require spatially localized coactivation for optimal signal transduction.  (+info)

Constitutively active MuSK is clustered in the absence of agrin and induces ectopic postsynaptic-like membranes in skeletal muscle fibers. (2/304)

In skeletal muscle fibers, neural agrin can direct the accumulation of acetylcholine receptors (AChR) and transcription of AChR subunit genes from the subsynaptic nuclei. Although the receptor tyrosine kinase MuSK is required for AChR clustering, it is less clear whether MuSK regulates gene transcription. To elucidate the role of MuSK in these processes, we constructed a constitutively active MuSK receptor, MuSKneuTMuSK, taking advantage of the spontaneous homodimerization of the transmembrane domain of neuT, an oncogenic variant of the neu/erbB2 receptor. In the extrasynaptic region of innervated muscle fibers, MuSKneuTMuSK formed highly concentrated aggregates that colocalized with AChR clusters. Associated with MuSK-induced AChR clusters was a normal complement of synaptic proteins. Moreover, transcription of the AChR-epsilon subunit gene was increased, albeit via an indirect mechanism by MuSK-induced aggregation of erbB receptors and neuregulin. Although neural agrin was not required, the activity of MuSKneuTMuSK was nevertheless potentiated by ectopic expression of a muscle agrin isoform inactive in AChR clustering. To define the role of the kinase domain in the formation of a postsynaptic-like membrane, a second fusion receptor, neuneuTMuSK, which included the MuSK kinase but not the MuSK extracellular domain, was expressed. Significantly, neuneuTMuSK induced AChR clusters that colocalized with aggregates of endogenous MuSK. Taken together, it was concluded that the MuSK kinase domain is sufficient to initiate the recruitment of additional MuSK receptors, which then develop into highly concentrated aggregates by means of a positive feedback loop to induce a postsynaptic membrane in the absence of neural agrin.  (+info)

Agrin in Alzheimer's disease: altered solubility and abnormal distribution within microvasculature and brain parenchyma. (3/304)

Agrin is a heparan sulfate proteoglycan that is widely expressed in neurons and microvascular basal lamina in the rodent and avian central nervous system. Agrin induces the differentiation of nerve-muscle synapses, but its function in either normal or diseased brains is not known. Alzheimer's disease (AD) is characterized by loss of synapses, changes in microvascular architecture, and formation of neurofibrillary tangles and senile plaques. Here we have asked whether AD causes changes in the distribution and biochemical properties of agrin. Immunostaining of normal, aged human central nervous system revealed that agrin is expressed in neurons in multiple brain areas. Robust agrin immunoreactivity was observed uniformly in the microvascular basal lamina. In AD brains, agrin is highly concentrated in both diffuse and neuritic plaques as well as neurofibrillary tangles; neuronal expression of agrin also was observed. Furthermore, patients with AD had microvascular alterations characterized by thinning and fragmentation of the basal lamina. Detergent extraction and Western blotting showed that virtually all the agrin in normal brain is soluble in 1% SDS. In contrast, a large fraction of the agrin in AD brains is insoluble under these conditions, suggesting that it is tightly associated with beta-amyloid. Together, these data indicate that the agrin abnormalities observed in AD are closely linked to beta-amyloid deposition. These observations suggest that altered agrin expression in the microvasculature and the brain parenchyma contribute to the pathogenesis of AD.  (+info)

Alternatively spliced isoforms of nerve- and muscle-derived agrin: their roles at the neuromuscular junction. (4/304)

Agrin induces synaptic differentiation at the skeletal neuromuscular junction (NMJ); both pre- and postsynaptic differentiation are drastically impaired in its absence. Multiple alternatively spliced forms of agrin that differ in binding characteristics and bioactivity are synthesized by nerve and muscle cells. We used surgical chimeras, isoform-specific mutant mice, and nerve-muscle cocultures to determine the origins and nature of the agrin required for synaptogenesis. We show that agrin containing Z exons (Z+) is a critical nerve-derived inducer of postsynaptic differentiation, whereas neural isoforms containing a heparin binding site (Y+) and all muscle-derived isoforms are dispensable for major steps in synaptogenesis. Our results also suggest that the requirement of agrin for presynaptic differentiation is mediated indirectly by its ability to promote postsynaptic production or localization of appropriate retrograde signals.  (+info)

Roles of rapsyn and agrin in interaction of postsynaptic proteins with acetylcholine receptors. (5/304)

At the neuromuscular junction, aggregates of acetylcholine receptors (AChRs) are anchored in the muscle membrane by association with rapsyn and other postsynaptic proteins. We have investigated the interactions between the AChR and these proteins in cultured C2 myotubes before and after treatment with agrin, a nerve-derived protein that induces AChRs to cluster. When AChRs were isolated from detergent extracts of untreated C2 myotubes, they were associated with rapsyn and, to a lesser degree, with utrophin, beta-dystroglycan, MuSK, and src-related kinases, but not with syntrophin. Treatment with agrin increased the association of AChRs with MuSK, a receptor tyrosine kinase that forms part of the agrin receptor complex, without affecting other interactions. Analysis of rapsyn-deficient myotubes, which do not form protein clusters in response to agrin, revealed that rapsyn is required for association of the AChR with utrophin and beta-dystroglycan, and for the agrin-induced increase in association with MuSK, but not for constitutive interactions with MuSK and src-related kinases. In rapsyn -/- myotubes, agrin caused normal tyrosine phosphorylation of AChR-associated and total MuSK, whereas phosphorylation of the AChR beta subunit, both constitutive and agrin-induced, was strongly reduced. These results show first that aneural myotubes contain preassembled AChR protein complexes that may function in the assembly of the postsynaptic apparatus, and second that rapsyn, in addition to its role in AChR phosphorylation, mediates selected protein interactions with the AChR and serves as a link between the AChR and the dystrophin/utrophin glycoprotein complex.  (+info)

Evidence of an agrin receptor in cortical neurons. (6/304)

Agrin plays a key role in directing the differentiation of the vertebrate neuromuscular junction. Understanding agrin function at the neuromuscular junction has come via molecular genetic analyses of agrin as well as identification of its receptor and associated signal transduction pathways. Agrin is also expressed by many populations of neurons in brain, but its role remains unknown. Here we show, in cultured cortical neurons, that agrin induces expression of the immediate early gene c-fos in a concentration-dependent and saturable manner, as expected for a signal transduction pathway activated by a cell surface receptor. Agrin is active in cortical neurons at picomolar concentrations, is Ca(2+) dependent, and is inhibited by heparin and staurosporine. Despite marked differences in acetylcholine receptor (AChR)-clustering activity, all alternatively spliced forms of agrin are equally potent inducers of c-fos in cortical neurons. A similar, isoform-independent response to agrin was also observed in cultures prepared from the hippocampus and cerebellum. Only agrin with high AChR-clustering activity was effective in cultured muscle, whereas non-neuronal cells were agrin insensitive. Although consistent with a receptor tyrosine kinase model similar to the muscle-specific kinase-myotube-associated specificity component complex in muscle, our data suggest that CNS neurons express a unique agrin receptor. Evidence that neuronal signal transduction is mediated via an increase in intracellular Ca(2+) means that agrin is well situated to influence important Ca(2+)-dependent functions in brain, including neuronal growth, differentiation, and adaptive changes in gene expression associated with synaptic remodeling.  (+info)

Distinct domains of MuSK mediate its abilities to induce and to associate with postsynaptic specializations. (7/304)

Agrin released from motor nerve terminals activates a muscle-specific receptor tyrosine kinase (MuSK) in muscle cells to trigger formation of the skeletal neuromuscular junction. A key step in synaptogenesis is the aggregation of acetylcholine receptors (AChRs) in the postsynaptic membrane, a process that requires the AChR-associated protein, rapsyn. Here, we mapped domains on MuSK necessary for its interactions with agrin and rapsyn. Myotubes from MuSK(-/)- mutant mice form no AChR clusters in response to agrin, but agrin-responsiveness is restored by the introduction of rat MuSK or a Torpedo orthologue. Thus, MuSK(-/)- myotubes provide an assay system for the structure-function analysis of MuSK. Using this system, we found that sequences in or near the first of four extracellular immunoglobulin-like domains in MuSK are required for agrin responsiveness, whereas sequences in or near the fourth immunoglobulin-like domain are required for interaction with rapsyn. Analysis of the cytoplasmic domain revealed that a recognition site for the phosphotyrosine binding domain-containing proteins is essential for MuSK activity, whereas consensus binding sites for the PSD-95/Dlg/ZO-1-like domain-containing proteins and phosphatidylinositol-3-kinase are dispensable. Together, our results indicate that the ectodomain of MuSK mediates both agrin- dependent activation of a complex signal transduction pathway and agrin-independent association of the kinase with other postsynaptic components. These interactions allow MuSK not only to induce a multimolecular AChR-containing complex, but also to localize that complex to a primary scaffold in the postsynaptic membrane.  (+info)

Formation of the neuromuscular junction. Agrin and its unusual receptors. (8/304)

Synapses are essential relay stations for the transmission of information between neurones and other cells. An ordered and tightly regulated formation of these structures is crucial for the functioning of the nervous system. The induction of the intensively studied synapse between nerve and muscle is initiated by the binding of neurone-specific isoforms of the basal membrane protein agrin to receptors on the surface of myotubes. Agrin activates a receptor complex that includes the muscle-specific kinase and most likely additional, yet to be identified, components. Receptor activation leads to the aggregation of acetylcholine receptors (AChR) and other proteins of the postsynaptic apparatus. This activation process has unique features which distinguish it from other receptor tyrosine kinases. In particular, the autophosphorylation of the kinase domain, which usually induces the recruitment of adaptor and signalling molecules, is not sufficient for AChR aggregation. Apparently, interactions of the extracellular domain with unknown components are also required for this process. Agrin binds to a second protein complex on the muscle surface known as the dystrophin-associated glycoprotein complex. This binding forms one end of a molecular link between the extracellular matrix and the cytoskeleton. While many components of the machinery triggering postsynaptic differentiation have now been identified, our picture of the molecular pathway causing the redistribution of synaptic proteins is still incomplete.  (+info)

Also, agrin may be involved in blood-brain barrier (BBB) formation and/or function and it influences Aβ homeostasis. Agrin is ... Agrin is required to activate MuSK, which is similarly also required for neuromuscular junction formation. Agrin was first ... During development in humans, the growing end of motor neuron axons secrete a protein called agrin. When secreted, agrin binds ... The requirement for Agrin and MuSK in the formation of the NMJ was demonstrated primarily by knockout mouse studies. In mice ...
Below is a list of human proteins containing the EGF-like domain: AGC1; AGRIN; AREG; ATRN; ATRNL1; BCAN; BMP1; BTC; C1S; CASPR4 ...
Moberg, Paul J.; Agrin, Rachel; Gur, Raquel E.; Gur, Ruben C.; Turetsky, Bruce I.; Doty, Richard L. (September 1999). " ...
The Famous Cookery Cookbook with Gloria Agrin Josephson (1963) Cafe Society: The Wrong Place for the Right People with Terry ... Josephson, Gloria Agrin; Josephson, Barney (1963). The Famous Cookery Cookbook. Horizon Press. LCCN 63013205. Josephson, Barney ...
1996). "Alternative splicing of agrin alters its binding to heparin, dystroglycan, and the putative agrin receptor." Neuron 16( ... Ruegg, M A; Tsim, K W; Horton, S E; Kröger, S; Escher, G; Gensch, E M; McMahan, U J (April 1992). "The agrin gene codes for a ... Tsim, K W; Ruegg, M A; Escher, G; Kröger, S; McMahan, U J (April 1992). "cDNA that encodes active agrin". Neuron. 8 (4): 677- ... Denzer, A J; Brandenberger, R; Gesemann, M; Chiquet, M; Ruegg, M A (1997-05-05). "Agrin binds to the nerve-muscle basal lamina ...
May 1996). "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513-23. doi:10.1016/S0092-8674(00)81252-0. PMID 8653787. ... In mice which are deficient for either agrin or MuSK, the neuromuscular junction does not form. Upon activation by its ligand ... Furthermore, the nerve-derived organizing factor agrin fails to stimulate MuSK activation in muscle cells genetically null for ... agrin, MuSK signals via the proteins called Dok-7 and rapsyn, to induce "clustering" of acetylcholine receptors (AChR). Cell ...
Agrin, a heparin proteoglycan, and MuSK kinase are thought to help stabilize the accumulation of AChR in the central regions of ... In mice which are deficient for either agrin or MuSK, the neuromuscular junction does not form. Further, mice deficient in Dok- ... Upon activation by its ligand agrin, MuSK signals via two proteins called "Dok-7" and "rapsyn", to induce "clustering" of ... "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513-23. doi:10.1016/S0092-8674(00)81252-0. PMID 8653787. S2CID 14930468 ...
May 1996). "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513-23. doi:10.1016/S0092-8674(00)81252-0. PMID 8653787. ...
Upon activation by its ligand agrin, MuSK signals via the proteins called casein kinase 2 (CK2), Dok-7 and rapsyn, to induce " ... It is activated by a nerve-derived proteoglycan called agrin, which is similarly also required for neuromuscular junction ... "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513-523. doi:10.1016/s0092-8674(00)81252-0. PMID 8653787. Gautam M, ... "Agrin acts via a MuSK receptor complex". Cell. 85 (4): 513-523. doi:10.1016/s0092-8674(00)81252-0. PMID 8653787. Cheusova T, ...
For example, agrin was first isolated from Torpedo. Scribonius Largus, a first century physician, advised the use of a live ...
Also, ennui is very important for agrin function. Ennui is very important in nerve-dependent acetylcholine clustering and the ...
Agrin induces clustering of AchRs on the muscle surface and synapse formation is disrupted in agrin knockout mice. Agrin ... Agrin appears not to be a central mediator of CNS synapse formation and there is active interest in identifying signals that ... They also showed that the synaptogenic signal is produced by the nerve, and they identified the factor as Agrin. ...
The dystroglycan complex is also known to serve as an agrin receptor in muscle, where it may regulate agrin-induced ... Gesemann M, Brancaccio A, Schumacher B, Ruegg MA (Jan 1998). "Agrin is a high-affinity binding protein of dystroglycan in non- ... Actin-binding protein Agrin GRCh38: Ensembl release 89: ENSG00000173402 - Ensembl, May 2017 GRCm38: Ensembl release 89: ... is a functional agrin receptor". Cell. 77 (5): 675-86. doi:10.1016/0092-8674(94)90052-3. PMID 8205617. S2CID 54232250. ...
Burkin DJ, Kim JE, Gu M, Kaufman SJ (2000). "Laminin and alpha7beta1 integrin regulate agrin-induced clustering of ...
Other, less frequent antibodies are found against LRP4, agrin, and titin proteins. Human leukocyte antigen haplotypes are ...
Agrin is unable to accept Riga as anything besides a taint, a continuous reminder of her brutal past. Agrin tries to abandon ... After multiple tries, Agrin finally ties Riga to a rock and throws him to the bottom of the lake, afterwards committing suicide ... He falls for a girl named Agrin, an orphan from Halabja who has recently came to the refugee camps, assisting her whenever ... Hengov grieves on the cliff from where Agrin jumped to her death. Meanwhile, a disabled Kak Satellite loses any charm he had ...
The rapsyn protein interacts directly with the AChRs and plays a vital role in agrin-induced clustering of the AChR. Without ... This pathway consists of agrin, muscle-specific tyrosine kinase (MuSK protein), AChRs and the AChR-clustering protein rapsyn, ... Han H, Noakes PG, Phillips WD (September 1999). "Overexpression of rapsyn inhibits agrin-induced acetylcholine receptor ... "Rapsyn may function as a link between the acetylcholine receptor and the agrin-binding dystrophin-associated glycoprotein ...
Meinen S, Lin S, Thurnherr R, Erb M, Meier T, Rüegg MA (2011). "Apoptosis inhibitors and mini-agrin have additive benefits in ... Meinen S, Lin S, Thurnherr R, Erb M, Meier T, Rüegg MA (August 2011). "Apoptosis inhibitors and mini-agrin have additive ... Given that the technology for mini-agrin administration to skeletal muscle in human subjects is not yet available, omigapil is ... Omigapil coupled with mini-agrin overexpression works as a dual treatment that enhances mechanical load bearing ability and ...
Agrin and Ueda continued work on the site with Sean McGregor, a web developer. In 2011, Ueda began collaboration with Scott ... iNaturalist began in 2008 as a UC Berkeley School of Information Master's final project of Nate Agrin, Jessica Kline, and Ken- ...
... , along with laminin, perlecan, agrin, neurexin, binds to α-dystroglycan in the extracellular space. As such, ...
... agrin. With the aid of agrin-knockout mice, he and his co-workers showed a particular form of agrin was required for formation ...
Agrin binds to a muscle-specific kinase (MuSK) receptor in the post-synaptic membrane, and this in turn leads to downstream ... The axon of the motoneuron releases agrin, a proteoglycan that initiates a cascade that eventually leads to AChR association. ... In motor neurons, Wnt-3 works with Agrin to promote growth cone enlargement, axon branching and synaptic vesicle clustering. ... AChR experiences multimerization within the post-synaptic membrane largely due to the signaling molecule Agrin. ...
Agrin, a protein linked to heparan sulfate basement membrane nephrin Renal corpuscle (glomerulus) showing glomular basement ...
The protein agrin, which concentrates acetylcholine receptors during human embryonic development, was first isolated from this ...
Rapsyn interacts directly with the AChRs and plays a vital role in agrin-induced clustering of the AChR. Without rapsyn, ... This pathway consists of agrin, muscle-specific tyrosine kinase (MuSK), acetylcholine receptors (AChRs) and the AChR-clustering ...
The encoded proteins are structurally similar to laminin, slit, and agrin, other proteins involved in axon guidance and ...
Lupa, MT; Caldwell, JH (Nov 1991). "Effect of Agrin on the Distribution of Acetylcholine Receptors and Sodium Channels on Adult ...
The C-terminal domain contains multiple extracellular SEA (sea urchin sperm protein, enterokinase, and agrin) modules, a ... enterokinase and agrin) module in cleavage of membrane-tethered mucins". The FEBS Journal. 272 (11): 2901-11. doi:10.1111/j. ...
... integrin beta-1D and agrin were significantly reduced nearly to undetectable levels; and this corresponded with lower mRNA ...
However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. ... However, kazal-like domains are also seen in the extracellular part of agrins, which are not known to be protease inhibitors. ... Human proteins with Kazal 1 domains: AGRIN, CPAMD8 FST, FSTL3, FSTL4, FSTL5 IGFBPL1 SMOC1, SPARC, SPARCL1, SPINK1, SPINK2, ... Kazal-like domains are also seen in the extracellular part of agrins which are not known to be proteinase inhibitors. ...
Agrin is the largest producer and processor of diverse varieties of herbs, spices and seeds in Morocco. A leader in the local ...
Lorem ipsum dolor sit amet, consectetur adipiscing elit. Morbi vitae dui et nunc ornare vulputate non fringilla massa. Praesent sit amet erat sapien, auctor consectetur ligula. Lorem ipsum dolor sit amet, consectetur adipiscing elit. Sed non ligula augue. Praesent imperdiet magna at risus lobortis ac accumsan lorem ornare. In aliquam, sapien ac vehicula vestibulum, arcu magna aliquet velit,. ...
Synapse-forming axons and recombinant agrin induce microprocess formation on myotubes. Chang Sub Uhm, Birgit Neuhuber, Brian ... Dive into the research topics of Synapse-forming axons and recombinant agrin induce microprocess formation on myotubes. ...
EDITORIAL OFFICE OF AGRIN. Faculty of Agriculture, Jenderal Soedirman University. Jln. Dr. Soeparno Karangwangkal. Purwokerto ... AGRIN (ISSN: 1410-0029, 2549-6786 (online)) is published by Faculty of Agriculture, Jenderal Soedirman University under ...
Expression of mutant agrins in cultured cells demonstrated accumulation of agrin in the endoplasmic reticulum associated with ... mutant agrins retained a normal capacity to trigger the formation of AChR clusters. To confirm agrin accumulation and secretion ... Moreover, co-cultures of patient iPS-derived motoneurons with myotubes confirmed the deficit in agrin secretion and revealed a ... Altogether, we report the first mutations in AGRN gene that specifically affect agrin secretion by motoneurons. Interestingly, ...
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Agrin in the Muscularis Mucosa Serves as a Biomarker Distinguishing Hyperplastic Polyps from Sessile Serrated Lesions. Hynes RO ... Agrin in the Muscularis Mucosa Serves as a Biomarker Distinguishing Hyperplastic Polyps from Sessile Serrated Lesions. Hynes RO ... Immunohistochemical staining of the MM for agrin represents a novel biomarker that assists in diagnosis of morphologically ... patterns of extracellular matrix proteins to identify markers distinguishing SSLs from other polyps and identified agrin in the ...
Agrin / metabolism Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Agrin / chemistry Actions. * Search in PubMed * Search in MeSH * Add to Search ...
Suppression of agrin-22 production and synaptic dysfunction in Cln1−/− mice. Ann Clin Transl Neurol 2015; 2(12):1085-104. ...
Agrin is a heparan sulfate proteoglycan.. Tsen G; Halfter W; Kröger S; Cole GJ. J Biol Chem; 1995 Feb; 270(7):3392-9. PubMed ID ...
for Engineering, Confortchem Inc., RKW, KAPCI, Eagle Polymers, Polymed Distribution Fze, Agrin Serve Co., KIRIAZI ...
Acetylcholine (ACh) and agrin are two opposing signals that regulate ACh receptor (AChR) clustering during neuromuscular ... ACh induces dispersion of AChR clusters that are not stabilized by agrin via a cyclin-dependent kinase 5 (Cdk5)-mediated ... Although the nerve-derived protein agrin has been suggested to be a positive signal, the negative signals remain elusive. Here ... In contrast, the subsequent stages of synaptic growth and maintenance require nerve-derived agrin, and a second nerve-derived ...
Agrin and LRP4 antibodies as new biomarkers of myasthenia gravis. Ann N Y Acad Sci. 2018;1413:126-35. DOIPubMedGoogle Scholar ...
Expression of agrin, dystroglycan, and utrophin in normal renal tissue and in experimental glomerulopathies. Am J Pathol. 2000; ...
Nate Agrin, Patrick Lok, Raghavendra Prabu, Sarah Brown, Sam Luckenbill, Stephen Fedele, Tian Wang, Yi Zhuang, Zhenghua Li. ...
agrin proteoglycan. Description. From NCBI Gene: This gene encodes one of several proteins that are critical in the development ...
The editor of the weekly Agrin Rozh, he was arrested after criticizing a wave of arrests in the province, where at least 80 ...
use AGRIN (NM) to search AGRIN 1988-93. History Note. 94; was AGRIN (NM) 1988-93. Date Established. 1994/01/01. Date of Entry. ... Agrin Preferred Term Term UI T054397. Date01/01/1999. LexicalTag NON. ThesaurusID NLM (1994). ... Agrin Preferred Concept UI. M0027395. Registry Number. 0. Scope Note. A protein component of the synaptic basal lamina. It has ... 94; AGRIN was indexed under NERVE TISSUE PROTEINS 1988-93. Online Note. ...
My sister came from Seattle to visit for a week. No one mentioned the whole May Gray thing that apparently happens here in May. May Gray is another way of saying, Your Sister Wont Get a Tan While She Visits. As soon as she left, the sun began to shine as if in apology or…
NCAM-1 specifically binds to heparan sulfate proteoglycans (1), the extracellular matrix protein agrin (2), and several ...
Mathew Daniels, from 1998-2003 where her research focused on the role of agrin in growth cone guidance. ...
In addition, new studies on synaptogenesis implicate the unique roles of organizing molecules, such as nARIA, agrin, gephyrin, ...
... such as agrin for AChRs, ephrins for N-methyl-D-aspartate (NMDA)-type GluRs, and neuronal activity-regulated pentraxin for AMPA ...
Modulation of agrin and RhoA pathways ameliorates movement defects and synapse morphology in MYO9A-depleted zebrafish ...
C-Terminal Agrin Fragment (CAF) Reflects Renal Function in Patients Suffering from Severe Sepsis or Septic Shock ...
OConnor, E et al (2018) MYO9A deficiency in motor neurons is associated with reduced neuromuscular agrin secretion. Hum Mol ...
  • On this basis we defined and consequently confirmed novel biomarker candidates such as the extreme C-terminus of the extracellular matrix protein agrin within the set of cancer-enriched immunorectivities. (biomedcentral.com)
  • NCAM-1 specifically binds to heparan sulfate proteoglycans (1), the extracellular matrix protein agrin (2), and several chondroitin sulfate proteoglycans that include neurocan and phosphocan (3). (rndsystems.com)
  • Genes encoding agrin (AGRN) and neurotrypsin (PRSS12) are associated with muscle mass, strength and plasma C-terminal agrin fragment concentration. (nih.gov)
  • Among them, AGRN encodes agrin , an essential synaptic protein secreted by motoneurons . (bvsalud.org)
  • Altogether, we report the first mutations in AGRN gene that specifically affect agrin secretion by motoneurons . (bvsalud.org)
  • See the reference protein sequence for agrin isoform 1 precursor (NP_001292204.1). (nih.gov)
  • In addition, new studies on synaptogenesis implicate the unique roles of organizing molecules, such as nARIA, agrin, gephyrin, PSD95, GRIP and other proteins with PDZ domains that act to recruit and assemble the synaptic apparatus at appropriate sites. (nih.gov)
  • Finally, we have looked for agrin-binding proteins in muscle that might mediate the action of agrin in muscle cells. (nih.gov)
  • Our results and those from several other labs show that the major agrin-binding protein in muscle cells is alpha -dystroglycan, an extracellular matrix protein previously identified as part of a complex of proteins associated with dystrophin. (nih.gov)
  • We show that the cell surface-binding LG domains of non-neural (muscle) agrin and perlecan promote AChR clustering in the presence of laminin-2. (unibas.ch)
  • Furthermore, AChR clustering can be mimicked with antibody binding to non-neural agrin, supporting a mechanism of ligand aggregation. (unibas.ch)
  • Neural agrin, in addition to its unique ability to cluster AChRs through its B/z sequence insert, also exhibits laminin-dependent AChR clustering, the latter enhancing and stabilizing its activity. (unibas.ch)
  • These findings provide evidence for cooperative and partially redundant MuSK-dependent functions of basement membrane in AChR assembly that can enhance neural agrin activity yet operate in its absence. (unibas.ch)
  • Such interactions may contribute to the assembly of aneural AChR clusters that precede neural agrin release as well as affect later NMJ development. (unibas.ch)
  • Interestingly, evaluation of the specific activity of individual agrins on AChR cluster formation indicated that when secreted, mutant agrins retained a normal capacity to trigger the formation of AChR clusters. (bvsalud.org)
  • Our recent work has focused on two areas: the mechanisms of assembly of the acetylcholine receptor (AChR) and the role in synaptogenesis of agrin, a neurally-secreted protein that causes AChRs to cluster. (nih.gov)
  • How agrin causes AChR clustering is unknown. (nih.gov)
  • We are currently investigating whether the interaction of agrin with alpha -dystroglycan is responsible for the formation of AChR clusters, or whether it plays some other role. (nih.gov)
  • It also requires conjugation of the agrin or perlecan to laminin together with laminin polymerization. (unibas.ch)
  • The molecules are named for their protein cores and come in five classes, comprising membrane-bound syndecans and glypicans, as well as secreted agrin, perlecan, and type XVIII collagen. (alzforum.org)
  • The collagen ColQ binds to LRP4 and regulates the activation of the Muscle-Specific Kinase-LRP4 receptor complex by agrin at the neuromuscular junction. (nih.gov)
  • Recent studies have revealed antibodies against agrin and its receptor LRP4-both critical for neuromuscular junction formation and maintenance-in MG patients from various populations. (nih.gov)
  • Suppression of agrin-22 production and synaptic dysfunction in Cln1−/− mice. (nih.gov)
  • Moreover, co-cultures of patient iPS-derived motoneurons with myotubes confirmed the deficit in agrin secretion and revealed a reduction in motoneuron survival . (bvsalud.org)
  • Patient iPS-derived motoneurons accumulated mutant agrin in the soma and increased XBP1 mRNA splicing, suggesting UPR activation. (bvsalud.org)
  • First, In collaboration with the laboratory of Richard Scheller of Stanford University, we have examined the ability of the various forms of agrin to cluster the AChRs of cultured muscle cells. (nih.gov)
  • Expression of mutant agrins in cultured cells demonstrated accumulation of agrin in the endoplasmic reticulum associated with induction of unfolded protein response (UPR) and impaired secretion in the culture medium. (bvsalud.org)
  • The clustering occurs, at least in part, in response to a protein, agrin, that is released from motor nerve terminals. (nih.gov)
  • Second, we found that a variant of the C2 muscle cell line that is defective in the synthesis of proteoglycans is much less sensitive to agrin than is the parental line, suggesting that proteoglycans are involved in the action of agrin. (nih.gov)
  • Agrin, another component of the basal lamina, could compensate for the absence of laminin-alpha2 and restore basal lamina integrity, but normal expression of agrin is too low to correct for the lack of laminin-alpha2. (nih.gov)
  • Neurons and muscle cells express different forms of agrin, which are generated by alternative RNA splicing. (nih.gov)
  • We have investigated the action of agrin on cultured muscle cells in several ways. (nih.gov)
  • Other forms of agrin, found in muscle and other tissues, are significantly less active. (nih.gov)
  • We have identified severe CMS patients with uncharacterized p.R1671Q, p.R1698P and p.L1664P mutations in the LG2 domain of agrin . (bvsalud.org)