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Sema domain, immunoglobulin domain

Semaphorin-3A, Sema3A, semaphorin III
This gene is a member of the semaphorin family and encodes a protein with an Ig-like C2-type (immunoglobulin-like) domain, a PSI domain and a Sema domain. This secreted protein can function as either a chemorepulsive agent, inhibiting axonal outgrowth, or as a chemoattractive agent, stimulating the growth of apical dendrites. In both cases, the protein is vital for normal neuronal pattern development. Increased expression of this protein is associated with schizophrenia and is seen in a variety of human tumor cell lines. Also, aberrant release of this protein is associated with the progression of Alzheimer's disease. [provided by RefSeq, Jul 2008] (from NCBI)
Top mentioned proteins: Neuropilin-1, CAN, vascular endothelial growth factor, V1a, Actin
Papers using Semaphorin-3A antibodies
Extracellular stimuli specifically regulate localized levels of individual neuronal mRNAs
Twiss Jeffery L. et al., In The Journal of Cell Biology, 2004
... NGF (Harlan), BDNF, NT3 (Alomone Labs), MAG-Fc (R&D Systems), and Sema3A-AP (Nakajima et al., 2006) were covalently coupled to 15-μm-diameter polystyrene microparticles according to the manufacturer's instructions (Polysciences).
Papers on Semaphorin-3A
Axon guidance molecule Semaphorin3A is a novel tumor suppressor in head and neck squamous cell carcinoma.
Song et al., Nanjing, China. In Oncotarget, Feb 2016
UNASSIGNED: Semaphorin3A (SEMA3A), an axon guidance molecule in the nervous system, plays an inhibitory role in oncogenesis.
Semaphorin 3A attenuates cardiac autonomic disorders and reduces inducible ventricular arrhythmias in rats with experimental myocardial infarction.
Yan et al., Jinan, China. In Bmc Cardiovasc Disord, Dec 2015
BACKGROUND: To investigate the effects of semaphorin 3A (sema 3A) on cardiac autonomic regulation and subsequent ventricular arrhythmias (VAs) in post-infarcted hearts.
MEIS3 is repressed in A549 lung epithelial cells by deoxynivalenol and the repression contributes to the deleterious effect.
Kamei et al., Obihiro, Japan. In J Toxicol Sci, Dec 2015
The repression of B3GALT4, MEIS3, AK7, SEMA3A, KCNMB4, and SCARA5 was confirmed by quantitative PCR.
Voltage-gated calcium and sodium channels mediate Sema3A retrograde signaling that regulates dendritic development.
Goshima et al., Yokohama, Japan. In Brain Res, Dec 2015
Semaphorin3A (Sema3A), a secreted repulsive axon guidance molecule, regulates synapse maturation and dendritic branching.
Retrograde signaling for climbing fiber synapse elimination.
Kano et al., Tokyo, Japan. In Cerebellum, Feb 2015
Here, we show that semaphorin3A (Sema3A) and semaphorin7A (Sema7A) mediate retrograde signals for elimination of redundant climbing fiber (CF) to Purkinje cell (PC) synapses in the developing cerebellum, a representative model of synapse elimination in the central nervous system.
Potential Role of Semaphorin 3A and Its Receptors in Regulating Aberrant Sympathetic Innervation in Peritoneal and Deep Infiltrating Endometriosis.
Yao et al., Guangzhou, China. In Plos One, 2014
Previous studies have demonstrated the involvement of nerve repellent factors in regulation of the imbalanced innervation of endometriosis.
The Role Of Semaphorin 3A In The Skeletal System.
Zhang et al., Beijing, China. In Crit Rev Eukaryot Gene Expr, 2014
Semaphorin 3A (Sema3A), characterized by a conserved N-terminal "Sema" domain, was originally described as an axon guidance molecule.
The extracellular matrix in plasticity and regeneration after CNS injury and neurodegenerative disease.
Fawcett, Cambridge, United Kingdom. In Prog Brain Res, 2014
A disulfated CS-E motif in these chains is responsible for binding of Semaphorin 3A to PNNs where it affects ocular dominance plasticity and probably other forms of plasticity.
Neuropilin regulation of angiogenesis.
Ruhrberg et al., London, United Kingdom. In Biochem Soc Trans, 2014
NRP1 also acts as a receptor for the class 3 semaphorin (SEMA3A) to regulate vessel maturation during tumour angiogenesis and vascular permeability in eye disease.
Neuropilin-1 (NRP-1) and Magnetic Nanoparticles, a Potential Combination for Diagnosis and Therapy of Gliomas.
Khan et al., Nanjing, China. In Curr Pharm Des, 2014
The role of NRP-1 in gliomas was explored in details, including relationships of NRP-1 expression and glioma prognosis, Sema3A-NRP-1 signaling in gliomas, NRP-1 signaling and VEGF/VEGFR、PlGF、TGF-β、PDGF、LD22-4 of FGF2、autocrine of HGF/SF、p130Cas tyrosine phosphorylation and integrin-associated tumor microenvironment in gliomas, NRP-1 intracellular trafficking, NRP-1 and glioma stem-like cells, as well as magnetic nanoparticles related to targeting gliomas.
Retrograde semaphorin signaling regulates synapse elimination in the developing mouse brain.
Kano et al., Tokyo, Japan. In Science, 2014
Knockdown of Sema3A, a secreted semaphorin, in Purkinje cells or its receptor in climbing fibers accelerated synapse elimination during postnatal day 8 (P8) to P18.
Astrocyte-encoded positional cues maintain sensorimotor circuit integrity.
Rowitch et al., San Francisco, United States. In Nature, 2014
Here we show that postnatal spinal cord astrocytes express several region-specific genes, and that ventral astrocyte-encoded semaphorin 3a (Sema3a) is required for proper motor neuron and sensory neuron circuit organization.
Impeding macrophage entry into hypoxic tumor areas by Sema3A/Nrp1 signaling blockade inhibits angiogenesis and restores antitumor immunity.
Mazzone et al., Leuven, Belgium. In Cancer Cell, 2014
Here, we report that hypoxia-induced Semaphorin 3A (Sema3A) acts as an attractant for TAMs by triggering vascular endothelial growth factor receptor 1 phosphorylation through the associated holoreceptor, composed of Neuropilin-1 (Nrp1) and PlexinA1/PlexinA4.
Location, location, location: macrophage positioning within tumors determines pro- or antitumor activity.
Bergers et al., San Francisco, United States. In Cancer Cell, 2014
In this issue of Cancer Cell, Casazza and colleagues report that tumor-associated macrophage (TAM) entry into avascular tumor areas is regulated by Semaphorin 3A/Neuropilin-1 signaling; interference with this pathway entraps TAMs in oxygenated areas, preventing their tumorigenic function.
Neuron-derived semaphorin 3A is an early inducer of vascular permeability in diabetic retinopathy via neuropilin-1.
Sapieha et al., Montréal, Canada. In Cell Metab, 2013
We provide evidence from both human and animal studies for the critical role of the classical neuronal guidance cue, semaphorin 3A, in instigating pathological vascular permeability in diabetic retinas via its cognate receptor neuropilin-1.
Semaphorin3A, Neuropilin-1, and PlexinA1 are required for lymphatic valve formation.
Eichmann et al., Paris, France. In Circ Res, 2012
Data demonstrate an essential direct function of Sema3A-Nrp1-PlexinA1 signaling in lymphatic valve formation.
An unexpected role of semaphorin3a-neuropilin-1 signaling in lymphatic vessel maturation and valve formation.
Detmar et al., Zürich, Switzerland. In Circ Res, 2012
Sema3A-Nrp-1 signaling directs the maturation of the lymphatic vascular network likely via regulating the perivascular cell coverage of the vessels thus affecting lymphatic vessel function and lymphatic valve development.
SEMA3A, a gene involved in axonal pathfinding, is mutated in patients with Kallmann syndrome.
Dodé et al., Saint-Pierre-des-Corps, France. In Plos Genet, 2012
Findings indicate that semaphorin-3A signaling insufficiency contributes to the pathogenesis of Kallmann syndrome. Nonsynonymous mutations in SEMA3A were found in 24 patients, all in heterozygous state .
Calpain cleaves and activates the TRPC5 channel to participate in semaphorin 3A-induced neuronal growth cone collapse.
Clapham et al., Boston, United States. In Proc Natl Acad Sci U S A, 2012
Semaphorin 3A initiates growth cone collapse via activation of calpain that in turn potentiates TRPC5 activity.
Osteoprotection by semaphorin 3A.
Takayanagi et al., Tokyo, Japan. In Nature, 2012
semaphorin 3A (Sema3A) exerts an osteoprotective effect by both suppressing osteoclastic bone resorption and increasing osteoblastic bone formation
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