SEMA3A

From Wikipedia, the free encyclopedia

Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3A

PDB rendering based on 1q47.

Available structures: 1q47

Identifiers

Symbol(s)

SEMA3A; SEMAL; Hsema-I; Hsema-III; MGC133243; SEMA1; SEMAD; SEMAIII; SemD; coll-1; sema III

External IDs

OMIM: 603961 MGI: 107558 HomoloGene: 31358

Gene ontology
Cellular Component:	• extracellular region
Biological Process:	• multicellular organismal development • nervous system development • axon guidance • cell differentiation • negative regulation of axon extension

RNA expression pattern

More reference expression data

Orthologs

Human

Mouse

Refseq

NM_006080 (mRNA)
NP_006071 (protein)

NM_009152 (mRNA)
NP_033178 (protein)

Location

Chr 7: 83.43 - 83.66 Mb

Chr 5: 13.4 - 13.61 Mb

Pubmed search

[1]

[2]

Sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3A, also known as SEMA3A, is a human gene.^[1]

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.^[1]

[edit] References

^ ^a ^b Entrez Gene: SEMA3A sema domain, immunoglobulin domain (Ig), short basic domain, secreted, (semaphorin) 3A.

[edit] Further reading

Schmidt EF, Strittmatter SM (2007). "The CRMP family of proteins and their role in Sema3A signaling.". Adv. Exp. Med. Biol. 600: 1–11. PMID 17607942.
Püschel AW, Adams RH, Betz H (1995). "Murine semaphorin D/collapsin is a member of a diverse gene family and creates domains inhibitory for axonal extension.". Neuron 14 (5): 941–8. PMID 7748561.
Kolodkin AL, Matthes DJ, Goodman CS (1994). "The semaphorin genes encode a family of transmembrane and secreted growth cone guidance molecules.". Cell 75 (7): 1389–99. PMID 8269517.
Bonaldo MF, Lennon G, Soares MB (1997). "Normalization and subtraction: two approaches to facilitate gene discovery.". Genome Res. 6 (9): 791–806. PMID 8889548.
Chen H, Chédotal A, He Z, et al. (1997). "Neuropilin-2, a novel member of the neuropilin family, is a high affinity receptor for the semaphorins Sema E and Sema IV but not Sema III.". Neuron 19 (3): 547–59. PMID 9331348.
Takahashi T, Nakamura F, Jin Z, et al. (1999). "Semaphorins A and E act as antagonists of neuropilin-1 and agonists of neuropilin-2 receptors.". Nat. Neurosci. 1 (6): 487–93. doi:10.1038/2203. PMID 10196546.
Takahashi T, Fournier A, Nakamura F, et al. (1999). "Plexin-neuropilin-1 complexes form functional semaphorin-3A receptors.". Cell 99 (1): 59–69. PMID 10520994.
Castellani V, De Angelis E, Kenwrick S, Rougon G (2003). "Cis and trans interactions of L1 with neuropilin-1 control axonal responses to semaphorin 3A.". EMBO J. 21 (23): 6348–57. PMID 12456642.
Eastwood SL, Law AJ, Everall IP, Harrison PJ (2003). "The axonal chemorepellant semaphorin 3A is increased in the cerebellum in schizophrenia and may contribute to its synaptic pathology.". Mol. Psychiatry 8 (2): 148–55. doi:10.1038/sj.mp.4001233. PMID 12610647.
Scherer SW, Cheung J, MacDonald JR, et al. (2003). "Human chromosome 7: DNA sequence and biology.". Science 300 (5620): 767–72. doi:10.1126/science.1083423. PMID 12690205.
Rieger J, Wick W, Weller M (2003). "Human malignant glioma cells express semaphorins and their receptors, neuropilins and plexins.". Glia 42 (4): 379–89. doi:10.1002/glia.10210. PMID 12730958.
Hillier LW, Fulton RS, Fulton LA, et al. (2003). "The DNA sequence of human chromosome 7.". Nature 424 (6945): 157–64. doi:10.1038/nature01782. PMID 12853948.
Serini G, Valdembri D, Zanivan S, et al. (2003). "Class 3 semaphorins control vascular morphogenesis by inhibiting integrin function.". Nature 424 (6947): 391–7. doi:10.1038/nature01784. PMID 12879061.
Bachelder RE, Lipscomb EA, Lin X, et al. (2003). "Competing autocrine pathways involving alternative neuropilin-1 ligands regulate chemotaxis of carcinoma cells.". Cancer Res. 63 (17): 5230–3. PMID 14500350.
Catalano A, Caprari P, Rodilossi S, et al. (2004). "Cross-talk between vascular endothelial growth factor and semaphorin-3A pathway in the regulation of normal and malignant mesothelial cell proliferation.". FASEB J. 18 (2): 358–60. doi:10.1096/fj.03-0513fje. PMID 14656993.
Bagnard D, Sainturet N, Meyronet D, et al. (2004). "Differential MAP kinases activation during semaphorin3A-induced repulsion or apoptosis of neural progenitor cells.". Mol. Cell. Neurosci. 25 (4): 722–31. doi:10.1016/j.mcn.2003.12.007. PMID 15080899.
Good PF, Alapat D, Hsu A, et al. (2005). "A role for semaphorin 3A signaling in the degeneration of hippocampal neurons during Alzheimer's disease.". J. Neurochem. 91 (3): 716–36. doi:10.1111/j.1471-4159.2004.02766.x. PMID 15485501.
Marzioni D, Tamagnone L, Capparuccia L, et al. (2005). "Restricted innervation of uterus and placenta during pregnancy: evidence for a role of the repelling signal Semaphorin 3A.". Dev. Dyn. 231 (4): 839–48. doi:10.1002/dvdy.20178. PMID 15517571.
Gu C, Yoshida Y, Livet J, et al. (2005). "Semaphorin 3E and plexin-D1 control vascular pattern independently of neuropilins.". Science 307 (5707): 265–8. doi:10.1126/science.1105416. PMID 15550623.
Kashiwagi H, Shiraga M, Kato H, et al. (2005). "Negative regulation of platelet function by a secreted cell repulsive protein, semaphorin 3A.". Blood 106 (3): 913–21. doi:10.1182/blood-2004-10-4092. PMID 15831706.