Semaphorin 7A, GPI membrane anchor (John Milton Hagen blood group) (SEMA7A) also known as CD108 (Cluster of Differentiation 108), is a human gene.[5]
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SEMA7A is a membrane-bound semaphorin that associates with cell surfaces via a glycosylphosphatidylinositol (GPI) linkage. SEMA7A is also known as the John-Milton-Hagen (JMH) blood group antigen, an 80-kD glycoprotein expressed on activated lymphocytes and erythrocytes.[supplied by OMIM][5] SEMA7A is expressed in various adult tissues such as adipose, colon, esophagus, heart, brain, spleen, testis, lung, ovary, and uterus.[6]
SEMA7A promotes axonal growth and is involved in mesoderm derived somite formation. Murine embryonic Sema7A expression is highest on day 7, which is indicative of its role on the differentiation of germ layer structure.[7] Embryonic Sema7A expression is noticeable at all developmental stages as well as in the newborn and adult thymus, indicative of a development T-cell role.[7] In wild type neurons, addition of Sema7A under in vitro conditions promotes elongation and branching in a dose dependent manner.[8] Unlike the majority of semaphorins, SEMA7A enhances axonal growth and is imperative for proper embryonic axonal tract formation.[9] Limited expression of SEMA7A is found in the hindbrain as opposed to an abundance of SEMA7A expression found in both the cranial and trunk neural crest cells, which indicates an involvement in migration and differentiation.[10] Sema7A -/- mice show defects in olfactory tract development.[11]
In normal breast tissue, mRNA expression of SEMA7A is low or not expressed, but activation to re-express SEMA7A occurs in these adult tissues to cause pleiotropic effects which increase tumorigenesis.[12][13] Tumor cell growth, EMT, lung metastasis and angiogenesis have been linked to increased Sema7a expression in murine models.[14][15][16] Increased SEMA7A expression correlates with poor prognosis in breast cancer patients.[13] Tumors increase SEMA7A expression in an involuting environment, but knockout of SEMA7a in mouse models undergoing involution decreases lymphangiogenesis.[17]
This protein is known to have eight variants in the extracellular region: seven lie within the Sema domain and one within the PSI domain.[citation needed]
This protein forms dimers.[citation needed]
This protein acts as a receptor for the malaria parasite Plasmodium falciparum.
- Xu X, Ng S, Wu ZL, Nguyen D, Homburger S, Seidel-Dugan C, et al. (August 1998). "Human semaphorin K1 is glycosylphosphatidylinositol-linked and defines a new subfamily of viral-related semaphorins". The Journal of Biological Chemistry. 273 (35): 22428–22434. doi:10.1074/jbc.273.35.22428. PMID 9712866.
- Lange C, Liehr T, Goen M, Gebhart E, Fleckenstein B, Ensser A (August 1998). "New eukaryotic semaphorins with close homology to semaphorins of DNA viruses". Genomics. 51 (3): 340–350. doi:10.1006/geno.1998.5256. PMID 9721204.
- Yamada A, Kubo K, Takeshita T, Harashima N, Kawano K, Mine T, et al. (April 1999). "Molecular cloning of a glycosylphosphatidylinositol-anchored molecule CDw108". Journal of Immunology. 162 (7): 4094–4100. doi:10.4049/jimmunol.162.7.4094. PMID 10201933.
- Angelisová P, Drbal K, Cerný J, Hilgert I, Horejsí V (June 1999). "Characterization of the human leukocyte GPI-anchored glycoprotein CDw108 and its relation to other similar molecules". Immunobiology. 200 (2): 234–245. doi:10.1016/s0171-2985(99)80073-4. PMID 10416131.
- Tamagnone L, Artigiani S, Chen H, He Z, Ming GI, Song H, et al. (October 1999). "Plexins are a large family of receptors for transmembrane, secreted, and GPI-anchored semaphorins in vertebrates". Cell. 99 (1): 71–80. doi:10.1016/S0092-8674(00)80063-X. PMID 10520995. S2CID 17386412.
- Mine T, Harada K, Matsumoto T, Yamana H, Shirouzu K, Itoh K, et al. (May 2000). "CDw108 expression during T-cell development". Tissue Antigens. 55 (5): 429–436. doi:10.1034/j.1399-0039.2000.550505.x. PMID 10885563.
- Holmes S, Downs AM, Fosberry A, Hayes PD, Michalovich D, Murdoch P, et al. (September 2002). "Sema7A is a potent monocyte stimulator". Scandinavian Journal of Immunology. 56 (3): 270–275. doi:10.1046/j.1365-3083.2002.01129.x. PMID 12193228. S2CID 26634136.
- Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–16903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
- Ota T, Suzuki Y, Nishikawa T, Otsuki T, Sugiyama T, Irie R, et al. (January 2004). "Complete sequencing and characterization of 21,243 full-length human cDNAs". Nature Genetics. 36 (1): 40–45. doi:10.1038/ng1285. PMID 14702039.
- Gerhard DS, Wagner L, Feingold EA, Shenmen CM, Grouse LH, Schuler G, et al. (October 2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Research. 14 (10B): 2121–2127. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334.
- Maurin JC, Delorme G, Machuca-Gayet I, Couble ML, Magloire H, Jurdic P, et al. (May 2005). "Odontoblast expression of semaphorin 7A during innervation of human dentin". Matrix Biology. 24 (3): 232–238. doi:10.1016/j.matbio.2005.03.005. PMID 15907379.
- Hu Y, Malone JP, Fagan AM, Townsend RR, Holtzman DM (December 2005). "Comparative proteomic analysis of intra- and interindividual variation in human cerebrospinal fluid". Molecular & Cellular Proteomics. 4 (12): 2000–2009. doi:10.1074/mcp.M500207-MCP200. PMID 16199891.
- Koh JM, Oh B, Lee JY, Lee JK, Kimm K, Kim GS, et al. (2006). "Association study of semaphorin 7a (sema7a) polymorphisms with bone mineral density and fracture risk in postmenopausal Korean women". Journal of Human Genetics. 51 (2): 112–117. doi:10.1007/s10038-005-0331-z. PMID 16372136.
This article incorporates text from the United States National Library of Medicine, which is in the public domain.