MAL (gene)
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Myelin and lymphocyte protein is a protein that in humans is encoded by the MAL gene.[1]
The protein encoded by this gene is a highly hydrophobic integral membrane protein belonging to the MAL family of proteolipids. The protein has been localized to the endoplasmic reticulum of T-cells and is a candidate linker protein in T-cell signal transduction. In addition, this proteolipid is localized in compact myelin of cells in the nervous system and has been implicated in myelin biogenesis and/or function. The protein plays a role in the formation, stabilization and maintenance of glycosphingolipid-enriched membrane microdomains. Alternative splicing produces four transcript variants which vary from each other by the presence or absence of alternatively spliced exons 2 and 3.[1]
[edit] References
[edit] Further reading
- Frank M (2000). "MAL, a proteolipid in glycosphingolipid enriched domains: functional implications in myelin and beyond". Prog. Neurobiol. 60 (6): 531–44. doi:10.1016/S0301-0082(99)00039-8. PMID 10739088.
- Alonso MA, Barton DE, Francke U (1988). "Assignment of the T-cell differentiation gene MAL to human chromosome 2, region cen----q13". Immunogenetics 27 (2): 91–5. doi:10.1007/BF00351081. PMID 3257199.
- Alonso MA, Weissman SM (1987). "cDNA cloning and sequence of MAL, a hydrophobic protein associated with human T-cell differentiation". Proc. Natl. Acad. Sci. U.S.A. 84 (7): 1997–2001. doi:10.1073/pnas.84.7.1997. PMC 304570. PMID 3494249. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=304570.
- Rancaño C, Rubio T, Alonso MA (1994). "Alternative splicing of human T-cell-specific MAL mRNA and its correlation with the exon/intron organization of the gene". Genomics 21 (2): 447–50. doi:10.1006/geno.1994.1294. PMID 8088843.
- Rancaño C, Rubio T, Correas I, Alonso MA (1994). "Genomic structure and subcellular localization of MAL, a human T-cell-specific proteolipid protein". J. Biol. Chem. 269 (11): 8159–64. PMID 8132541.
- Millán J, Puertollano R, Fan L et al (1997). "The MAL proteolipid is a component of the detergent-insoluble membrane subdomains of human T-lymphocytes". Biochem. J. 321 (1): 247–52. PMC 1218061. PMID 9003426. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=1218061.
- Millán J, Puertollano R, Fan L, Alonso MA (1997). "Caveolin and MAL, two protein components of internal detergent-insoluble membranes, are in distinct lipid microenvironments in MDCK cells". Biochem. Biophys. Res. Commun. 233 (3): 707–12. doi:10.1006/bbrc.1997.6530. PMID 9168919.
- Martín-Belmonte F, Kremer L, Albar JP et al (1998). "Expression of the MAL gene in the thyroid: the MAL proteolipid, a component of glycolipid-enriched membranes, is apically distributed in thyroid follicles". Endocrinology 139 (4): 2077–84. doi:10.1210/en.139.4.2077. PMID 9528996.
- Köhler C, Håkansson A, Svanborg C et al (1999). "Protease activation in apoptosis induced by MAL". Exp. Cell Res. 249 (2): 260–8. doi:10.1006/excr.1999.4472. PMID 10366425.
- Frank M, Schaeren-Wiemers N, Schneider R, Schwab ME (1999). "Developmental expression pattern of the myelin proteolipid MAL indicates different functions of MAL for immature Schwann cells and in a late step of CNS myelinogenesis". J. Neurochem. 73 (2): 587–97. doi:10.1046/j.1471-4159.1999.0730587.x. PMID 10428054.
- Puertollano R, Alonso MA (1999). "MAL, an integral element of the apical sorting machinery, is an itinerant protein that cycles between the trans-Golgi network and the plasma membrane". Mol. Biol. Cell 10 (10): 3435–47. PMC 25613. PMID 10512878. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=25613.
- Erne B, Sansano S, Frank M, Schaeren-Wiemers N (2002). "Rafts in adult peripheral nerve myelin contain major structural myelin proteins and myelin and lymphocyte protein (MAL) and CD59 as specific markers". J. Neurochem. 82 (3): 550–62. doi:10.1046/j.1471-4159.2002.00987.x. PMID 12153479.
- Copie-Bergman C, Plonquet A, Alonso MA et al (2003). "MAL expression in lymphoid cells: further evidence for MAL as a distinct molecular marker of primary mediastinal large B-cell lymphomas". Mod. Pathol. 15 (11): 1172–80. doi:10.1097/01.MP.0000032534.81894.B3. PMID 12429796.
- Strausberg RL, Feingold EA, Grouse LH et al (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=139241.
- Kazemi-Noureini S, Colonna-Romano S, Ziaee AA et al (2004). "Differential gene expression between squamous cell carcinoma of esophageus and its normal epithelium; altered pattern of mal, akr1c2, and rab11a expression". World J. Gastroenterol. 10 (12): 1716–21. PMID 15188492.
- Llorente A, de Marco MC, Alonso MA (2005). "Caveolin-1 and MAL are located on prostasomes secreted by the prostate cancer PC-3 cell line". J. Cell. Sci. 117 (Pt 22): 5343–51. doi:10.1242/jcs.01420. PMID 15466889.
- Gerhard DS, Wagner L, Feingold EA et al (2004). "The status, quality, and expansion of the NIH full-length cDNA project: the Mammalian Gene Collection (MGC)". Genome Res. 14 (10B): 2121–7. doi:10.1101/gr.2596504. PMC 528928. PMID 15489334. http://www.pubmedcentral.nih.gov/articlerender.fcgi?tool=pmcentrez&artid=528928.
- Dukhovny A, Goldstein Magal L, Hirschberg K (2006). "The MAL proteolipid restricts detergent-mediated membrane pore expansion and percolation". Mol. Membr. Biol. 23 (3): 245–57. doi:10.1080/09687860600601445. PMID 16785208.
- Mimori K, Nishida K, Nakamura Y et al (2007). "Loss of MAL expression in precancerous lesions of the esophagus". Ann. Surg. Oncol. 14 (5): 1670–7. doi:10.1245/s10434-006-9064-2. PMID 17151798.
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