Emopamil binding protein
In this article, we will explore the fascinating world of Emopamil binding protein. From its origin to its impact on today's society, we will delve into its many facets and discover its influence in different areas. Emopamil binding protein has been the subject of study and debate throughout history, awakening the interest of specialists and amateurs alike. Along these lines, we will examine its origins, evolution and its relevance in the current context, offering a complete and detailed vision of Emopamil binding protein. Likewise, we will analyze its impact in different areas, highlighting its role in culture, technology, politics and much more. Get ready to embark on a fascinating journey through Emopamil binding protein!
Emopamil binding protein is a protein that in humans is encoded by the EBP gene, located on the X chromosome.[5] The protein is shown to have a high-affinity reception for anti-ischemic drugs, such as Emopamil, resulting in its discovery and given name. EBP has a mass of 27.3 kDa and resembles the σ2-receptor that resides in the endoplasmic reticulum of various tissues as an integral membrane protein.[6]
Clinical significance
Mutations in EBP cause Conradi–Hünermann syndrome and impairs cholesterol biosynthesis.[7] Unborn males affected with EBP mutations are not expected to be liveborn, (with up to only 5% male births). Individuals, mostly female, that are liveborn with EBP mutations experience stunted growth, limb reduction and back problems. Later in life, the individual may develop cataracts along with coarse hair and hair loss.[8]
Research areas
Remyelination and MS
The inhibition of EBP promotes oligodendrocyte formation, which may help remyelination and thus limit multiple sclerosis development. [9]
Cloning
Isolation, replication and characterization of the EBP and EBP-like protein have been performed in yeast/E. Coli strains (which lack the EBP protein in nature) to study the high-affinity drug binding effects.[6]
See also
References
- ^ a b c GRCh38: Ensembl release 89: ENSG00000147155 – Ensembl, May 2017
- ^ a b c GRCm38: Ensembl release 89: ENSMUSG00000031168 – Ensembl, May 2017
- ^ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
- ^ Guggenberger C, Ilgen D, Adamski J (May 2007). "Functional analysis of cholesterol biosynthesis by RNA interference". The Journal of Steroid Biochemistry and Molecular Biology. 104 (3–5): 105–109. doi:10.1016/j.jsbmb.2007.03.001. PMID 17498944. S2CID 20838858.
- ^ a b Hanner M, Moebius FF, Weber F, Grabner M, Striessnig J, Glossmann H (March 1995). "Phenylalkylamine Ca2+ antagonist binding protein. Molecular cloning, tissue distribution, and heterologous expression". The Journal of Biological Chemistry. 270 (13): 7551–7557. doi:10.1074/jbc.270.13.7551. PMID 7706302.
- ^ Barboza-Cerda MC, Wong LJ, Martínez-de-Villarreal LE, Zhang VW, Déctor MA (July 2014). "A novel EBP c.224T>A mutation supports the existence of a male-specific disorder independent of CDPX2". American Journal of Medical Genetics. Part A. 164A (7): 1642–1647. doi:10.1002/ajmg.a.36508. PMID 24700572. S2CID 6501291.
- ^ Krakow D (2018). "Chondrodysplasia Punctata". In Copel JA, D'Alton ME, Reapply WC, Feltovich H, Gratacós E, Krakow D, Odibo AO, Platt LD, Tutschek B (eds.). Obstetric Imaging: Fetal Diagnosis and Care (2nd ed.). Elsevier. pp. 259–261. doi:10.1016/b978-0-323-44548-1.00048-6. ISBN 978-0-323-44548-1.
- ^ Dorel R, Sun D, Carruthers N, Castanedo GM, Ung PM, Factor DC, et al. (March 2024). "Discovery and Optimization of Selective Brain-Penetrant EBP Inhibitors that Enhance Oligodendrocyte Formation". Journal of Medicinal Chemistry. 67 (6): 4819–4832. doi:10.1021/acs.jmedchem.3c02396. PMID 38470227.
External links
- GeneReviews/NCBI/NIH/UW entry on Chondrodysplasia Punctata 2, X-Linked, Conradi-Hünermann Syndrome, Happle Syndrome
- EBP+protein,+human at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
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