RDH16
Retinol dehydrogenase 16 (all-trans) is a protein that in humans is encoded by the RDH16 gene.[1] The gene is also known as RODH-4 and SDR9C8.[1]
Model organisms
| Characteristic | Phenotype |
|---|---|
| Homozygote viability | Normal |
| Fertility | Normal |
| Body weight | Normal |
| Anxiety | Normal |
| Neurological assessment | Normal |
| Grip strength | Normal |
| Hot plate | Normal |
| Dysmorphology | Normal |
| Indirect calorimetry | Normal |
| Glucose tolerance test | Normal |
| Auditory brainstem response | Normal |
| DEXA | Normal |
| Radiography | Normal |
| Body temperature | Normal |
| Eye morphology | Normal |
| Clinical chemistry | Normal |
| Plasma immunoglobulins | Normal |
| Haematology | Normal |
| Peripheral blood lymphocytes | Normal |
| Micronucleus test | Normal |
| Heart weight | Normal |
| Eye Histopathology | Normal |
| Salmonella infection | Normal[2] |
| Citrobacter infection | Normal[3] |
| All tests and analysis from[4][5] |
Model organisms have been used in the study of RDH16 function. A conditional knockout mouse line, called Rdh16tm1a(KOMP)Wtsi[6][7] was generated as part of the International Knockout Mouse Consortium program — a high-throughput mutagenesis project to generate and distribute animal models of disease to interested scientists — at the Wellcome Trust Sanger Institute.[8][9][10]
Male and female animals underwent a standardized phenotypic screen to determine the effects of deletion.[4][11] Twenty four tests were carried out on mutant mice, but no significant abnormalities were observed.[4]
References
- ^ a b "Retinol dehydrogenase 16 (all-trans)". Retrieved 2011-12-06.
- ^ "Salmonella infection data for Rdh16". Wellcome Trust Sanger Institute.
- ^ "Citrobacter infection data for Rdh16". Wellcome Trust Sanger Institute.
- ^ a b c Gerdin AK (2010). "The Sanger Mouse Genetics Programme: High throughput characterisation of knockout mice". Acta Ophthalmologica. 88 (S248). doi:10.1111/j.1755-3768.2010.4142.x.
- ^ Mouse Resources Portal, Wellcome Trust Sanger Institute.
- ^ "International Knockout Mouse Consortium".
- ^ "Mouse Genome Informatics".
- ^ Skarnes, W. C.; Rosen, B.; West, A. P.; Koutsourakis, M.; Bushell, W.; Iyer, V.; Mujica, A. O.; Thomas, M.; Harrow, J.; Cox, T.; Jackson, D.; Severin, J.; Biggs, P.; Fu, J.; Nefedov, M.; De Jong, P. J.; Stewart, A. F.; Bradley, A. (2011). "A conditional knockout resource for the genome-wide study of mouse gene function". Nature. 474 (7351): 337–342. doi:10.1038/nature10163. PMC 3572410. PMID 21677750.
- ^ Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
- ^ Collins FS, Rossant J, Wurst W (January 2007). "A mouse for all reasons". Cell. 128 (1): 9–13. doi:10.1016/j.cell.2006.12.018. PMID 17218247.
{{cite journal}}: CS1 maint: multiple names: authors list (link) - ^ van der Weyden L, White JK, Adams DJ, Logan DW (2011). "The mouse genetics toolkit: revealing function and mechanism". Genome Biol. 12 (6): 224. doi:10.1186/gb-2011-12-6-224. PMC 3218837. PMID 21722353.
{{cite journal}}: CS1 maint: multiple names: authors list (link) CS1 maint: unflagged free DOI (link)
Further reading
- Persson, B.; Kallberg, Y.; Bray, J. E.; Bruford, E.; Dellaporta, S. L.; Favia, A. D.; Duarte, R. G.; Jörnvall, H.; Kavanagh, K. L.; Kedishvili, N.; Kisiela, M.; Maser, E.; Mindnich, R.; Orchard, S.; Penning, T. M.; Thornton, J. M.; Adamski, J.; Oppermann, U. (2009). "The SDR (Short-Chain Dehydrogenase/Reductase and Related Enzymes) Nomenclature Initiative". Chemico-Biological Interactions. 178 (1–3): 94–98. doi:10.1016/j.cbi.2008.10.040. PMC 2896744. PMID 19027726.
- Lapshina, E. A.; Belyaeva, O. V.; Chumakova, O. V.; Kedishvili, N. Y. (2003). "Differential Recognition of the Free versus Bound Retinol by Human Microsomal Retinol/Sterol Dehydrogenases: Characterization of the Holo-CRBP Dehydrogenase Activity of RoDH-4†". Biochemistry. 42 (3): 776–784. doi:10.1021/bi026836r. PMID 12534290.
- Cain, J. M.; Zaino, R.; Shearer, D.; Bennett, R. A.; Olt, G.; Weisz, J. (2002). "Expression of a retinol dehydrogenase (hRoDH-4), a member of the retinol/steroid dehydrogenase family implicated in retinoic acid biosynthesis, in normal and neoplastic endometria". American Journal of Obstetrics and Gynecology. 186 (4): 675–683. doi:10.1067/mob.2002.122127. PMID 11967490.
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