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

Rdh16 knockout mouse phenotype

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 Rdh16^{tm1a(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

1. "Retinol dehydrogenase 16 (all-trans)". Retrieved 2011-12-06.
2. "Salmonella infection data for Rdh16". Wellcome Trust Sanger Institute.
3. "Citrobacter infection data for Rdh16". Wellcome Trust Sanger Institute.
4. 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.
5. Mouse Resources Portal, Wellcome Trust Sanger Institute.
6. "International Knockout Mouse Consortium".
7. "Mouse Genome Informatics".
8. 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.
9. Dolgin E (June 2011). "Mouse library set to be knockout". Nature. 474 (7351): 262–3. doi:10.1038/474262a. PMID 21677718.
10. 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.
11. 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.

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.[phone]. PMID 11967490.