User:Andor J Kiss
- Director ~ Center for Bioinformatics and Functional Genomics
- Adjunct Assistant Professor ~ Departments of Biology & Microbiology
- 086C Pearson Hall
- Miami University
- Oxford, OH 45056
- 2005, PhD, University of Illinois at Urbana-Champaign (Ecology, Ethology & Evolution/Animal Biology)
- 1999, MSc, University of Western Ontario (Molecular Genetics/Zoology)
- 1994, BSc, University of Victoria (Biochemistry & Microbiology)
- Adaptive and evolutionary physiology of vertebrate animals. More specifically I am interested in their adaptation to extreme cold and heat, and how their physiological systems have evolved to allow them to exploit such niches. The model system that I have been using is that of the proteins in the eye lens. The proteins are called “crystallins” and play an important role in light refraction. Most vertebrates (excluding some birds) have three kinds of crystallins; alpha (α), beta (β) and gamma (γ). Alpha crystallin is also a type of small heat shock (sHsp) protein and comes in at least two flavours (isoforms). One of these α isoforms can be found widely expressed outside the eye lens and has important roles as a stress protein in a number of tissues. The β and γ crystallins are part of the same super-gene family, but presently there are no known non-refractive structure/function roles. Adaptation of ectothermic vertebrate lenses to cold is of interest to me as means of modeling not only lens cataracts, but to modeling globular protein stability. Cold-cataracts in mammalian lens have been used to model senile cataracts. Many ectothermic vertebrates that are cold-adapted do not show a cold-cataract (see interest #2). Thus, the appearance or absence of a lens cataract is a rare example of a protein model system that allows investigation into evolutionary adaptation and physiological importance of globular non-enzymatic protein stability.
- Structure/Function basis of long-term stability of globular protein systems. A second major interest of mine is molecular (amino acid) adaptations that occur in globular (structural) proteins which impart a long-term stability. This is essentially an extrapolation of the first research interest to non-lenticular proteins. However, lenses from ectothermic animals are ideal systems to study this problem as these animals (including their lenses) are thermally adapted to their native environments (whether cold or hot). Because lens proteins are conserved amongst vertebrates these structure/function comparisons are valid. Human lenses do not show thermal adaptation thus providing an excellent comparative basis to determine the structural basis of the instability in many mammalian lenses. In fact, human lenses exhibit a so-called “cold-cataract” at temperatures below +20°C, which has been used to model not only senile (age-related) cataracts, but also other protein condensation diseases such as Alzheimer's Diseases and Sickle Cell Anæmia. The common thread through each of these pathologies are instabilities in the globular/structural proteins. By using a novel cross-species chaperone assay developed in my lab (Kiss et. al., 2004), coupled with phylogenetic analysis (Kiss et. al., 2008), and mass-spectrometry proteomics approaches, we are identifying individual crystallins, their residue changes and their post-translational modifications that we believe have increased the stability of the crystallins and thus maintaining lens transparency.
- Sensory systems in the acclimatory response. The ability of an animal to change its physiology dependent on environmental cues is a complex and multifaceted process. Whether the animal is a fish, frog, bird, rat or human, an acclimatory response is something that occurs readily everyday in animals. I am currently engaged in studies using the North American wood frog Rana sylvatica to determine the changes in protein expression permitting these frogs to be able to freeze solid, thaw and survive. This overwintering strategy is rare among higher vertebrates and demonstrates an extreme example of physiological, biochemical and molecular adaptation. Future plans to employ cDNA arrays and genome technologies are underway that will further elucidate the mechanisms by which these animals are able to sense their environment thereby prompting a freeze competent state in the frogs.
- BIO 209: Cell Biology
- BIO 400: Epigenetics
- BIO 407/507: Ichthyology
- PDF describing a Python script to parse BLASTX output from NCBI
- Link to a gz zipped tarball of the actual Python script and examples
1) Thompson SM, Rakoczy RJ, Duffy MA, Kiss AJ, McMurray MS. 2023. Differential consumption of alcohol, caffeine, and caffeinated alcohol by adolescent rats, and effects on post-adolescent gene expression signatures in the nucleus accumbens and orbitofrontal cortex. Drug Alcohol Depend [Internet] 251:110921. Link
2) Walters, A. D. et al. Phylogenetic relationship and habitat both impact the gut microbiome in two microendemic gastropods. J. Molluscan Stud. 88, 88 (2022). OPEN ACCESS
3) Rainey, A., A. Pierce, X. Deng, L. A. Actis, P. Smith, A. J. Kiss, and T. J. Wilson. 2021. Validation and deployment of a direct saliva real-time RT-PCR test on pooled samples for COVID-19 surveillance testing. PLOS ONE 16:e0261956 OPEN ACCESS
4) Oswald, K. J., Spinks, E., Duktig, G. S., Baker, J. S., Kibbey, M. R., Zimmerman, B., Tucker, H., Boucher, C. E., Cincotta, D. A., Starnes, W. C., Kiss, A. J., Wright, J. J., Carlson, D. M., Bangs, M. R., Roberts, M. A., & Quattro, J. M. (2020). Drainage History, Evolution, and Conservation of Tonguetied Minnow (Exoglossum laurae), a Rare and Imperiled Teays River Endemic. Copeia, 108(2), 381. doi:10.1643/CI-18-118 Link
5) Posner, M., McDonald, M. S., Murray, K. L., & Kiss, A. J. (2019). Why does the zebrafish cloche mutant develop lens cataract? PLOS ONE, 14(3), e0211399. doi:10.1371/JOURNAL.PONE.0211399 OPEN ACCESS
6) Bierma, J. C., Roskamp, K. W., Ledray, A. P., Kiss, A. J., Christina Cheng, C.-H. and Martin, R. W. (2018). Controlling Liquid-Liquid Phase Separation of Cold-Adapted Crystallin Proteins from the Antarctic Toothfish. J. Mol. Biol. 18. doi:10.1016/j.jmb.2018.10.023 Link
7) Teufel, A.G., Li, W., Kiss, A.J. and Rachael Morgan-Kiss. Polar Biol (2016). Impact of nitrogen and phosphorus on phytoplankton production and bacterial community structure in two stratified Antarctic lakes: a bioassay approach doi:10.1007/s00300-016-2025-8 Link
8) Marlo K. Sellin Jeffries, Andor J. Kiss, Austin W. Smith and James T. Oris. (2014). A comparison of commercially-available automated and manual extraction kits for the isolation of total RNA from small tissue samples. BMC Biotechnology. 14:94 doi:10.1186/s12896-014-0094-8 OPEN ACCESS
9) Andrew J. Rosendale, Jon P. Costanzo, Andor J. Kiss, and Richard E. Lee Jr. (2014). Identification and Expression of a Putative Facilitative Urea Transporter in Three Species of True Frogs (Ranidae): Implications for Terrestrial Adaptation. Advances in Biology. Volume 2014, Article ID 148276, 11 pages. OPEN ACCESS
10) Posner M., Kiss A.J., Skiba J., Drossman A., Dolinska M.B., Hejtmancik, J.F. and Sergeev, Y.V. (2012). Functional Validation of Hydrophobic Adaptation to Physiological Temperature in the Small Heat Shock Protein αA-crystallin. PLoS ONE 7(3): e34438. OPEN ACCESS
Above article highlighted as an Editorial Feature Hydrophobicity Counts in Large Amounts in the ‘Outside JEB’ section of Journal of Experimental Biology.
11) Kiss, A.J., Muir, T.J., Lee R.E. and Costanzo, J. (2011). Seasonal Variation in the Hepatoproteome of the Dehydration and Freeze-tolerant Wood Frog Rana sylvatica. International Journal of Molecular Sciences. 12(12), 8406-8414 OPEN ACCESS
12) Philip, B.N., Kiss, A.J. and Lee, R.E. (2011). The protective role of aquaporins in the freeze-tolerant insect Eurosta solidaginis: Functional characterization and tissue abundance of EsAQP1. J. Exp. Biol. 214: 848-857. http://dx.doi.org/10.1242/jeb.051276
13) Kiss, A.J., DeVries, A.L. and Morgan-Kiss, R.M (2010). Comparative Analysis of Crystallins and Lipids from the Lens of Antarctic Toothfish and Cow. Journal of Comparative Physiology B Oct;180(7):1019-32. http://dx.doi.org/10.1007/s00360-010-0475-9
14) Mirarefi, A.Y., Boutet, S., Ramakrishnan, S., Kiss, A.J., Cheng, C-H. C., DeVries, A.L., Robinson, I.K. and Zukoski, C.F. (2010). Small Angle X-ray Scattering Studies of the Intact Eye Lens: Effect of Crystallin Composition and Concentration on Microstructure. Biochimica et Biophysica Acta – General Subjects. Jun;1800(6):556-64.http://dx.doi.org/10.1016/j.bbagen.2010.02.004
15) Kiss, A.J. (2008). The Antarctic Toothfish: A new model system for eye lens biology. in Animal Models in Eye Research. Ed: Panangoitis A. Tsonis. Academic Press (Elsevier), NY. pp. 48-56. http://dx.doi.org/10.1016/B978-0-12-374169-1.00005-9
16) Kiss, A.J. and Cheng, C.-H.C. (2008). Molecular Diversity and Genomic Organisation of the α, β and γ Eye Lens Crystallins from the Antarctic Toothfish Dissostichus mawsoni. Comparative Biochemistry and Physiology. Part D: Genomics and Proteomics. 3(2):155-171. http://dx.doi.org/10.1016/j.cbd.2008.02.002
17) Kiss, A.J., Mirarefi, A.Y, Ramakrishnan, S., Zukoski, C.F., DeVries, A.L. and Cheng, C-H.C. (2004). Cold Stable Eye Lens Crystallins of the Antarctic Nototheniid Toothfish Dissostichus mawsoni Norman. Journal of Experimental Biology. 207:4633–4649. http://jeb.biologists.org/cgi/content/full/207/26/4633
Above article highlighted as an Editorial Feature Blindingly Cold in the ‘Inside JEB’ section of Journal of Experimental Biology.
18) Kiss, A.J., Farah, K., Kim, J., Garriock, R. J., Drysdale, T. A. and Hammond, J. R. (2000). Molecular Cloning and Functional Characterization of Inhibitor-Sensitive (mENT1) and Inhibitor-Resistant (mENT2) Equilibrative Nucleoside Transporters from Mouse Brain. Biochemical Journal. 352 Pt 2, 363-72. http://www.ncbi.nlm.nih.gov/pmc/articles/PMC1221467/?tool=pubmed
19) Hunt, J.G., Kasinsky, H.E., Elsey, R.M., Wright, C.L., Rice, P., Bell, J.E., Sharp ,D.J., Kiss, A.J., Hunt, D.F., Arnott, D.P., Russ, M.M.; Shabanowitz, J. and Juan Ausió. (1996). Protamines of Reptiles. Journal of Biological Chemistry. Sep 20;271(38):23547-57. doi: 10.1074/jbc.271.38.23547
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