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Aquaporins and related genes. Landon Lasseter Biol 7020 26 April 2010. Aquaporins. What are Aquaporins ? How many organisms have them? Why are they important? Who discovered them?. Aquaporins. There are at least 12 Aquaporin proteins present in the human body.

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aquaporins and related genes

Aquaporins and related genes

Landon Lasseter

Biol 7020

26 April 2010

  • What are Aquaporins?
  • How many organisms have them?
  • Why are they important?
  • Who discovered them?
  • There are at least 12 Aquaporin proteins present in the human body.
  • Mutations in some lead to disease.
  • Some are essential for numerous body functions.
  • Without them, we would die of dehydration.
what do they look like
What do they look like?
  • Constructed of 6 alpha-helices in a right hand configuration
  • Form tetramers, each acts as a monomer.

types of aquaporin
Types of Aquaporin
  • AquaporinsvsAquaglyceroporins
  • What is the difference?

how do they work
How do they work?
  • NPA motif
  • Ar/R selective filter

what is my project
What is my project?
  • Comparing the Aquaporin and Aquaporin like genes in the human genome.
  • 20 sequences found
  • 16 used for phylogeny tree once reduced
purpose of the project
Purpose of the Project?
  • To possibly find the gene that gave rise to the numerous Aquaporin like genes found today.
  • A better understanding of Aquaporin genes could lead to effective treatments for diseases related to their mutations.
  • Understanding the similarities and differences in Aquaporins provides a better understanding of cellular function and specialization.
  • Results with no outgroup (n=16)
  • Results with Daniorerio as an outgroup (n=17)
  • Results with other outgroups?
seaview sequences
Seaview Sequences

Seaview view of my sequences in protein view.

  • Agre P, Preston GM, Smith BL, Jung JS, Raina S, Moon C, Guggino WB, Nielsen S (1 October 1993). "Aquaporin CHIP: the archetypal molecular water channel". Am. J. Physiol.265 (4 Pt 2): F463–76.
  • Agre P (2006). "The aquaporin water channels". Proc Am Thorac Soc3 (1): 5–13.
  • Damiano,A., Zotta,E., Goldstein,J., Reisin,I. and Ibarra,C. (2001) “Water channel proteins AQP3 and AQP9 are present in syncytiotrophoblast of human term placenta”. Placenta 22 (8-9), 776-781.
  • Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated water transport". Proc. Soc. Exp. Biol. Med.219 (3): 183–99.
  • Fischer,H., Stenling,R., Rubio,C. and Lindblom,A. (2001) “Differential expression of aquaporin 8 in human colonic epithelial cells and colorectal tumors”. BMC Physiol. 1, 1.
  • Fu D, Lu M (2007). "The structural basis of water permeation and proton exclusion in aquaporins". Mol. Membr. Biol.24 (5-6): 366–74.
  • Gonen T, Walz T (2006). "The structure of aquaporins". Q. Rev. Biophys.39 (4): 361–96.
resources cont
Resources (cont.)
  • de Groot BL, Grubmüller H (2001). "Water permeation across biological membranes: mechanism and dynamics of aquaporin-1 and GlpF". Science294 (5550): 2353–2357.
  • Hatakeyama,S., Yoshida,Y., Tani,T., Koyama,Y., Nihei,K., Ohshiro,K., Kamiie,J.I., Yaoita,E., Suda,T., Hatakeyama,K. and Yamamoto,T. (2001) “Cloning of a new aquaporin (AQP10) abundantly expressed in duodenum and jejunum”. Biochem. Biophys. Res. Commun. 287 (4), 814-819.
  • Ishibashi,K., Kuwahara,M., Gu,Y., Tanaka,Y., Marumo,F. and Sasaki,S. (1998) “Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol”. Biochem. Biophys. Res. Commun. 244 (1), 268-274.
  • Lennon VA, Kryzer TJ, Pittock SJ, Verkman AS, Hinson SR (August 2005). "IgG marker of optic-spinal multiple sclerosis binds to the aquaporin-4 water channel". J. Exp. Med.202 (4): 473–7.
  • Mobasheri, A., Shakibaei, M., Marples, D.  (2004) “Immunohistochemical localization of aquaporin 10 in the apical membranes of the human ileum: a potential pathway for luminal water and small solute absorption”.Histochem. Cell Biol. Jun;121(6):463-71.
  • Preston GM, Carroll TP, Guggino WB, Agre P. Appearance of water channels in Xenopusoocytes expressing red cell CHIP28 protein. Science 1992;256:385–387.
  • Reizer J, Reizer A, SaierJr MH (1993). "The MIP family of integral membrane channel proteins: sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins". Crit. Rev. Biochem. Mol. Biol.28 (3): 235–257.
resources cont1
Resources (cont.)
  • Savelkoul,P.J., De Mattia,F., Li,Y., Kamsteeg,E.J., Konings,I.B., van derSluijs,P. and Deen,P.M. (2009) “p.R254Q mutation in the aquaporin-2 water channel causing dominant nephrogenic diabetes insipidus is due to a lack of arginine vasopressin-induced phosphorylation” Hum. Mutat. 30 (10), E891-E903.
  • Tajkhorshid E, Nollert P, Jensen MØ, Miercke LJ, O'Connell J, Stroud RM, Schulten K (2002). "Control of the selectivity of the aquaporin water channel family by global orientational tuning". Science296 (5567): 525–30.
  • Unknown author. (2003) “The Nobel Prize in Chemistry 2003”. Nobel Foundation. Retrieved 4/14/2010.
  • Walter F., PhD. Boron (2005). Medical Physiology: A Cellular And Molecular Approaoch. Elsevier/Saunders. Page 842.
  • Wistow GJ, Pisano MM, Chepelinsky AB (1991). “Tandem sequence repeats in transmembrane channel proteins.” Trends Biochem. Sci. 16 170-1.
  • Entrez Gene Link MIP
  • Entrez Gene Link AQP5
  • Entrez Gene Link AQP6
  • Entrez Gene Link AQP7
  • Entrez Gene Link AQP8
software used
Software Used
  • FigTree Version 1.3.1
  • MAFFT Version 6.717
  • RAxML Version 7.0.4
  • Seaview Version 4.1.2