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Phylogenetic Analysis and Taste Cell Expression of Calpain 9 in Catfish (Ictalurus punctatus)

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DOI: 10.4236/ns.2015.73016    2,772 Downloads   3,160 Views   Citations

ABSTRACT

The calpains, calcium-activated neutral proteases, play important roles in calcium-regulated intra-cellular signal transduction cascades. Here we report the isolation and initial characterization of a cDNA encoding a calpain 9, digestive tract specific calpain, from catfish taste epithelium. This calpain 9 (Ip-CAPN9a) shares 61% identity with human calpain 9. Phylogenetic analysis provides evidence that catfish calpain 9 and the related enzymes from Oncorhynchus mykiss, Danio rerio, Xenopus laevis, Mus musculus, Rattus norvegicus and Homo sapiens make up a distinct clade within the tissue-specific calpain family. Northern blot analysis reveals that Ip-CAPN9a is predominantly expressed in barbell and digestive tract, but not expressed in brain. An antibody against the N-terminal segment of Ip-CAPN9a recognizes cells within the taste buds in catfish barbells.

Conflicts of Interest

The authors declare no conflicts of interest.

Cite this paper

Ookura, T. , Koyama, E. , Hansen, A. , Teeter, J. , Kawamura, Y. and Brand, J. (2015) Phylogenetic Analysis and Taste Cell Expression of Calpain 9 in Catfish (Ictalurus punctatus). Natural Science, 7, 143-150. doi: 10.4236/ns.2015.73016.

References

[1] Sorimachi, H., Toyama-Sorimachi, N., Saido, T.C., Kawasaki, H., Sugita, H., Miyasaka, M., Arahata, K., Ishiura, S. and Suzuki, K. (1993) Muscle-Specific Calpain, p94, Is Degraded by Autolysis Immediately after Translation, Resulting in Disappearance from Muscle. Journal of Biological Chemistry, 268, 10593-10605.
[2] Richard, I., Broux, O., Allamand, V., Fougerousse, F., Chiannilkulchai, N., Bourg, N., Brenguier, L., Devaud, C., Pasturaud, P., Roudaut, C., et al. (1995) Mutations in the Proteolytic Enzyme Calpain 3 Cause Limb-Girdle Muscular Dystrophy Type 2A. Cell, 81, 27-40.
http://dx.doi.org/10.1016/0092-8674(95)90368-2
[3] Ma, H., Fukiage, C., Azuma, M. and Shearer, T.R. (1998) Cloning and Expression of mRNA for Calpain Lp82 from Rat Lens: Splice Variant of p94. Investigative Ophthalmology Visual Science, 39, 454-461.
[4] Sorimachi, H., Ishiura, S. and Suzuki, K. (1993) A Novel Tissue-Specific Calpain Species Expressed Predominantly in the Stomach Comprises Two Alternative Splicing Products with and without Ca(2+)-Binding Domain. Journal of Biological Chemistry, 268, 19476-19482.
[5] Lee, H.J., Sorimachi, H., Jeong, S.Y., Ishiura, S. and Suzuki, K. (1998) Molecular Cloning and Characterization of a Novel Tissue-Specific Calpain Predominantly Expressed in the Digestive Tract. Biological Chemistry, 379, 175-183.
http://dx.doi.org/10.1515/bchm.1998.379.2.175
[6] Hata, S., Abe, M., Suzuki, H., Kitamura, F., Toyama-Sorimachi, N., Abe, K., Sakimura, K. and Sorimachi, H. (2010) Calpain 8/nCL-2 and Calpain 9/nCL-4 Constitute an Active Protease Complex, G-Calpain, Involved in Gastric Mucosal Defense. PLoS Genetics, 6, e1001040.
http://dx.doi.org/10.1371/journal.pgen.1001040
[7] Yoshikawa, Y., Mukai, H., Hino, F., Asada, K. and Kato, I. (2000) Isolation of Two Novel Genes, Down-Regulated in Gastric Cancer. Japanese Journal of Cancer Research, 91, 459-463.
http://dx.doi.org/10.1111/j.1349-7006.2000.tb00967.x
[8] Markmann, A., Schafer, S., Linz, W., Lohn, M., Busch, A.E. and Wohlfart, P. (2005) Down-Regulation of Calpain 9 Is Linked to Hypertensive Heart and Kidney. Cellular Physiology and Biochemistry, 15, 109-116.
http://dx.doi.org/10.1159/000083643
[9] Sorimachi, H., Ishiura, S. and Suzuki, K. (1997) Structure and Physiological Function of Calpains. Biochemical Journal, 328, 721-732.
[10] Lin, G.D., Chattopadhyay, D., Maki, M., Wang, K.K., Carson, M., Jin, L., Yuen, P.W., Takano, E., Hatanaka, M., DeLucas, L.J. and Narayana, S.V. (1997) Crystal Structure of Calcium Bound Domain VI of Calpain at 1.9 A Resolution and Its Role in Enzyme Assembly, Regulation, and Inhibitor Binding. Nature Structural Molecular Biology, 4, 539-547.
http://dx.doi.org/10.1038/nsb0797-539
[11] Blanchard, H., Grochulski, P., Li, Y., Arthur, J.S., Davies, P.L., Elce, J.S. and Cygler, M. (1997) Structure of a Calpain Ca2+-Binding Domain Reveals a Novel EF-Hand and Ca2+-Induced Conformational Changes. Nature Structural Biology, 4, 532-538.
http://dx.doi.org/10.1038/nsb0797-532
[12] Lee, H.J., Tomioka, S., Kinbara, K., Masumoto, H., Jeong, S.Y., Sorimachi, H., Ishiura, S. and Suzuki, K. (1999) Characterization of a Human Digestive Tract-Specific Calpain, nCL-4, Expressed in the Baculovirus System. Archives of Biochemistry and Biophysics, 362, 22-31.
http://dx.doi.org/10.1006/abbi.1998.1021
[13] Azarian, S.M., King, A.J., Hallett, M.A. and Williams, D.S. (1995) Selective Proteolysis of Arrestin by Calpain. Molecular and Its Effect on Rhodopsin Dephosphorylation. The Journal of Biological Chemistry, 270, 24375-24384.
http://dx.doi.org/10.1074/jbc.270.41.24375,
[14] Magnusson, A., Haug, L.S., Walaas, S.I. and Ostvolt, A.C. (1993) Calcium-Induced Degradation of the Inositol(1,4,5)-Trisphosphate Receptor/Ca2+-Channel. FEBS Letters, 323, 229-232.
http://dx.doi.org/10.1016/0014-5793(93)81345-Z
[15] Banno, Y., Nakashima, S., Hachiya, T. and Nozawa, Y. (1995) Endogenous Cleavage of Phospholipase C-beta3 by Agonist-Induced Activation of Calpain in Human Platelets. The Journal of Biological Chemistry, 270, 4318-4324.
http://dx.doi.org/10.1074/jbc.270.9.4318
[16] Greenwood, A.F. and Jope, R.S. (1994) Brain G-Protein Proteolysis by Calpain: Enhancement by Lithium. Brain Research, 636, 320-326.
http://dx.doi.org/10.1016/0006-8993(94)91031-6
[17] Shinozaki, K., Maruyama, K., Kume, H., Tomita, T., Saido, T.C., Iwatsubo, T. and Obata, K. (1998) The Presenilin 2 Loop Domain Interacts with the Mu-Calpain C-Terminal Region. International Journal of Molecular Medicine, 1, 797-799.
[18] Roper, S.D. (2006) Signaling in the Chemosensory Systems. Cellular and Molecular Life Sciences, 63, 1494-1500.
http://dx.doi.org/10.1007/s00018-006-6112-9
[19] Ookura, T., Koyama, E., Puchalski, R.B., Teeter, J.H., Bayley, D.L. and Brand, J.G. (1997) Molecular Cloning of Calpain from Taste Epithelium of the Channel Catfish, Ictalurus punctatus. Chemical Senses, 22,764-765.
[20] Katoh, K., Kuma, K., Toh, H. and Miyata, T. (2005) MAFFT Version 5: Improvement in Accuracy of Multiple Sequence Alignment. Nucleic Acids Research, 33, 511-518.
http://dx.doi.org/10.1093/nar/gki198
[21] Felsenstein, J. (1981) Evolutionary Trees from DNA Sequences: A Maximum Likelihood Approach. Journal of Molecular Evolution, 17, 368-376.
http://dx.doi.org/10.1007/BF01734359
[22] Stamatakis, A. (2006) RAxML-VI-HPC: Maximum Likelihood-Based Phylogenetic Analyses with Thousands of Taxa and Mixed Models. Bioinformatics, 22, 2688-2690.
http://dx.doi.org/10.1093/bioinformatics/btl446
[23] Jones, D.T., Taylor, W.R. and Thornton, J.M. (1992) The Rapid Generation of Mutation Data Matrices from Protein Sequences. Computer Applications in the Biosciences, 8, 275-282.
[24] Tamura, K., Dudley, J., Nei, M. and Kumar, S. (2007) MEGA4: Molecular Evolutionary Genetics Analysis (MEGA) Software Version 4.0. Molecular Biology and Evolution, 24, 1596-1599.
http://dx.doi.org/10.1093/molbev/msm092
[25] Toyohara, H. and Makinodan, Y. (1989) Comparison of Calpain I and Calpain II from Carp Muscle. Comparative Biochemistry and Physiology Part B: Comparative Biochemistry, 92, 577-581.
http://dx.doi.org/10.1016/0305-0491(89)90134-X
[26] Salem, M., Nath, J., Rexroad, C.E., Killefer, J. and Yao, J. (2005) Identification and Molecular Characterization of the Rainbow Trout Calpains (Capn1 and Capn2): Their Expression in Muscle Wasting during Starvation. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, 140, 63-71.
http://dx.doi.org/10.1016/j.cbpc.2004.09.007
[27] Salem, M., Rexroad, C.E. and Yao, J. (2006) Identification of a Novel Gill-Specific Calpain from Rainbow Trout (Oncorhynchus mykiss). Fish Physiology and Biochemistry, 32, 1-6.
http://dx.doi.org/10.1007/s10695-005-0560-2
[28] Jekely, G. and Friedrich, P. (1999) The Evolution of the Calpain Family as Reflected in Paralogous Chromosome Regions. Journal of Molecular Evolution, 49, 272-281.
http://dx.doi.org/10.1007/PL00006549
[29] Maki, M., Narayana, S.V.L. and Hitomi, K. (1997) A Growing Family of the Ca2+-Binding Proteins with Five EF-Hand Motifs. Biochemical Journal, 328, 718-720.
[30] Theopold, U., Pinter, M., Daffre, S., Tryselius, Y., Friedrich, P., Nassel, D.R. and Hultmark, D. (1995) CalpA, a Drosophila Calpain Homologue Specifically Expressed in a Small Set of Nerve, Midgut, and Blood Cells. Molecular and Cellular Biology, 15, 824-834.
[31] Sorimachi, H., Tsukahara, T., Okada-Ban, M., Sugita, H., Ishiura, S. and Suzuki, K. (1995) Identification of a Third Ubiquitous Calpain Species-Chicken Muscle Expresses Four Distinct Calpains. Biochimica et Biophysica Acta (BBA)-Gene Structure and Expression, 1261, 381-393.
http://dx.doi.org/10.1016/0167-4781(95)00027-E

  
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