Back
 AJMB  Vol.11 No.2 , April 2021
Characteristics of a Critical Calcium Transportation Regulator: Plasma Membrane Ca2+-ATPase Involved in Calcium Homeostasis from Hyriopsis cumingii (Lea)
Abstract: Plasma Membrane Calcium ATPase (PMCA) plays a critical role in transporting Ca2+ out of the cytosol across the plasma membrane. Here, a full-length cDNA sequence of plasma membrane Ca2+-ATPase gene was isolated from the gill of Hyriopsis cumingii (HcPMCA) by using SMART RACE technique. The entire cDNA was 5230 bp, including a 417-bp 5'-UTR, a 3588-bp ORF and a 1225-bp 3'-UTR, encoding a 1195-amino acid protein, and no putative signal peptide was predicted. Compared with PMCA homologs from seawater mollusks, HcPMCA had high similarity with them in both sequence and structure. Tissue-specific expression analysis revealed that HcPMCA mRNA was detected in all the sampled tissues, but was prominently expressed in the gill and mantle. When exposed to a serie of increasing Ca2+ that lasted for 7 days, the mRNA expression of HcPMCA in the mantle was slightly downregulated, but peaked at 60 mg/L. Moreover, the temporal expression of HcPMCA transcripts in the mantle after 60 mg/L Ca2+ exposure was shown to be bell-shaped, which was slightly downregulated at 24 h, but upregulated from 24 h to 48 h post-treatment, peaking at 48 h. The result of present study provides useful information for further studies on function and regulation mechanism of HcPMCA gene.
Cite this paper: Zhang, A. and Zhou, Z. (2021) Characteristics of a Critical Calcium Transportation Regulator: Plasma Membrane Ca2+-ATPase Involved in Calcium Homeostasis from Hyriopsis cumingii (Lea). American Journal of Molecular Biology, 11, 38-50. doi: 10.4236/ajmb.2021.112004.
References

[1]   Docampo, R. and Huang, G. (2015) Calcium Signaling in Trypanosomatid Parasites. Cell Calcium, 57, 194-202.
https://doi.org/10.1016/j.ceca.2014.10.015

[2]   Peterson, J.A., Oblad, R.V., Mecham, J.C. and Kenealey, J.D. (2016) Resveratrol Inhibits Plasma Membrane Ca2+-ATPase Inducing an Increase in Cytoplasmic Calcium. Biochemistry & Biophysics Reports, 7, 253-258.
https://doi.org/10.1016/j.bbrep.2016.06.019

[3]   Schatzmann, H.J. (1966) ATP-Dependent Ca++-Extrusion from Human Red Cells. Experientia, 22, 364.
https://doi.org/10.1007/BF01901136

[4]   Carafoli, E. and Stauffer, T. (2010) The Plasma Membrane Calcium Pump: Functional Domains, Regulation of the Activity, and Tissue Specificity of Isoform Expression. Developmental Neurobiology, 25, 312-324.
https://doi.org/10.1002/neu.480250311

[5]   Rasmussen, H. and Barrett, P.Q. (1984) Calcium Messenger System: An Integrated View. Physiological Reviews, 64, 938-984.
https://doi.org/10.1152/physrev.1984.64.3.938

[6]   Wang, X., Fan, W.M., Xie, L.P. and Zhang, R.Q. (2008) Molecular Cloning and Distribution of a Plasma Membrane Calcium ATPase Homolog from the Pearl Oyster Pinctada fucata. Journal of Tsinghua University (Science and Technology), 13, 439-446.
https://doi.org/10.1016/S1007-0214(08)70071-3

[7]   Zhang, A.J., Liu, S.L., Zhu, J.Y., Gu, Z.M. and Lu K.H. (2016) Transcriptome Analysis of the Freshwater Pearl Mussel, Hyriopsis cumingii (Lea) Using Illumina Paired-End Sequencing to Identify Genes and Markers. Iranian Journal of Fisheries Sciences, 15, 1425-1440.

[8]   Tusnády, G.E. and Simon, I. (2001) The HMMTOP Transmembrane Topology Prediction Server. Bioinformatics, 17, 849-850.
https://doi.org/10.1093/bioinformatics/17.9.849

[9]   Li, X.C., Zhu, L., Li, L.G., Ren, Q. and Huang, Y.Q. (2013) A Novel Myeloid Differentiation Factor 88 Homolog, SpMyD88, Exhibiting Sp Toll-Binding Activity in the Mud Crab Scylla paramamosain. Developmental and Comparative Immunology, 39, 313-322.
https://doi.org/10.1016/j.dci.2012.11.011

[10]   Livak, K.J. and Schmittgen, T.D. (2001) Analysis of Relative Gene Expression Data Using Real-Time Quantitative PCR and the 2-ΔΔCT Method. Methods, 25, 402-408.
https://doi.org/10.1006/meth.2001.1262

[11]   Lopreiato, R., Giacomello, M. and Carafoli, E. (2014) The Plasma Membrane Calcium Pump: New Ways to Look at an Old Enzyme. Journal of Biological Chemistry, 289, 10261-10268.
https://doi.org/10.1074/jbc.O114.555565

[12]   Brini, M. and Carafoli, E. (2011) The Plasma Membrane Ca2+ ATPase and the Plasma Membrane Sodium Calcium Exchanger Cooperate in the Regulation of Cell Calcium. Cold Spring Harbor Perspectives in Biology, 3, 487-496.
https://doi.org/10.1101/cshperspect.a004168

[13]   Brini, M. and Carafoli, E. (2014) Calcium Pumps in Health and Disease. Cardiac Electrophysiology from Cell to Bedside, 89, 43-53.
https://doi.org/10.1016/B978-1-4557-2856-5.00005-4

[14]   Barbato, G., Ikura, M., Kay, L.E., Pastor, R.W. and Bax, A. (1992) Backbone Dynamics of Calmodulin Studied by 15N Relaxation Using Inverse Detected Two-Dimensional NMR Spectroscopy: The Central Helix Is Flexible. Biochemistry, 31, 5269-5278.
https://doi.org/10.1021/bi00138a005

[15]   Moore, C.M., Hoey, E.M., Trudgett, A. and Timson, D.J. (2012) A Plasma Membrane Ca2+-ATPase (PMCA) from the Liver Fluke, Fasciola hepatica. International Journal for Parasitology, 42, 851.
https://doi.org/10.1016/j.ijpara.2012.06.003

[16]   Mruk, K., Farley, B.M., Ritacco, A.W. and Kobertz, W.R. (2014) Calmodulation Meta-Analysis: Predicting Calmodulin Binding via Canonical Motif Clustering. Journal of General Physiology, 144, 105-114.
https://doi.org/10.1085/jgp.201311140

[17]   Carafoli, E. and Guerini, D. (1993) Molecular and Cellular Biology of Plasma Membrane Calcium ATPase. Trends in Cardiovascular Medicine, 3, 177-184.
https://doi.org/10.1016/1050-1738(93)90003-O

[18]   Carafoli, E. and Lim, D. (2012) Plasma Membrane Calcium ATPase. Acta Biophysica Sinica, 28, 581-596.
https://doi.org/10.1007/978-0-387-30370-3_32

[19]   Hao, Y.Y. (2011) Effect of Three Different Factors on the Calcium Ion Metabolism and Expression of Alkaline Phosphatase Gene in Hyriopsis cumingii. Shanghai Ocean University, Shanghai.

[20]   Cho, J.H., Bandyopadhyay, J., Lee, J., Park, C.S. and Ahnn, J. (2000) Two Isoforms of Sarco/Endoplasmic Reticulum Calcium ATPase (SERCA) Are Essential in Caenorhabditis elegans. Gene, 261, 211-219.
https://doi.org/10.1016/S0378-1119(00)00536-9

[21]   Beirao, P.S., Hamilton, J. and Nascimento, M. (1989) Sodium- and Calcium-Dependent Mechanisms in the Action Potential of the Secretory Epithelium of a Clam Mantle. Journal of Experimental Biology, 145, 395-402.

[22]   Kirschner, L.B., Sorenson, A.L. and Kriebel, M. (1960) Calcium and Electric Potential across the Clam Mantle. Science, 131, 735.
https://doi.org/10.1126/science.131.3402.735-a

[23]   Coimbra, J., Machado, J., Fernandes, P.L., Ferreira, H.G. and Ferreira, K.G. (1988) Electrophysiology of the Mantle of Anodonta cygnea. Journal of Experimental Biology, 140, 65-88.

[24]   Tang, M. and Shi, A.J. (2000) Studies of Environmental Calcium Concentration Effect on the Calcium Metabolism of the Mantle and Pearl Sac of the Freshwater Pearl Mussel. Journal of Sichuan University, 37, 741-747.

[25]   Li, W.J., Shi, Z.Y., Hao, Y.Y., Han, J., Qi, L.L. and Ye, X.F. (2011) Research of Calcium Flux by Ion-Selective Microelectrodes in Mantle Tissue of Hyriopsis cumingii. Acta Hydrobiologica Sinica, 35, 545-549.

[26]   Shu, M.A., Hu, H.J., Lu, J.Y., Xu, B.P., Wang, Y., Liu, G.X. and Guo, X.L. (2013) Full-Length cDNA Cloning and Expression Analysis of calreticulin Gene from Hyriopsis cumingii. Acta Hydrobiologica Sinica, 37, 999-1006.

 
 
Top