Tissue distribution of the four gene products of the plasma membrane Ca2+ pump. A study using specific antibodies.

Antibodies against the four isoforms of the human plasma membrane Ca(2+)-ATPase (PMCA) were raised using an N-terminal sequence of the pump as epitope. The antibodies against PMCA isoforms 1, 2, and 3 were not species-specific, e.g. they also recognized the corresponding proteins in rat, whereas that against the human PMCA isoform 4 failed to do so. The tissue distribution of the four isoforms was estimated by Western blot analysis. Two, PMCA1 and PMCA4, were expressed in all tissues tested (with the exception of the choroid plexus, where the former was not detected). In most tissues the signal from the PMCA1 protein exceeded that of PMCA4, the exception being the erythrocyte. The PMCA2 and PMCA3 proteins were only found in neuronal tissues; the PMCA2 protein was present in high concentrations in the cerebellum and in the cerebral cortex. At variance with previous results on mRNA (e.g. the kidney) no other tissues contained the PMCA2 protein. PMCA3 was the other tissue-specific isoform; in agreement with results in the rat, the protein was found in human neuronal tissues, particularly in the choroid plexus, but was practically absent in all other tissues tested.

[1]  D. Zacharias,et al.  Transcript distribution of plasma membrane Ca2+ pump isoforms and splice variants in the human brain. , 1995, Brain research. Molecular brain research.

[2]  E. Carafoli,et al.  Cloning and expression of isoform 2 of the human plasma membrane Ca2+ ATPase. Functional properties of the enzyme and its splicing products. , 1994, The Journal of biological chemistry.

[3]  E. Carafoli Biogenesis: Plasma membrane calcium ATPase: 15 years of work on the purified enzyme 1 , 1994, FASEB journal : official publication of the Federation of American Societies for Experimental Biology.

[4]  T. Stauffer,et al.  The plasma membrane calcium pump: functional domains, regulation of the activity, and tissue specificity of isoform expression. , 1994, Journal of neurobiology.

[5]  T. H. Brown,et al.  Confocal laser scanning microscopy reveals voltage-gated calcium signals within hippocampal dendritic spines. , 1994, Journal of neurobiology.

[6]  R. Heim,et al.  The Ca2+ affinity of the plasma membrane Ca2+ pump is controlled by alternative splicing. , 1994, The Journal of biological chemistry.

[7]  O. Mcbride,et al.  Localization of two genes encoding plasma membrane Ca2+ ATPases isoforms 2 (ATP2B2) and 3 (ATP2B3) to human chromosomes 3p26-->p25 and Xq28, respectively. , 1994, Cytogenetics and cell genetics.

[8]  J. T. Penniston,et al.  Immunocytochemical localization of the plasma membrane calcium pump, calbindin-D28k, and parvalbumin in Purkinje cells of avian and mammalian cerebellum. , 1993, Proceedings of the National Academy of Sciences of the United States of America.

[9]  T. Stauffer,et al.  Quantitative analysis of alternative splicing options of human plasma membrane calcium pump genes. , 1993, The Journal of biological chemistry.

[10]  M. Berridge A tale of two messengers , 1993, Nature.

[11]  E. Carafoli,et al.  Molecular and cellular biology of plasma membrane calcium ATPase. , 1993, Trends in cardiovascular medicine.

[12]  D. Paslier,et al.  von Hippel-Lindau syndrome: cloning and identification of the plasma membrane Ca(++)-transporting ATPase isoform 2 gene that resides in the von Hippel-Lindau gene region. , 1993, Cancer research.

[13]  G. Shull,et al.  Alternative splicing of exons encoding the calmodulin-binding domains and C termini of plasma membrane Ca(2+)-ATPase isoforms 1, 2, 3, and 4. , 1993, The Journal of biological chemistry.

[14]  N. Harrison,et al.  Calcium homeostasis in rat septal neurons in tissue culture , 1993, Brain Research.

[15]  R. Heim,et al.  Expression, purification, and properties of the plasma membrane Ca2+ pump and of its N-terminally truncated 105-kDa fragment. , 1992, The Journal of biological chemistry.

[16]  W L Stahl,et al.  Plasma membrane Ca(2+)-ATPase isoforms: distribution of mRNAs in rat brain by in situ hybridization. , 1992, Brain research. Molecular brain research.

[17]  R. Neve,et al.  Determination of the nucleotide sequence and chromosomal localization of the ATP2B2 gene encoding human Ca(2+)-pumping ATPase isoform PMCA2. , 1992, Genomics.

[18]  C. D. Benham,et al.  Ca2+ efflux mechanisms following depolarization evoked calcium transients in cultured rat sensory neurones. , 1992, The Journal of physiology.

[19]  T. Vanaman,et al.  Analysis of the tissue-specific distribution of mRNAs encoding the plasma membrane calcium-pumping ATPases and characterization of an alternately spliced form of PMCA4 at the cDNA and genomic levels. , 1992, The Journal of biological chemistry.

[20]  E Carafoli,et al.  The Ca2+ pump of the plasma membrane. , 1992, The Journal of biological chemistry.

[21]  Rodolfo R. Llinás,et al.  The Electrophysiology of the Cerebellar Purkinje Cell Revisited , 1992 .

[22]  R. Llinás,et al.  The Cerebellum Revisited , 1992, Springer US.

[23]  O. Mcbride,et al.  Localization of two genes encoding plasma membrane Ca2(+)-transporting ATPases to human chromosomes 1q25-32 and 12q21-23. , 1991, Genomics.

[24]  R. Meloen,et al.  New B cell epitopes in the Plasmodium falciparum malaria circumsporozoite protein , 1990, European journal of immunology.

[25]  T. Vorherr,et al.  Peptide sequence analysis and molecular cloning reveal two calcium pump isoforms in the human erythrocyte membrane. , 1990, The Journal of biological chemistry.

[26]  J. Greeb,et al.  Molecular cloning of a third isoform of the calmodulin-sensitive plasma membrane Ca2+-transporting ATPase that is expressed predominantly in brain and skeletal muscle. , 1989, The Journal of biological chemistry.

[27]  J. T. Penniston,et al.  Calcium pump epitopes in placental trophoblast basal plasma membranes. , 1989, The American journal of physiology.

[28]  R. Kumar,et al.  Cerebrospinal fluid calcium homeostasis: evidence for a plasma membrane Ca2+-pump in mammalian choroid plexus , 1989, Brain Research.

[29]  T. Vorherr,et al.  Primary structure of the cAMP-dependent phosphorylation site of the plasma membrane calcium pump. , 1989, Biochemistry.

[30]  E. Wieben,et al.  Complete primary structure of a human plasma membrane Ca2+ pump. , 1988, The Journal of biological chemistry.

[31]  J. Greeb,et al.  Molecular cloning of two isoforms of the plasma membrane Ca2+-transporting ATPase from rat brain. Structural and functional domains exhibit similarity to Na+,K+- and other cation transport ATPases. , 1988, The Journal of biological chemistry.

[32]  H. Schägger,et al.  Tricine-sodium dodecyl sulfate-polyacrylamide gel electrophoresis for the separation of proteins in the range from 1 to 100 kDa. , 1987, Analytical biochemistry.

[33]  M. Zurini,et al.  Purification, reconstitution, and molecular characterization of the Ca2+ pump of plasma membranes. , 1987, Methods in enzymology.

[34]  Á. Enyedi,et al.  Molecular characterization of the in situ red cell membrane calcium pump by limited proteolysis. , 1986, The Journal of biological chemistry.

[35]  P. Caroni,et al.  Regulation of Ca2+-pumping ATPase of heart sarcolemma by a phosphorylation-dephosphorylation Process. , 1981, The Journal of biological chemistry.

[36]  J. T. Penniston,et al.  Purification of the (Ca2+-Mg2+)-ATPase from human erythrocyte membranes using a calmodulin affinity column. , 1979, The Journal of biological chemistry.

[37]  H. Towbin,et al.  Electrophoretic transfer of proteins from polyacrylamide gels to nitrocellulose sheets: procedure and some applications. , 1979, Proceedings of the National Academy of Sciences of the United States of America.

[38]  M. M. Bradford A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. , 1976, Analytical biochemistry.

[39]  J. Hoffman,et al.  Electrophoretic Separation of Different Phophosproteins Associated with Ca-ATPase and Na,K-ATPase in Human Red Cell Ghosts , 1974, The Journal of general physiology.

[40]  U. K. Laemmli,et al.  Cleavage of Structural Proteins during the Assembly of the Head of Bacteriophage T4 , 1970, Nature.