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Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting
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| Zeitschriftentitel: | Journal of Experimental Biology |
|---|---|
| Personen und Körperschaften: | , |
| In: | Journal of Experimental Biology, 207, 2004, 17, S. 2991-3002 |
| Format: | E-Article |
| Sprache: | Englisch |
| veröffentlicht: |
The Company of Biologists
|
| Schlagwörter: |
| author_facet |
Gao, Yongping Wheatly, Michele G. Gao, Yongping Wheatly, Michele G. |
|---|---|
| author |
Gao, Yongping Wheatly, Michele G. |
| spellingShingle |
Gao, Yongping Wheatly, Michele G. Journal of Experimental Biology Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting Insect Science Molecular Biology Animal Science and Zoology Aquatic Science Physiology Ecology, Evolution, Behavior and Systematics |
| author_sort |
gao, yongping |
| spelling |
Gao, Yongping Wheatly, Michele G. 1477-9145 0022-0949 The Company of Biologists Insect Science Molecular Biology Animal Science and Zoology Aquatic Science Physiology Ecology, Evolution, Behavior and Systematics http://dx.doi.org/10.1242/jeb.01101 <jats:title>SUMMARY</jats:title><jats:p>The discontinuous pattern of crustacean cuticular mineralization (the molting cycle) has emerged as a model system to study the spatial and temporal regulation of genes that code for Ca2+-transporting proteins including pumps, channels and exchangers. The plasma membrane Ca2+-ATPase (PMCA) is potentially of significant interest due to its role in the active transport of Ca2+ across the basolateral membrane, which is required for routine maintenance of intracellular Ca2+ as well as unidirectional Ca2+ influx. Prior research has suggested that PMCA expression is upregulated during periods of elevated Ca2+ influx associated with postmolt cuticular mineralization. This paper describes the cloning, sequencing and functional characterization of a novel PMCA3 gene from the antennal gland(kidney) of the crayfish Procambarus clarkii. The complete sequence,the first obtained from a non-genetic invertebrate species, was obtained through reverse transcription-polymerase chain reaction (RTPCR) and rapid amplification of cDNA ends (RACE) techniques. Crayfish PMCA3 consists of 4148 bp with a 3546 bp open reading frame coding for 1182 amino acid residues with a molecular mass of 130 kDa. It exhibits 77.5-80.9% identity at the mRNA level and 85.3-86.9% identity at the protein level with PMCA3 from human, mouse and rat. Membrane topography was typical of published mammalian PMCAs. Northern blot analysis of total RNA from crayfish gill, antennal gland,cardiac muscle and axial abdominal muscle revealed that a 7.5 kb species was ubiquitous. The level of PMCA3 mRNA expression in all tissues(transporting epithelia and muscle) increased significantly in pre/postmolt stages compared with relatively low abundance in intermolt. Western analysis confirmed corresponding changes in PMCA protein expression (130 kDa).</jats:p> Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfish<i>Procambarus clarkii</i>antennal gland during molting Journal of Experimental Biology |
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Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_unstemmed |
Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_full |
Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_fullStr |
Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_full_unstemmed |
Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_short |
Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_sort |
characterization and expression of plasma membrane ca2+ atpase(pmca3) in the crayfish<i>procambarus clarkii</i>antennal gland during molting |
| topic |
Insect Science Molecular Biology Animal Science and Zoology Aquatic Science Physiology Ecology, Evolution, Behavior and Systematics |
| url |
http://dx.doi.org/10.1242/jeb.01101 |
| publishDate |
2004 |
| physical |
2991-3002 |
| description |
<jats:title>SUMMARY</jats:title><jats:p>The discontinuous pattern of crustacean cuticular mineralization (the molting cycle) has emerged as a model system to study the spatial and temporal regulation of genes that code for Ca2+-transporting proteins including pumps, channels and exchangers. The plasma membrane Ca2+-ATPase (PMCA) is potentially of significant interest due to its role in the active transport of Ca2+ across the basolateral membrane, which is required for routine maintenance of intracellular Ca2+ as well as unidirectional Ca2+ influx. Prior research has suggested that PMCA expression is upregulated during periods of elevated Ca2+ influx associated with postmolt cuticular mineralization. This paper describes the cloning, sequencing and functional characterization of a novel PMCA3 gene from the antennal gland(kidney) of the crayfish Procambarus clarkii. The complete sequence,the first obtained from a non-genetic invertebrate species, was obtained through reverse transcription-polymerase chain reaction (RTPCR) and rapid amplification of cDNA ends (RACE) techniques. Crayfish PMCA3 consists of 4148 bp with a 3546 bp open reading frame coding for 1182 amino acid residues with a molecular mass of 130 kDa. It exhibits 77.5-80.9% identity at the mRNA level and 85.3-86.9% identity at the protein level with PMCA3 from human, mouse and rat. Membrane topography was typical of published mammalian PMCAs. Northern blot analysis of total RNA from crayfish gill, antennal gland,cardiac muscle and axial abdominal muscle revealed that a 7.5 kb species was ubiquitous. The level of PMCA3 mRNA expression in all tissues(transporting epithelia and muscle) increased significantly in pre/postmolt stages compared with relatively low abundance in intermolt. Western analysis confirmed corresponding changes in PMCA protein expression (130 kDa).</jats:p> |
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| author | Gao, Yongping, Wheatly, Michele G. |
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| description | <jats:title>SUMMARY</jats:title><jats:p>The discontinuous pattern of crustacean cuticular mineralization (the molting cycle) has emerged as a model system to study the spatial and temporal regulation of genes that code for Ca2+-transporting proteins including pumps, channels and exchangers. The plasma membrane Ca2+-ATPase (PMCA) is potentially of significant interest due to its role in the active transport of Ca2+ across the basolateral membrane, which is required for routine maintenance of intracellular Ca2+ as well as unidirectional Ca2+ influx. Prior research has suggested that PMCA expression is upregulated during periods of elevated Ca2+ influx associated with postmolt cuticular mineralization. This paper describes the cloning, sequencing and functional characterization of a novel PMCA3 gene from the antennal gland(kidney) of the crayfish Procambarus clarkii. The complete sequence,the first obtained from a non-genetic invertebrate species, was obtained through reverse transcription-polymerase chain reaction (RTPCR) and rapid amplification of cDNA ends (RACE) techniques. Crayfish PMCA3 consists of 4148 bp with a 3546 bp open reading frame coding for 1182 amino acid residues with a molecular mass of 130 kDa. It exhibits 77.5-80.9% identity at the mRNA level and 85.3-86.9% identity at the protein level with PMCA3 from human, mouse and rat. Membrane topography was typical of published mammalian PMCAs. Northern blot analysis of total RNA from crayfish gill, antennal gland,cardiac muscle and axial abdominal muscle revealed that a 7.5 kb species was ubiquitous. The level of PMCA3 mRNA expression in all tissues(transporting epithelia and muscle) increased significantly in pre/postmolt stages compared with relatively low abundance in intermolt. Western analysis confirmed corresponding changes in PMCA protein expression (130 kDa).</jats:p> |
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| spelling | Gao, Yongping Wheatly, Michele G. 1477-9145 0022-0949 The Company of Biologists Insect Science Molecular Biology Animal Science and Zoology Aquatic Science Physiology Ecology, Evolution, Behavior and Systematics http://dx.doi.org/10.1242/jeb.01101 <jats:title>SUMMARY</jats:title><jats:p>The discontinuous pattern of crustacean cuticular mineralization (the molting cycle) has emerged as a model system to study the spatial and temporal regulation of genes that code for Ca2+-transporting proteins including pumps, channels and exchangers. The plasma membrane Ca2+-ATPase (PMCA) is potentially of significant interest due to its role in the active transport of Ca2+ across the basolateral membrane, which is required for routine maintenance of intracellular Ca2+ as well as unidirectional Ca2+ influx. Prior research has suggested that PMCA expression is upregulated during periods of elevated Ca2+ influx associated with postmolt cuticular mineralization. This paper describes the cloning, sequencing and functional characterization of a novel PMCA3 gene from the antennal gland(kidney) of the crayfish Procambarus clarkii. The complete sequence,the first obtained from a non-genetic invertebrate species, was obtained through reverse transcription-polymerase chain reaction (RTPCR) and rapid amplification of cDNA ends (RACE) techniques. Crayfish PMCA3 consists of 4148 bp with a 3546 bp open reading frame coding for 1182 amino acid residues with a molecular mass of 130 kDa. It exhibits 77.5-80.9% identity at the mRNA level and 85.3-86.9% identity at the protein level with PMCA3 from human, mouse and rat. Membrane topography was typical of published mammalian PMCAs. Northern blot analysis of total RNA from crayfish gill, antennal gland,cardiac muscle and axial abdominal muscle revealed that a 7.5 kb species was ubiquitous. The level of PMCA3 mRNA expression in all tissues(transporting epithelia and muscle) increased significantly in pre/postmolt stages compared with relatively low abundance in intermolt. Western analysis confirmed corresponding changes in PMCA protein expression (130 kDa).</jats:p> Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfish<i>Procambarus clarkii</i>antennal gland during molting Journal of Experimental Biology |
| spellingShingle | Gao, Yongping, Wheatly, Michele G., Journal of Experimental Biology, Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting, Insect Science, Molecular Biology, Animal Science and Zoology, Aquatic Science, Physiology, Ecology, Evolution, Behavior and Systematics |
| title | Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_full | Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_fullStr | Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_full_unstemmed | Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_short | Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| title_sort | characterization and expression of plasma membrane ca2+ atpase(pmca3) in the crayfish<i>procambarus clarkii</i>antennal gland during molting |
| title_unstemmed | Characterization and expression of plasma membrane Ca2+ ATPase(PMCA3) in the crayfishProcambarus clarkiiantennal gland during molting |
| topic | Insect Science, Molecular Biology, Animal Science and Zoology, Aquatic Science, Physiology, Ecology, Evolution, Behavior and Systematics |
| url | http://dx.doi.org/10.1242/jeb.01101 |