Functional characterization of alternatively spliced human SERCA3 transcripts
| Autor: | David H. MacLennan, Jonathan Lytton, Tasha Cacic, Esteban Poch, Susan Snape, Stephen Leach |
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| Rok vydání: | 1998 |
| Předmět: |
DNA
Complementary SERCA Transcription Genetic Physiology Molecular Sequence Data Sarcoplasm Calcium-Transporting ATPases Biology Endoplasmic Reticulum Kidney Cell Line Gene product Jurkat Cells Gene expression Humans Tissue Distribution Amino Acid Sequence RNA Messenger Endoplasmic reticulum Alternative splicing Cell Biology Blotting Northern Molecular biology Calcium ATPase Alternative Splicing Sarcoplasmic Reticulum Homeostasis Subcellular Fractions |
| Zdroj: | American Journal of Physiology-Cell Physiology. 275:C1449-C1458 |
| ISSN: | 1522-1563 0363-6143 |
| DOI: | 10.1152/ajpcell.1998.275.6.c1449 |
| Popis: | The sarcoplasmic (or endoplasmic) reticulum Ca2+-ATPase (SERCA)-3 has been implicated in the possible dysregulation of Ca2+homeostasis that accompanies the pathology of hypertension and diabetes. We report the molecular cloning of two alternatively spliced transcripts from the human SERCA3 gene, ATP2A3, that encode proteins that differ at their carboxy termini by 36 amino acids. SERCA3 transcripts were most abundantly expressed in lymphoid tissues, intestine, pancreas, and prostate. The two human SERCA3 proteins encoded by alternatively spliced transcripts were recognized by the monoclonal antibody PL/IM430 and demonstrated Ca2+uptake and ATPase activity with an apparent Ca2+affinity 0.5 pCa unit lower than that of other SERCA gene products. The subcellular distribution of SERCA3 protein was indistinguishable from that of SERCA2b, with expression in the nuclear envelope and in the endoplasmic reticulum throughout the cell. Two variant SERCA3 constructs, huS3-I and huS3-II, were isolated that encode proteins with three amino acid differences: Ala-673 (in huS3-I) substituted for Thr (in huS3-II), Ile-817 substituted for Met, and an insertion of Glu-994. huS3-I displayed a 10-fold lower capacity to transport Ca2+than huS3-II. |
| Databáze: | OpenAIRE |
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