Localization of Plasma Membrane Ca2+Pump mRNA and Protein in Human Ameloblasts byIn SituHybridization and Immunohistochemistry
| Autor: | Maija I. Mednieks, James L. Borke, D. R. Eisenmann, Abd El-Moneim Zaki |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Cytoplasm
DNA Complementary Transcription Genetic ATPase Calcium-Transporting ATPases In situ hybridization Biochemistry Epithelium stomatognathic system Rheumatology Ameloblasts Animals Homeostasis Humans Orthopedics and Sports Medicine RNA Messenger Coloring Agents Molecular Biology Gene In Situ Hybridization Messenger RNA biology Cell Membrane Antibodies Monoclonal Cell Biology Immunohistochemistry Molecular biology Rats Gene Expression Regulation Genes biology.protein Plasma membrane Ca2+ ATPase Ameloblast Tooth Calcification Intracellular |
| Zdroj: | Connective Tissue Research. 33:139-144 |
| ISSN: | 1607-8438 0300-8207 |
| DOI: | 10.3109/03008209509016993 |
| Popis: | The distribution of the plasma membrane Ca(2+)-pump (PMCA) proteins in human ameloblasts was examined immunohistochemically using monoclonal antibodies JA8 and 5F10. Further, the distribution of mRNA transcripts derived from two PMCA genes, PMCA-1 and PMCA-4 was examined using in situ hybridization. In rats, the PMCA-1 gene is purported to code for PMCA proteins with a role in maintaining the intracellular Ca2+ levels in nonepithelial cells. Other genes including the PMCA-4 gene may code for PMCA proteins characteristic of Ca2+ transporting epithelia. The present results show immunohistochemical staining in the Tomes processes and plasma membranes of human ameloblasts. Our studies also demonstrate a gradation of expression of the PMCA-1 and PMCA-4 mRNA transcripts which parallels the onset and progression of enamel mineralization. These studies suggest that PMCA proteins in human ameloblasts may function both in intracellular Ca2+ homeostasis and in regulating the vectorial Ca2+ influx into mineralizing enamel. |
| Databáze: | OpenAIRE |
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