Organelles Containing Inositol Trisphosphate Receptor Type 2 in Adrenal Medullary Cells
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- Endo Yutaka
- Department of Cell and System Physiology, University of Occupational and Environmental Health School of Medicine
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- Harada Keita
- Department of Cell and System Physiology, University of Occupational and Environmental Health School of Medicine
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- Fujishiro Naoji
- Department of Cell and System Physiology, University of Occupational and Environmental Health School of Medicine
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- Funahashi Hisasachi
- Department of Anatomy, Showa University School of Medicine
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- Shioda Seiji
- Department of Anatomy, Showa University School of Medicine
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- Prestwich Glenn D.
- Department of Medical Chemistry, University of Utah
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- Mikoshiba Katsuhiko
- Division of Molecular Neurobiology, The Institute of Medical Science, The University of Tokyo
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- Inoue Masumi
- Department of Cell and System Physiology, University of Occupational and Environmental Health School of Medicine
Bibliographic Information
- Other Title
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- Organelles Containing Inositol Trisphosphate Receptor Type 2 in Adrenal Medullaly Cells
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Abstract
To identify which organelles contained inositol trisphosphate (InsP3) receptor type 2 (InsP3R2) in adrenal medullary (AM) cells, immunocytochemical and biochemical studies were performed on AM cells of several species. InsP3R2-like immunoreactive materials produced by two different anti-InsP3R2 antibodies (Abs) (Chemicon and Sigma) were distributed in rat AM cells in agreement with BODIPY-FL-InsP3 binding sites. For two other Abs (KM1083 and Santa Cruz), some of the anti-InsP3R2 immunoreactive materials were stained with an anti-dopamine-β-hydroxylase Ab, but not by BODIPY-FL-InsP3. BODIPY-FL-thapsigargin binding sites were consistent with a distribution of the endoplasmic reticulum (ER) identified by an anti-calnexin Ab, and a prior application of thapsigargin significantly eliminated BODIPY-FL-thapsigargin bindings, suggesting that BODIPY-FL-thapsigargin bindings were mediated by thapsigargin, but not the fluorescence molecule. The anti-InsP3R2 Ab that produced stainings consistent with BODIPY-FL-InsP3 bindings recognized a protein with about 250 kDa. A fractional analysis of bovine adrenal medullae revealed that the 250 kDa InsP3R2 was detected in a crude membrane fraction, but not in a secretory granule fraction. The results suggest that the InsP3R2 was present in the ER, but not in secretory granules in AM cells.<br>
Journal
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- The Journal of Physiological Sciences
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The Journal of Physiological Sciences 56 (6), 415-423, 2006
PHYSIOLOGICAL SOCIETY OF JAPAN
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Details
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- CRID
- 1390282680229004160
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- NII Article ID
- 10018493953
- 130004466867
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- NII Book ID
- AA12129145
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- ISSN
- 18806562
- 18806546
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- NDL BIB ID
- 8612970
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- Text Lang
- en
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- Data Source
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- JaLC
- NDL
- Crossref
- CiNii Articles
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- Abstract License Flag
- Disallowed