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Hippocalcin increases phospholipase D2 expression through extracellular signal-regulated kinase activation and lysophosphatidic acid potentiates the hippocalcin-induced phospholipase D2 expression by Doo-Yi Oh; Changsuek Yon; Kyoung-Jin Oh; Ki Sung Lee; Joong-Soo Han is a Biochemistry, Genetics and Molecular Biology article available to read on EtoBox.

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## Abstract We have previously isolated a 22 kDa protein from a rat brain which was found to be involved in activating phospholipsae D (PLD), and identified the protein as hippocalcin through sequence analysis. Nevertheless, the function of hippocalcin for PLD activation still remains to be resolved. Here, we proposed that hippocalcin was involved in extracellular signal‐regulated kinase (ERK)‐mediated PLD2 expression. To elucidate a role of hippocalcin, we made hippocalcin transfected NIH3T3 cells and showed that the expression of PLD2 and basal PLD activity were increased in hippocalcin transfected cells. We performed PLD assay with dominant negative PLD2 (DN‐PLD2) and hippocalcin co‐transfected cells. DN‐PLD2 suppressed increase of basal PLD activity in hippocalcin transfected cells, suggesting that increased basal PLD activity is due to PLD2 over‐expression. Hippocalcin is a Ca^2+^‐binding protein, which is expressed mainly in the hippocampus. Since it is known that lysophosphatidic acid (LPA) increases intracellular Ca^2+^, we investigated the possible role of hippocalcin in the LPA‐induced elevation of intracellular Ca^2+^. When the intracellular Ca^2+^ level was increased by

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It is typically read by researchers, students, and practitioners in Biochemistry, Genetics and Molecular Biology.

Author
Doo-Yi Oh; Changsuek Yon; Kyoung-Jin Oh; Ki Sung Lee; Joong-Soo Han
Publisher
John Wiley and Sons; Wiley (John Wiley & Sons); John Wiley & Sons Inc.; Wiley (ISSN 0730-2312)
Published
2005
Language
EN
Field
Biochemistry, Genetics and Molecular Biology (Life Sciences)