Neuronal Calcium Sensor Protein Visinin-like Protein-3 Interacts with Microsomal Cytochrome b5 in a Ca2+-dependent Manner

Oikawa, Kensuke; Kimura, Shoji; Aoki, Naoko; Atsuta, Yuji; Takiyama, Yumi; Nagato, Toshihiro; Yanai, Mitsuru; Kobayashi, Hiroya; Sato, Keisuke; Sasajima, Tadahiro; Tateno, Masatoshi

doi:10.1074/jbc.m312766200

Cited by 20 publications

(17 citation statements)

References 57 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…We recently showed that PLD can be activated by hippocalcin in the presence of Ca 21 , that hippocalcin is one of the major regulatory proteins in the Ca 21 -mediated PLD signaling pathway (Hyun et al, 2000), and that activation of hippocalcin by increasing intracellular Ca 21 is important in PLD2 expression and ERK activation (Oh et al, 2006). Several studies have also shown that hippocalcin interacts with neuronal apoptosis inhibitor protein (Lindholm et al, 2002) and cytochrome b5 (Oikawa et al, 2004). However, the role of hippocalcin remains unclear.…”

mentioning

confidence: 95%

A novel role of hippocalcin in bFGF‐induced neurite outgrowth of H19‐7 cells

Cho

Park

et al. 2008

J of Neuroscience Research

View full text Add to dashboard Cite

Hippocalcin is a Ca2+-binding protein that is expressed mainly in pyramidal nerve cells of the hippocampus. However, its functions and mechanism in the brain remain unclear. To elucidate the role of hippocalcin, we used a conditionally immortalized hippocampal cell line (H19-7) and showed that bFGF treatment increased the expression of hippocalcin during bFGF-induced neurite outgrowth of H19-7 cells. Overexpression of hippocalcin dramatically elongated neurites and increased the expression of basic helix-loop-helix transcription factor, that is, NeuroD without bFGF stimulation. Treatment of the cells with hippocalcin siRNA completely blocked bFGF-induced neurite outgrowth and NeuroD expression. bFGF stimulation resulted in activation of phospholipase C-gamma (PLC-gamma) and an increased level of intracellular Ca2+. Hippocalcin expression by bFGF stimulation was fully blocked by both the PLC-gamma inhibitor U73122 and BAPTA-AM, a chelator of intracellular Ca2+, suggesting that hippocalcin expression by bFGF is dependent on PLC-gamma and Ca2+. Moreover, both U73122 and BAPTA-AM completely blocked bFGF-induced neurite outgrowth and NeuroD expression. Taken together, these results suggest for the first time that bFGF induces hippocalcin expression in H19-7 cells through PLC-gamma activation, which leads to neurite outgrowth.

show abstract

mentioning

confidence: 95%

A novel role of hippocalcin in bFGF‐induced neurite outgrowth of H19‐7 cells

Cho

Park

et al. 2008

J of Neuroscience Research

View full text Add to dashboard Cite

show abstract

“…Recent studies have shown that hippocalcin interacts with the neuronal apoptosis inhibitor protein (NAIP) that is an antiapoptotic protein expressed by neuron [Lindholm et al, 2002]. Hippocalcin also binds other proteins, such as mitogen-activated protein kinase, MLK2 [Nagata et al, 1998], and cytochrome b5 [Oikawa et al, 2004]. Little is known about the function of hippocalcin, nevertheless hippocalcin suggests that it may be involved in Ca 2þ -dependent cellular signaling.…”

mentioning

confidence: 98%

Hippocalcin increases phospholipase D2 expression through extracellular signal‐regulated kinase activation and lysophosphatidic acid potentiates the hippocalcin‐induced phospholipase D2 expression

Yon

et al. 2005

J of Cellular Biochemistry

View full text Add to dashboard Cite

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 Ca2+-binding protein, which is expressed mainly in the hippocampus. Since it is known that lysophosphatidic acid (LPA) increases intracellular Ca2+, we investigated the possible role of hippocalcin in the LPA-induced elevation of intracellular Ca2+. When the intracellular Ca2+ level was increased by LPA, hippocalcin was translocated to the membrane after LPA treatment in hippocalcin transfected cells. In addition, treatment with LPA in hippocalcin transfected cells markedly potentiated PLD2 expression and showed morphological changes of cell shape suggesting that increased PLD2 expression acts as one of the major factors to cause change of cell shape by making altered membrane lipid composition. Hippocalcin-induced PLD2 expression potentiated by LPA in hippocalcin transfected cells was inhibited by a PI-PLC inhibitor, U73122 and a chelator of intracellular Ca2+, BAPTA-AM suggesting that activation of hippocalcin caused by increased intracellular Ca2+ is important to induce over-expression of PLD2. However, downregulation of PKC and treatment of a chelator of extracellular Ca2+, EGTA had little or no effect on the inhibition of hippocalcin-induced PLD2 expression potentiated by LPA in the hippocalcin transfected cells. Interestingly, when we over-express hippocalcin, ERK was activated, and treatment with LPA in hippocalcin transfected cells significantly potentiated ERK activation. Specific inhibition of ERK dramatically abolished hippocalcin-induced PLD2 expression. Taken together, these results suggest for the first time that hippocalcin can induce PLD2 expression and LPA potentiates hippocalcin-induced PLD2 expression, which is mediated by ERK activation.

show abstract

“…In wdl mice, there were no significant changes in the expression of several major common calcium-binding protein genes including Calb1, Calb2, and Pvalb. However, wdl mice did show cerebellar upregulation of the Ca 2+ -binding protein encoding genes Hpcal1 and Slc8a1 (Table 3), which are predominantly expressed in Purkinje cells [30,33]. It is interesting to note that two other Ca 2+ -binding protein genes, Nptx1 and Pclo, whose protein products are enriched in presynaptic plasma membranes [9], were downregulated in the mutant mice (Table 2).…”

Section: Discussionmentioning

confidence: 99%

Effects of carbonic anhydrase VIII deficiency on cerebellar gene expression profiles in the wdl mouse

Yan

Jiao

et al. 2007

Neuroscience Letters

View full text Add to dashboard Cite

Recently, the waddles (wdl) mouse was identified as a carbonic anhydrase VIII (Car8) mutant. The mutation is associated with marked deficiency of Car8, an inositol triphosphate receptor 1-binding protein expressed at high levels in cerebellar Purkinje cells. To help unravel the molecular aberrations contributing to motor dysfunction in wdl mice, cerebellar gene expression profiles were examined in the mutants and their wild-type littermates. Genes involved in signaling, cell division, zinc-ion binding, synapse integrity and plasticity were down-regulated in wdl mice. Several of the upregulated genes encode proteins that function in the Golgi apparatus which suggests that Car8 deficiency has important effects on synaptic vesicle formation and transport.

show abstract

Neuronal Calcium Sensor Protein Visinin-like Protein-3 Interacts with Microsomal Cytochrome b5 in a Ca2+-dependent Manner

Cited by 20 publications

References 57 publications

A novel role of hippocalcin in bFGF‐induced neurite outgrowth of H19‐7 cells

A novel role of hippocalcin in bFGF‐induced neurite outgrowth of H19‐7 cells

Hippocalcin increases phospholipase D2 expression through extracellular signal‐regulated kinase activation and lysophosphatidic acid potentiates the hippocalcin‐induced phospholipase D2 expression

Effects of carbonic anhydrase VIII deficiency on cerebellar gene expression profiles in the wdl mouse

Contact Info

Product

Resources

About