ZFIN ID: ZDB-PUB-150508-6
Hydrogen sulfide promotes calcium uptake in larval zebrafish
Kwong, R.W., Perry, S.F.
Date: 2015
Source: American journal of physiology. Cell physiology   309(1): C60-9 (Journal)
Registered Authors: Perry, Steve F.
Keywords: Calcium, ECaC, hydrogen sulfide, protein kinase, zebrafish
MeSH Terms:
  • Animals
  • Animals, Genetically Modified
  • Calcium/metabolism*
  • Cyclic AMP-Dependent Protein Kinases/antagonists & inhibitors
  • Cyclic AMP-Dependent Protein Kinases/metabolism
  • Cystathionine beta-Synthase/genetics
  • Cystathionine beta-Synthase/metabolism
  • Gene Knockdown Techniques
  • Hydrogen Sulfide/pharmacology*
  • Ion Transport
  • Larva/drug effects
  • Larva/metabolism
  • Morpholines/pharmacology*
  • Morpholinos/metabolism
  • Oligonucleotides, Antisense/metabolism
  • Organothiophosphorus Compounds/pharmacology*
  • Protein Kinase Inhibitors/pharmacology
  • Sodium-Potassium-Exchanging ATPase/metabolism
  • Sulfides/pharmacology*
  • Time Factors
  • Zebrafish/embryology
  • Zebrafish/genetics
  • Zebrafish/metabolism*
  • Zebrafish Proteins/antagonists & inhibitors
  • Zebrafish Proteins/genetics
  • Zebrafish Proteins/metabolism
PubMed: 25948733 Full text @ Am. J. Physiol. Cell Physiol.
Hydrogen sulfide (H2S) can act as a signalling molecule for various ion channels and/or transporters, however, little is known about its potential involvement in Ca(2+) balance. Using developing zebrafish (Danio rerio) as an in vivo model system, the present study demonstrated that acute exposure to H2S donors increased Ca(2+) influx at 4 days post fertilization (dpf) while chronic (3-day) exposure caused a rise in whole-body Ca(2+) levels. The mRNA expression of Ca(2+)-transport related genes was unaffected by H2S exposure, suggesting that post-transcriptional modifications were responsible for the altered rates of Ca(2+) uptake. Indeed, treatment of fish with the protein kinase A (PKA) inhibitor H-89 abolished the H2S-mediated stimulation of Ca(2+) influx, suggesting that H2S increased Ca(2+) influx by activating cAMP-PKA pathways. Cystathionine β-synthase (CBS) and cystathionine γ-lyase (CSE) are two key enzymes in the endogenous synthesis of H2S. Using an antisense morpholino knockdown approach, we demonstrated that Ca(2+) influx was reduced in CBSb- but not in CSE-deficient fish. Interestingly, the reduction in Ca(2+) influx in CBSb-deficient fish was observed only in fish that were acclimated to low Ca(2+) water (i.e., 25 µM Ca(2+); control: 250 µM Ca(2+)). Similarly, mRNA expression of cbsb but not cse was increased in fish acclimated to low Ca(2+) water. Results from whole-mount immunohistochemistry further revealed that CBSb was expressed in Na(+)/K(+)-ATPase-rich cells (NaR cells), which are implicated in Ca(2+) uptake in zebrafish larvae. Collectively, the present study suggests a novel role for H2S in promoting Ca(2+) influx, particularly in a low Ca(2+) environment.