Metallomics and the Cell pp 119-168

Part of the Metal Ions in Life Sciences book series (MILS, volume 12)

Intracellular Calcium Homeostasis and Signaling

Abstract

Ca2+ is a universal carrier of biological information: it controls cell life from its origin at fertilization to its end in the process of programmed cell death. Ca2+ is a conventional diffusible second messenger released inside cells by the interaction of first messengers with plasma membrane receptors. However, it can also penetrate directly into cells to deliver information without the intermediation of first or second messengers. Even more distinctively, Ca2+ can act as a first messenger, by interacting with a plasma membrane receptor to set in motion intracellular signaling pathways that involve Ca2+ itself. Perhaps the most distinctive property of the Ca2+ signal is its ambivalence: while essential to the correct functioning of cells, Ca2+ becomes an agent that mediates cell distress, or even (toxic) cell death, if its concentration and movements inside cells are not carefully tuned. Ca2+ is controlled by reversible complexation to specific proteins, which could be pure Ca2+ buffers, or which, in addition to buffering Ca2+, also decode its signal to pass it on to targets. The most important actors in the buffering of cell Ca2+ are proteins that transport it across the plasma membrane and the membrane of the organelles: some have high Ca2+ affinity and low transport capacity (e.g., Ca2+ pumps), others have opposite properties (e.g., the Ca2+ uptake system of mitochondria). Between the initial event of fertilization, and the terminal event of programmed cell death, the Ca2+ signal regulates the most important activities of the cell, from the expression of genes, to heart and muscle contraction and other motility processes, to diverse metabolic pathways involved in the generation of cell fuels.

Keywords

apoptosis calcium calcium buffering proteins calcium sensor proteins calmodulin fertilization gene expression ion pumps mitochondria protein dephosphorylation protein phosphorylation Please cite as: Met. Ions Life Sci. 12 (2013) 119–168 

Abbreviations

AMPA

2-amino-3-hydroxyl-5-ethyl-4-isoxazolepropionic acid

ATP

adenosine 5’-triphosphate

cADPR

cyclic adenosine diphosphate ribose

CaM

calmodulin

CaMK

calmodulin dependent kinase

cAMP

cyclic adenosine monophosphate

CaR

calcium receptor

CBD

Ca2+-binding domain

CICR

Ca2+-induced Ca2+ release

CRAC

Ca2+-release activated current

CREB

cAMP response element binding

DHPR

dihydropyridine receptor

DRE

downstream regulatory element

DREAM

downstream regulatory element

ER

endoplasmic reticulum

GA

Golgi apparatus

GABA

γ-amino butyric acid

GluR

glutamate receptor

IMM

inner mitochondrial membrane

IMS

intermembrane space

InsP3

inositol 1,4,5-trisphosphate

InsP3R

inositol 1,4,5-trisphosphate receptor

KA

kainate

MCO

mitochondrial Ca2+ overload

MCU

mitochondrial Ca2+ uniporter

MICU1

mitochondrial calcium uptake 1

MPT

mitochondrial permeability transition

NAADP

nicotinic acid adenine dinucleotide phosphate

NADP

nicotinamide adenosine diphosphate

NCLX

mitochondrial Na+/Ca2+ exchanger

NCX

Na+/Ca2+ exchanger

NFAT

nuclear factor of activated T cells

NHE

Na+/H+ exchanger

NMDA

N-methyl-D-aspartate

OMM

outer mitochondrial membrane

PC12

pheochromcytoma cells

PIP2

phosphatidylinositol 4,5-bisphosphate

PKA

protein kinase A

PKC

protein kinase C

PLC

phospholipase C

PM

plasma membrane

PMCA

plasma membrane Ca2+-ATPase

PTP

permeability transition pore

PV

parvalbumin

ROC

receptor operated Ca2+ channels

ROS

reactive oxygen species

RR

ruthenium red

RyR

ryanodine receptor

SERCA

sarco/endoplasmic reticulum Ca2+-ATPase

SLC

solute carrier

SNAP-25

synaptosomal-associated protein 25

SNARE

soluble NSF attachment protein receptor

SNP

single nucleotide polymorphism

SOCE

store operated Ca2+ entry channels

SPCA

secretory pathway Ca2+ ATPase

SR

sarcoplasmic reticulum

STIM

sensors stromal interaction molecule

TG

thapsigargin

TPC

two pore channel

TRP

transient receptor potential channels

VAMP

vesicle associate membrane protein

VOC

voltage operated Ca2+-channels

Copyright information

© Springer Science+Business Media Dordrecht 2013

Authors and Affiliations

  1. 1.Department of Comparative Biomedicine and Food SciencesUniversity of PadovaPadovaItaly
  2. 2.Department of Biomedical SciencesUniversity of PadovaPadovaItaly
  3. 3.Venetian Institute of Molecular Medicine (VIMM)PadovaItaly

Personalised recommendations