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Toxicology of Cadmium and Its Damage to Mammalian Organs

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Cadmium: From Toxicity to Essentiality

Part of the book series: Metal Ions in Life Sciences ((MILS,volume 11))

Abstract

The detrimental health effects of cadmium (Cd) were first described in the mid 19th century. As part of industrial developments, increasing usage of Cd has led to widespread contamination of the environment that threatens human health, particularly today. Rather than acute, lethal exposures, the real challenge in the 21st century in a global setting seems to be chronic low Cd exposure (CLCE), mainly from dietary sources. Ubiquity of Cd makes it a serious environmental health problem that needs to be thoroughly assessed because it already affects or will affect large proportions of the world’s population. CLCE is a health problem that affects increasingly organ toxicity, especially nephrotoxicity, without a known threshold, implying that there is currently no safe limit for CLCE. In this chapter, we summarize current knowledge on the sources of Cd in the environment, describe the entry pathways for Cd into mammalian organisms, sum up the major organs targeted by acute or chronic Cd exposure and review the impact of Cd on organ function and human health. We also aim to put early pioneering studies on Cd poisoning into perspective in the context of recent ground-breaking prospective long-term population studies, which link CLCE to leading causes of diseases in modern societies – cancer, diabetes, and cardiovascular diseases, and of state-of-the-art studies detailing cellular and molecular mechanisms of acute and chronic Cd toxicity.

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Abbreviations

ABCB1:

multidrug resistance protein 1

ABCC2:

multidrug resistance-associated protein 2

ABCC7:

cystic fibrosis transmembrane conductance regulator

ABCG2:

ATP-binding cassette sub-family G member 2; breast cancer resistance protein

AIF:

apoptosis-inducing factor

Akt:

protein kinase B

AMPK:

AMP-activated protein kinase

ANT:

adenine nucleotide translocase

ARFY:

Atherosclerosis Risk Factors in Female Youngsters

ATF6:

activating transcription factor 6

ATP:

adenosine 5'-triphosphate

ATSDR:

Agency for Toxic Substance and Disease Registry

b.w.:

body weight

Bak:

Bcl-2 homologous antagonist/killer

BAPTA:

1,2-bis(o-aminophenoxy)ethane-N,N,N',N'-tetraacetic acid

BAPTA-AM:

BAPTA acetoxymethyl ester

Bax:

Bcl-2–associated X protein

BBB:

blood-brain barrier

Bcl-2:

B-cell lymphoma 2

BCRP:

breast cancer resistance protein

CaMKII:

Ca2+/calmodulin-dependent protein kinase II

cAMP:

cyclic 3'-5'-adenosine monophosphate

CAT:

catalase

CC-16:

Clara-cell protein

CFTR:

cystic fibrosis transmembrane conductance regulator

cGMP:

cyclic 3'-5'-guanosine monophosphate

CHO:

Chinese hamster ovary

CHOP:

CCAAT/-enhancer-binding protein homologous protein

CLCE:

chronic low cadmium exposure

cMOAT:

canalicular multispecific organic anion transporter; multidrug resistance-associated protein 2

Cox-2:

cyclooxygenase-2

CREB:

cAMP response element-binding

CsA:

cyclosporin A

CTH:

adrenocorticotropic hormone

Cu-ZnSOD:

copper-zinc superoxide dismutase

Cys:

cysteine

DCT1:

divalent cation transporter 1

DMSA:

dimercaptosuccinic acid

DMT1:

divalent metal transporter 1

DNMT:

DNA methyltransferase

DTPA:

diethylenetriaminepentaacetate

EDTA:

ethylenediamine-N,N,N',N'-tetraacetate

EF-hand:

helix-loop-helix structural domain in calcium-binding proteins

EGFR:

epidermal growth factor receptor

EGTA:

ethyleneglycoltetraacetic acid

eIF2α:

eukaryotic translation initiation factor 2A

EMT:

epithelial-to-mesenchymal transition

EPO:

erythropoietin

ER:

endoplasmic reticulum

ERAD:

ER-associated degradation

ERK:

extracellular signal-regulated kinases

ESR:

electron spin resonance

ESRD:

end-stage renal disease

EU:

European Union

FAO:

Food and Agriculture Organization

Fas:

pro-apoptotic type-II transmembrane protein; CD95L

FPN1:

ferroportin 1

G1:

post-mitotic Gap 1 cell cycle phase

G2/M:

post-mitotic Gap 2 / mitosis cell cycle phases

GCLC:

glutamate cysteine ligase catalytic subunit

GFR:

glomerular filtration rate

GH:

growth hormone

GI:

gastrointestinal

G-protein:

guanosine 5'-triphosphate-binding protein

GPx:

glutathione peroxidase

GRP78:

glucose-regulated protein, 78kDa

GRP94:

glucose-regulated protein, 94kDa

GSH:

glutathione

GSK3β:

glycogen synthase kinase 3 beta

α-GST:

α-glutathione-S-transferase

His:

histidine

HMW:

high molecular weight

i.v.:

intravenous

IARC:

International Agency for Research on Cancer

IC50 :

half maximal inhibitory concentration

ICAM-1:

intercellular adhesion molecule 1

ICdA:

International Cadmium Association

IKK:

IκB kinase

IL:

interleukin

IMM:

inner mitochondrial membrane

IP3 :

inositol 1,4,5-trisphosphate

IRE1:

inositol-requiring enzyme 1

IREG1:

iron-regulated transporter 1; ferroportin 1

IκB:

inhibitor of NF-κB

JNK:

c-Jun N-terminal kinases

Keap1:

Kelch-like ECH-associated protein 1

Kim-1:

kidney injury molecule-1

K m :

Michaelis constant

LC3:

microtubule-associated protein 1 light chain 3

LD50 :

median (50%) lethal dose

LDH:

lactate dehydrogenase

LEF:

lymphoid enhancer factor-1 transcription factor

LMW:

low molecular weight

Lrp:

low-density-lipoprotein-related protein

MAPK:

mitogen activated protein kinase

MCU:

mitochondrial calcium uniporter

MDC:

monodansylcadaverine

MDCK:

Madin-Darby canine kidney (cells)

Mdm2:

murine double minute 2

MDR1:

multidrug resistance protein 1

MMP:

mitochondrial membrane potential

MnSOD:

manganese superoxide dismutase

MRL:

minimal risk level

MRP2:

multidrug resistance-associated protein 2

MT:

metallothionein

mTOR:

mammalian target of rapamycin

MTP1:

metal-transporter protein 1; ferroportin 1

MW:

molecular weight

NADPH:

nicotinamide adenine dinucleotide phosphate (reduced)

NAG:

N-acetyl-β-D-glucosamidase

NF-κB:

nuclear factor-κB

NGAL:

neutrophil gelatinase-associated lipocalin

NHANES III:

Third National Health and Nutrition Examination Survey

NO:

nitric oxide

NOS:

nitric oxide synthase

NRAMP2:

natural resistance-associated macrophage protein-2

Nrf2:

NF-E2-related factor 2

O\( _2^{\bullet - } \) :

superoxide anion

OMM:

outer mitochondrial membrane

ONOO– :

peroxinitrite anion

OSHA:

Occupational Safety & Health Administration from the US Dept. of Labor

p38:

p38 mitogen activated protein kinase

p53:

tumor suppressor protein 53

PARP:

poly (ADP-ribose) polymerase

PC:

phytochelatin

PERK:

protein kinase RNA-like endoplasmic reticulum kinase

PGF:

placental growth factor

PI3K:

phosphoinositide 3 kinase

PIP2 :

phosphatidylinositol 4,5-bisphosphate

PIP3 :

phosphatidylinositol (3,4,5)-triphosphate

PKA:

protein kinase A

PKC:

protein kinase C

PT:

proximal tubule

PTP:

permeability transition pore

Px:

peroxidase

Ras:

rat sarcoma proto-oncogene

RME:

receptor-mediated endocytosis

ROS:

reactive oxygen species

SERCA:

sarco/endoplasmic reticulum Ca2+-ATPase

SH:

sulfhydryl

Shh:

sonic Hedgehog

SOD:

superoxide dismutase

Sp1:

specificity protein 1 transcription factor

STAT3:

signal transducer and activator of transcription 3 transcription factor

TCF:

T-cell specific transcription factor 1

TNF-α:

tumor necrosis factor α

TRP:

transient receptor potential (channel)

TRPM7:

transient receptor potential malastatin 7 (channel)

TRPV5,6:

transient receptor potential vanilloid 5,6 (channel)

TSH:

thyroid-stimulating hormone

uNGAL:

urinary NGAL

UPR:

unfolded protein response

VDAC:

voltage-dependent anion channel

VE:

vascular endothelial

WHO:

World Health Organization

Wnt:

wingless/Int-1 signaling protein

XBP1:

X-box binding protein 1

ZIP:

Zrt-/Irt-like protein

ΔΨm:

mitochondrial membrane potential

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Acknowledgments

The authors acknowledge the scientific contributions of past and present coworkers, in particular Drs. M. Abouhamed, P. K. Chakraborty, J. M. Friedmann, C. Langelüddecke, and N. A. Wolff. Research in the laboratory is funded by The German Research Foundation (DFG) (grants FT345/8-1 to FT345/11-1) and the Centre for Biomedical Research and Training (ZBAF) at the University of Witten/Herdecke.

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    Frank Thévenod & Wing-Kee Lee

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Thévenod, F., Lee, WK. (2013). Toxicology of Cadmium and Its Damage to Mammalian Organs. In: Sigel, A., Sigel, H., Sigel, R. (eds) Cadmium: From Toxicity to Essentiality. Metal Ions in Life Sciences, vol 11. Springer, Dordrecht. https://doi.org/10.1007/978-94-007-5179-8_14

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