Interactions of zinc- and redox-signaling pathways DOI Creative Commons
Christopher Hübner, Hajo Haase

Redox Biology, Journal Year: 2021, Volume and Issue: 41, P. 101916 - 101916

Published: Feb. 24, 2021

Zinc and cellular oxidants such as reactive oxygen species (ROS) each participate in a multitude of physiological functions. There is considerable overlap between the affected events, including signal transduction. While there no obvious direct connection zinc ROS, mainly because bivalent cation does not change its oxidation state biological systems, these are linked by their interaction with sulfur, forming remarkable triad zinc, protein thiols. First, binds to reduced thiols can be released upon oxidation. Thereby, redox signals translated into changes free concentration, which act signals. Second, affects several ways, directly well indirectly. A incorporating many interactions metallothionein (MT), rich cysteine capable binding up seven ions fully state. diminished after (partial) oxidation, while show increased reactivity absence bound metal ions. Adding still more complexity, MT promoter controlled (via regulatory transcription factor 1 (MTF-1)) nuclear erythroid 2-related 2 (NRF2)). Many signaling cascades that important for cell proliferation or apoptosis contain thiols, acting centers crosstalk zinc- redox-signaling. prominent example shared molecular targets ROS active site tyrosine phosphatases (PTP), activity being downregulated binding. Because also protects PTP form irreversible multi-faceted reciprocal interaction, illustrating redox-signaling intricately on multiple levels.

Language: Английский

The redox biology of redox-inert zinc ions DOI
Wolfgang Maret

Free Radical Biology and Medicine, Journal Year: 2019, Volume and Issue: 134, P. 311 - 326

Published: Jan. 6, 2019

Language: Английский

Citations

187
Zinc transporters and their functional integration in mammalian cells DOI Creative Commons
Taiho Kambe, KM Taylor, Dax Fu

et al.

Journal of Biological Chemistry, Journal Year: 2021, Volume and Issue: 296, P. 100320 - 100320

Published: Jan. 1, 2021

Zinc is a ubiquitous biological metal in all living organisms. The spatiotemporal zinc dynamics cells provide crucial cellular signaling opportunities, but also challenges for intracellular homeostasis with broad disease implications. transporters play central role regulating balance and subcellular distributions. discoveries of two complementary families mammalian (ZnTs ZIPs) the mid-1990s spurred much speculation on their selectivity functions. After decades research, we have arrived at biochemical description transport. However, vitro functions are fundamentally different from those cells, where directed to specific locations, engaged dedicated macromolecular machineries, connected diverse processes. Hence, molecular individual reshaped deeply integrated promote utilization chemistry perform enzymatic reactions, tune responsiveness pathophysiologic signals, safeguard homeostasis. At present, underlying mechanisms driving functional integration largely unknown. This knowledge gap has motivated shift research focus studies purified cell context locations protein interactions. In this review, will outline how been accumulated in-test-tube in-cell studies, highlighting new insights paradigm shifts our understanding basis transporter defining feature eukaryotic proteomes, populating zinc-binding proteins that encoded by ∼10% human genome (1Rosenzweig A.C. Metallochaperones: Bind deliver.Chem. Biol. 2002; 9: 673-677Abstract Full Text PDF PubMed Scopus (165) Google Scholar, 2Andreini C. Banci L. Bertini I. Rosato A. Counting zinc-proteins genome.J. Proteome Res. 2006; 5: 196-201Crossref (592) Scholar). While fundamental biology, it later addition proteomes after advent geochemical an ancient high-sulfide ocean modern oxidizing, sulfate-rich one (3Bekker Holland H.D. Wang P.L. Rumble 3rd, D. Stein H.J. Hannah J.L. Coetzee L.L. Beukes N.J. Dating rise atmospheric oxygen.Nature. 2004; 427: 117-120Crossref (922) 4Arnold G.L. Anbar A.D. Barling J. Lyons T.W. Molybdenum isotope evidence widespread anoxia mid-Proterozoic oceans.Science. 304: 87-90Crossref (447) release sulfide-bound provided bioavailability prompt burst innovation structures such as fingers consequences quickening diversification eukaryotes evolution (5Dupont C.L. Butcher Valas R.E. Bourne P.E. Caetano-Anolles G. History inferred through phylogenomic analysis structures.Proc. Natl. Acad. Sci. U. S. 2010; 107: 10567-10572Crossref (197) came expense increasing risk interference preexisting machineries evolved earlier. Accordingly, body harnesses potentially toxic spatially confined manner avoid cytotoxicity. organ level, highly enriched hippocampus neocortex region brain, prostate gland, islets Langerhans pancreas (6Kambe T. Matsunaga M. Takeda T.A. Understanding contribution function early secretory pathway.Int. Mol. 2017; 18 (2179)Crossref (26) These tissues accumulate abundant into pathways stored demand. total content submillimolar uneven distributions ranging picomolar range free cytosolic over 20 mM specialized vesicles (7Eide D.J. trafficking zinc.Biochim. Biophys. Acta. 1763: 711-722Crossref (582) 8Vinkenborg Nicolson T.J. Bellomo E.A. Koay M.S. Rutter G.A. Merkx Genetically FRET sensors monitor Zn2+ homeostasis.Nat. Methods. 2009; 6: 737-740Crossref (311) 9Bozym R.A. Thompson R.B. Stoddard A.K. Fierke C.A. Measuring exchangeable PC-12 using ratiometric fluorescence biosensor.ACS Chem. 1: 103-111Crossref (201) 10Dunn M.F. Zinc-ligand interactions modulate assembly stability insulin hexamer -- review.Biometals. 2005; 18: 295-303Crossref (196) 11Dodson Steiner insulin's biosynthesis.Curr. Opin. Struct. 1998; 8: 189-194Crossref (401) For example, pancreatic β-cells packaging, epithelial citrate production, mammary lactation (12Kelleher S.L. McCormick N.H. Velasquez V. Lopez tissues: Roles pancreas, prostate, gland.Adv. Nutr. 2011; 2: 101-111Crossref (187) selectively capture transport ions across membrane barriers control gradients various membranes. Mammalian belong (13Kambe Yamaguchi-Iwai Y. Sasaki R. Nagao Overview transporters.Cell Life 61: 49-68Crossref (320) Scholar): Transporter (ZnT) (14Palmiter R.D. Huang Efflux compartmentalization members SLC30 family solute carriers.Pflugers Arch. 447: 744-751Crossref (316) Scholar) Zrt, Irt-like Protein (ZIP) (15Jeong Eide SLC39 transporters.Mol. Aspects Med. 2013; 34: 612-619Crossref (236) Ten ZnT 14 ZIP homologs SLC30A1-10 SLC39A1-14 genes humans, respectively Common ability selective binding, bound ZnTs ZIPs transported opposite directions. efflux responsible removing excess cytoplasm, whereas uptake replenish (Fig. 1, A–C). stabilize concentration around homeostatic setpoint while enriching lumen compartments support zinc-dependent multisite localizations increase number protein–protein drive cross talks between array performing processes beyond organized hierarchy scales—from complexes up constitute physiology cells. review begin isolated illuminate coordination geometric arrangements binding residues confer bindings structural move or down membrane. In-cell further showcase distinct response environmental stimuli. next level integrations takes place which coordinate networks involved signaling, endoplasmic reticulum (ER) unfolded response, activation ectoenzymes pathway. involvement provides global pathophysiology. Finally, summarize existing loss-of-function (LOF) mutations polymorphisms clinical manifestations major diseases. Cells acquire variety transition elements including iron, zinc, copper, manganese, cobalt, nickel, molybdenum, tungsten, chromium, vanadium. metals may exist tightly forms metal-bound cofactors nucleic-acid-bound species, loosely association heterogeneous buffer. Biomolecules milieu extraordinary chelation capacity, probably containing high-affinity sites relative (16Finney L.A. O'Halloran T.V. Transition speciation cell: Insights ion receptors.Science. 2003; 300: 931-936Crossref (861) According Irving–Williams series divalent (17Irving H. Williams R.J.P. complexes.J. Soc. 1953; 637: 3192-3210Crossref (0) Scholar), copper would form most stable complexes, preferentially accumulating biomolecules if presented equal amounts test tube. organisms, acquired override intrinsic thermodynamic propensity selection enable metal-specific As such, essential aspect composition metallome safeguarding fidelity delivery right amount. directions mechanisms, common these overall zinc. raises question exploit select against other similar ions. unusual electron configuration [Ar]3d10. completely filled d-orbital renders redox-inert, its ionic fixed valence state +2. considered borderline soft-hard metal, being coordinated both sulfur atom cysteine nitrogen histidine (soft base ligands) carboxylate oxygen atoms aspartate glutamate (hard (18Vahrenkamp Why does nature use zinc--a personal view.Dalton Trans. 2007; : 4751-4759Crossref (106) Often, water molecules participate ligation particular conformations. some cases, molecule positively charged center reduces pKa 15.7 ∼7, generating hydroxide catalytically active species (19Baird Jr., T.T. Waheed Okuyama Sly W.S. Catalysis inhibition carbonic anhydrase IV.Biochemistry. 1997; 36: 2669-2678Crossref A d subshell marked preference tetrahedral geometry (20Laitaoja Valjakka Janis spheres structures.Inorg. 52: 10983-10991Crossref (117) dictated 18-electron rule (21Langmuir Types valence.Science. 1921; 54: 59-67Crossref (145) addition, penta- hexa-coordinated Zn(II) frequently found metalloenzymes inhibitors solvent each site broadly categorized (N) bond angles (N = 4), trigonal bipyramidal 5), octahedral geometries 6). Despite variability environments, affinity toward usually high μM pM metalloproteins (22Maret W. New perspectives environments proteins.J. Inorg. Biochem. 2012; 111: 110-116Crossref (122) 23Maret Li Coordination proteins.Chem. Rev. 109: 4682-4707Crossref (419) vectorial movements barrier. two-step process, chemical properties dictate metal-binding immediate surroundings afford selectivity. bacteria, archaea, 24Paulsen Saier M.J. novel heavy Membr. 156: 99-103Crossref 25Eide transporters.Pflugers 796-800Crossref (284) bacterial transporters, YiiP ZIPB, representative crystal determined and/or isomorphous Cd(II) 2, B). selectivities ZIPB explicitly determined, providing experimental correlating geometry. integral cytoplasmic Escherichia coli (26Grass Fan B. Rosen B.P. Franke Nies D.H. Rensing ZitB (YbgR), member cation diffusion facilitator family, additional coli.J. Bacteriol. 2001; 183: 4664-4667Crossref (119) It belongs (CDF) (27Montanini Blaudez Jeandroz Sanders Chalot Phylogenetic Cation Diffusion Facilitator family: Improved signature prediction substrate specificity.BMC Genomics. 107Crossref (226) was initially thought be ferrous iron based effects deletion trans-expression growth survival (28Grass Otto Fricke Haney C.J. Munkelt FieF (YiiP) mediates decreased accumulation relieves stress.Arch. Microbiol. 9-18Crossref (151) presence redundant systems compensatory controls could lead misinformation more rigorous determination developed direct measurements proteoliposomes mediated reconstituted proteins. spectrum substrates profiled inductively coupled plasma–mass spectrometry (ICP-MS), showing Cd(II), rejected fourth period (29Hoch E. Lin Chai Hershfinkel Fu Sekler Histidine pairing Cd2+ selectivity.Proc. 7202-7207Crossref (85) profile tube identical single-cysteine mutant native plasma (30Wei Selective membrane-embedded (FieF).J. 280: 33716-33724Abstract (70) genomic target selected large collection microbial homologs. bronchiseptica, thereby termed (31Lin Love electrodiffusion Zrt-, protein, ZIPB.J. 285: 39013-39020Abstract (66) ICP-MS transports rejects Fe(II), Cu(II), Co(II), Mn(II), Ni(II) Thus, shares YiiP. cadmium group-12 d-block fifth period, respectively. They outer configurations vary radii. appears features exploited Zn(II)/Cd(II) On hand, accommodation sizes 0.74 Å 0.97 demonstrates considerable fluidity size selection, making critical distinction size-based mechanism used channels discriminate s-block metals, potassium sodium (32Doyle D.A. Morais Cabral Pfuetzner Kuo Gulbis J.M. Cohen Chait B.T. MacKinnon structure channel: Molecular K+ conduction selectivity.Science. 69-77Crossref (5443) revealed Y-shaped dimeric architecture arranged twofold axis-oriented perpendicular plane (33Lu Structure YiiP.Science. 317: 1746-1748Crossref (268) 34Lu Structural autoregulation YiiP.Nat. 16: 1063-1067Crossref (162) 2A). cryo-EM oneidensis inward-facing conformation lipid environment (35Coudray N. Valvo Hu Lasala Kim Vink Zhou Provasi Filizola Tao Fang Penczek P.A. Ubarretxena-Belandia Stokes D.L. Inward-facing cryoelectron microscopy.Proc. 110: 2140-2145Crossref (64) 36Lopez-Redondo M.L. Coudray Zhang Z. Alexopoulos alternating access YiiP.Proc. 2018; 115: 3042-3047Crossref (25) 2C). Each protomer comprises N-terminal transmembrane domain (TMD) followed C-terminal (CTD) protrudes cytoplasm. Three were protomer. intramembranous site, known localized hydrophobic core TMD Side chains four conserved (D49, D53, H153, D157) projected antiparallel helices (TM2 TM5) classic Zn(II)/Cd(II)-binding Metal-binding isothermal titration calorimetry sub-μM 37Chao Thermodynamic YiiP.J. 279: 17173-17180Abstract (76) reaction 1.23 proton upon suggesting 1:1 Cd(II)-for-proton exchange (37Chao H153 sole proton-titratable residue under physiological pH range. act donor acceptor depending coordination. showed monomeric unit consisting eight (TMs) forming single helix bundle first TMs (TM1 TM4) approximately related last (TM5–TM8) (38Zhang Liu Fellner Sui Crystal reveal binuclear pathway.Sci. Adv. 3e1700344Crossref (51) 2B). intertwine embrace within inner four-helix stabilized peripheral fill inter-TM gaps. situated core, likely cocrystallized solved without back soaking partially replace yielding conformations occupied either trapped M1 M2, bridged (E181 E181 + E211) bidentate penta-coordinated M2 hexa-coordinated. Their primarily ligands located hexapeptides: "177HNhPEG182" "207QD/NhPEG212" (h refers residue) TM4 TM5, kinked P180 P210 properly multiple ligating residues. nested neighboring TMs, M99 TM2 E239 TM6, sphere. Of note, can closely associated 4.5-Å low-dielectric-constant show richly classical complex numbers 4 6. Carboxylate anions predominantly employed 1C). offers alternative modes monodentate bonds separate bridging residue. group rearrange coordinating gives flexibility sphere maintaining constant (39Sousa S.F. Fernandes Ramos enzymes: computational study.J. Am. 129: 1378-1385Crossref (120) accommodated virtue shared geometries, despite difference Although enzymes (40Vallee B.L. Auld D.S. coordination, function, proteins.Biochemistry. 1990; 29: 5647-5659Crossref (1452) occurs less sites. Nevertheless, plays proton-coupled pH-dependent acceptor. Cysteine another prevalent many (41Barber-Zucker Shaanan Zarivach correlation classification family.Sci. Rep. 7: 16381Crossref (39) Scholar); however, conspicuously missing ZIPB. Structure-guided discovery roles conserved, alanine substitutions quartets resulted loss activity 42Ohana Hoch Keasar Kambe Yifrach O. Identification mode operation transporter.J. 284: 17677-17686Abstract (129) functionally important. Moreover, DDHD quartet transporting HDHD only. H-to-D substitution raised barrier giving refined

Language: Английский

Citations

181
Zinc and Skin Disorders DOI Open Access
Youichi Ogawa, Manao Kinoshita, Shinji Shimada

et al.

Nutrients, Journal Year: 2018, Volume and Issue: 10(2), P. 199 - 199

Published: Feb. 11, 2018

The skin is the third most zinc (Zn)-abundant tissue in body. consists of epidermis, dermis, and subcutaneous tissue, each fraction composed various types cells. Firstly, we review physiological functions Zn transporters these Several human disorders accompanied with manifestations are caused by mutations or dysregulation transporters; acrodermatitis enteropathica (Zrt-, Irt-like protein (ZIP)4 intestinal epithelium possibly epidermal basal keratinocytes), spondylocheiro dysplastic form Ehlers-Danlos syndrome (ZIP13 dermal fibroblasts), transient neonatal deficiency (Zn transporter (ZnT)2 secretory vesicles mammary glands), epidermodysplasia verruciformis (ZnT1 keratinocytes). Additionally, acquired deeply involved development some diseases related to nutritional deficiencies (acquired enteropathica, necrolytic migratory erythema, pellagra, biotin deficiency), alopecia, delayed wound healing. Therefore, it important associate existence manifestations.

Language: Английский

Citations

173
Functionalization treatment of micro-arc oxidation coatings on magnesium alloys: a review DOI
Zhensheng Lin, Tianlin Wang, Xiaoming Yu

et al.

Journal of Alloys and Compounds, Journal Year: 2021, Volume and Issue: 879, P. 160453 - 160453

Published: May 21, 2021

Language: Английский

Citations

138
Interactions of zinc- and redox-signaling pathways DOI Creative Commons
Christopher Hübner, Hajo Haase

Redox Biology, Journal Year: 2021, Volume and Issue: 41, P. 101916 - 101916

Published: Feb. 24, 2021

Zinc and cellular oxidants such as reactive oxygen species (ROS) each participate in a multitude of physiological functions. There is considerable overlap between the affected events, including signal transduction. While there no obvious direct connection zinc ROS, mainly because bivalent cation does not change its oxidation state biological systems, these are linked by their interaction with sulfur, forming remarkable triad zinc, protein thiols. First, binds to reduced thiols can be released upon oxidation. Thereby, redox signals translated into changes free concentration, which act signals. Second, affects several ways, directly well indirectly. A incorporating many interactions metallothionein (MT), rich cysteine capable binding up seven ions fully state. diminished after (partial) oxidation, while show increased reactivity absence bound metal ions. Adding still more complexity, MT promoter controlled (via regulatory transcription factor 1 (MTF-1)) nuclear erythroid 2-related 2 (NRF2)). Many signaling cascades that important for cell proliferation or apoptosis contain thiols, acting centers crosstalk zinc- redox-signaling. prominent example shared molecular targets ROS active site tyrosine phosphatases (PTP), activity being downregulated binding. Because also protects PTP form irreversible multi-faceted reciprocal interaction, illustrating redox-signaling intricately on multiple levels.

Language: Английский

Citations

115