> Chemicals & Drugs > Amino Acid > Metallothionein

Metallothionein

Metallothioneins are low-molecular-weight, cysteine-rich proteins that play a crucial role in the regulation of metal homeostasis and detoxification.
These proteins are found in a wide range of organisms, including mammals, plants, and microorganisms.
Metallothioneins can bind to and sequester heavy metals like zinc, copper, and cadmium, protecting cells from their toxic effects.
They are also involved in the cellular response to oxidative stress and inflammation.
Reserach on metallothionein is important for understanding metal-related diseases, developming therapeutic applications, and enhanceing environmental remediation efforts.

Most cited protocols related to «Metallothionein»

Cardiac Myocyte Isolation and Analysis

Cited 19 times

After ketamine/xylazine sedation, hearts were removed and perfused with Krebs-Henseleit bicarbonate (KHB) buffer containing (in mM): 118 NaCl, 4.7 KCl, 1.2 MgSO₄, 1.2 KH₂PO₄, 25 NaHCO₃, 10 HEPES and 11.1 glucose. Hearts were digested with collagenase D for 20 min. Left ventricles were removed and minced before being filtered. Myocyte yield was ∼ 75% which was not affected by high fat diet or metallothionein. Only rod-shaped myocytes with clear edges were selected for mechanical and intracellular Ca²⁺ study 11 (link).

Doser T.A., Turdi S., Thomas D.P., Epstein P.N., Li S.Y, & Ren J. (2009). Transgenic Overexpression of Aldehyde Dehydrogenase-2 Rescues Chronic Alcohol Intake-Induced Myocardial Hypertrophy and Contractile Dysfunction. Circulation, 119(14), 1941-1949.

Publication 2009

Bicarbonate, Sodium Collagenase Diet, High-Fat Glucose Heart HEPES Ion, Bicarbonate Ketamine Krebs-Henseleit solution Left Ventricles Metallothionein Muscle Cells Protoplasm Sedatives Sodium Chloride Sulfate, Magnesium Xylazine

Comprehensive Molecular Profiling of Astronaut Twins

Cited 10 times

The materials and methods are briefly summarized here; expanded materials and methods are included in the supplementary materials. Data were generated across human and microbial cells, including isolations of stool, saliva, skin, urine, blood, plasma, PBMCs, and immune cells that are CD4+, CD8+, and CD19+ enriched and lymphocyte-depleted (LD), from AutoMACS magnetic bead separation and validated by FACS (fig. S1). Molecular techniques included assessments of telomere length, telomerase activity, and chromosome aberration frequencies (qRT-PCR T:A, qRT-PCR TRAP, Telo-FISH, and dGH), WGBS, RNA-seq (polyA, riboRNA, and miRNA), mitochondrial quantification (qPCR and qRT-PCR), shotgun metagenome sequencing of fecal microbiome, targeted proteomics (LC-MS), untargeted proteomics (PECAN, MaxQuant for urine and SWATH-MS for plasma), targeted metabolomics (GC-MS), untargeted metabolomics (LC-MS), mitochondrial respiration (Seahorse XF), oxidative state measures (EPR), TCR and BCR (T cell and B cell receptor repertoire) profiling, 10 cognitive tests (motor praxis, visual object learning, fractal 2-back, abstract matching, line orientation, emotion recognition, matrix reasoning, digit symbol substitution, balloon analog risk, and psychomotor vigilance), vascular and ocular measures by ultrasound and optical coherence tomography, respectively, and a wide range of other biometrics (e.g., nutrition, height, and weight). Finally, a large set of biochemical profiles were measured pre-, in-, and postflight for both subjects: body mass, height, energy intake, vitamin levels (A, B6, B12, C, D, and E and 1-carbon metabolites), minerals (copper, ceruloplasmin, selenium, zinc, calcium, phosphorus, magnesium, and iodine), iron levels (ferritin, transferrin, transferrin receptors, Hgb, Hct, MCV, TIBC, and hepcidin), urine proteins (total, albumin, TTR, RBP, creatinine, metallothionein, 3-MH, nitrogen, and fibrinogen), bone markers (BSAP, PTH, OPG, RANKL, P1NP, sclerostin, and osteocalcin), collagen crosslinks (NTX, CTX, and DPD), oxidative stress and antioxidant capacity (8-OHdG, PGF2α, GPX, SOD, TAC, oxLDL, total lipid peroxides, heme, and glutathione), protein carbonyls (myeloperoxidase, lp-PLA2, neopterin, and beta-2 microglobulin), hormones and immune system markers (cytokines, testosterone, estradiol, DHEA/S, cortisol, IGF1, leptin, thyroid hormones, angiotensin, aldosterone, ANP, PRA, and insulin), and general urine chemistry (Na, K, and Cl ions; uric acid; cholesterol; triglyceride; HDL; LDL; phospholipids; renal stone risk; liver enzymes; hsCRP; NAD/P; and pH). Together, these data span 25 months for the flight subject twin (TW), who was compared with himself, either preflight, inflight, or postflight, and also with his twin control (HR) on Earth using generalized linear models (GLM), DESeq2, and fuzzy c-means clustering for longitudinal trends. All P values were corrected for multiple testing using a FDR of 0.05 or 0.01, and q values are reported in all tables.

Garrett-Bakelman F.E., Darshi M., Green S.J., Gur R.C., Lin L., Macias B.R., McKenna M.J., Meydan C., Mishra T., Nasrini J., Piening B.D., Rizzardi L.F., Sharma K., Siamwala J.H., Taylor L., Vitaterna M.H., Afkarian M., Afshinnekoo E., Ahadi S., Ambati A., Arya M., Bezdan D., Callahan C.M., Chen S., Choi A.M., Chlipala G.E., Contrepois K., Covington M., Crucian B.E., De Vivo I., Dinges D.F., Ebert D.J., Feinberg J.I., Gandara J.A., George K.A., Goutsias J., Grills G.S., Hargens A.R., Heer M., Hillary R.P., Hoofnagle A.N., Hook V.Y., Jenkinson G., Jiang P., Keshavarzian A., Laurie S.S., Lee-McMullen B., Lumpkins S.B., MacKay M., Maienschein-Cline M.G., Melnick A.M., Moore T.M., Nakahira K., Patel H.H., Pietrzyk R., Rao V., Saito R., Salins D.N., Schilling J.M., Sears D.D., Sheridan C.K., Stenger M.B., Tryggvadottir R., Urban A.E., Vaisar T., Van Espen B., Zhang J., Ziegler M.G., Zwart S.R., Charles J.B., Kundrot C.E., Scott G.B., Bailey S.M., Basner M., Feinberg A.P., Lee S.M., Mason C.E., Emmanuel M.i.g.n.o.t., Rana B.K., Smith S.M., Snyder M.P, & Turek F.W. (2019). The NASA Twins Study: A multidimensional analysis of a year-long human spaceflight. Science (New York, N.Y.), 364(6436), eaau8650.

Publication 2019

8-Hydroxy-2'-Deoxyguanosine Albumins Aldosterone Angiotensins Antioxidants BETA MICROGLOBULIN 2 BLOOD Blood Vessel Bones Calcium Carbon Cell Respiration Cells Ceruloplasmin Cholesterol Chromosome Aberrations Cognitive Testing Collagen Copper C Reactive Protein Creatinine Cytokine Dehydroepiandrosterone Sulfate Dinoprost Emotions Enzymes Estradiol Feces Ferritin Fibrinogen Fingers Fishes Gas Chromatography-Mass Spectrometry Glutathione Heme Hepcidin Homo sapiens Hormones Human Body Hydrocortisone IGF1 protein, human Insulin Iodine Ions Iron isolation Kidney Calculi Leptin Lipid Peroxides Liver Lymphocyte Magnesium Metagenome Metallothionein Microbiome MicroRNAs Minerals Mitochondria Neopterin Nitrogen Osteocalcin Oxidative Stress oxidized low density lipoprotein PAF 2-Acylhydrolase PAX5 protein, human Pecans Peroxidase Phospholipids Phosphorus Plasma Poly A procollagen Type I N-terminal peptide Proteins Receptors, Antigen, B-Cell RNA-Seq Saliva Seahorses Selenium Skin T-Lymphocyte Telomerase Telomere Testosterone Thyroid Hormones TNFSF11 protein, human Tomography, Optical Coherence Transferrin Transferrin Receptor Triglycerides Twins Ultrasonics Uric Acid Urine Vision Vitamins Wakefulness Zinc

Immunoprecipitation and Ubiquitination Assays for Cap-H2 and Plk4

Cited 7 times

Polyclonal anti-Slimb antibody was bound to equilibrated Protein A–coupled Sepharose (Sigma-Aldrich) by gently rocking overnight at 4°C in 0.2 M sodium borate. For GFP immunoprecipitations, GFP-binding protein (GBP; Rothbauer et al., 2008 (link)) was fused to the Fc domain of human IgG (pIg-Tail; R&D Systems), tagged with His₆ in pET28a (EMD Millipore), expressed in E. coli, and purified on Talon resin (Takara Bio Inc.) according to manufacturer’s instructions. GBP was bound to Protein A–coupled Sepharose, cross-linked to the resin using dimethyl pimelimidate, and rocked for 1 h at 22°C; the coupling reaction was then quenched in 0.2 M ethanolamine, pH 8.0, and rocked for 2 h at 22°C. Antibody or GBP-coated beads were washed three times with 1.5 ml of cell lysis buffer (CLB; 100 mM Tris, pH 7.2, 125 mM NaCl, 1 mM DTT, 0.1% Triton X-100, and 0.1 mM PMSF). Transfected S2 cells were induced to express recombinant Cap-H2 with 1–2 mM CuSO₄. After 24 h, transfected cells were lysed in CLB, clarified by centrifugation, and then diluted to 2–5 mg/ml in CLB. Antibody-coated beads were mixed with lysate for 40 min at 4°C, washed three times with CLB, and then boiled in Laemmli sample buffer. Lambda phosphatase (New England Biolabs, Inc.) treatments were performed for 1 h at 37°C. In vivo ubiquitination assays were performed by coexpressing Plk4-GFP (Rogers et al., 2009 (link)) or Cap-H2-GFP constructs with 3×FLAG–tagged Drosophila ubiquitin (CG32744), driven under the inducible metallothionein promoter pMT vector, immunoprecipitated using anti-GFP JL8 antibody, and analyzed by anti-FLAG immunoblotting.

Buster D.W., Daniel S.G., Nguyen H.Q., Windler S.L., Skwarek L.C., Peterson M., Roberts M., Meserve J.H., Hartl T., Klebba J.E., Bilder D., Bosco G, & Rogers G.C. (2013). SCFSlimb ubiquitin ligase suppresses condensin II–mediated nuclear reorganization by degrading Cap-H2. The Journal of Cell Biology, 201(1), 49-63.

Publication 2013

Antibodies, Anti-Idiotypic Binding Proteins Biological Assay Buffers Cells Centrifugation Claw Cloning Vectors dimethyl pimelimidate Drosophila Escherichia coli Ethanolamine Homo sapiens Immunoglobulins Immunoprecipitation Laemmli buffer Metallothionein Phosphoric Monoester Hydrolases Resins, Plant sodium borate Sodium Chloride Staphylococcal protein A-sepharose Tail TRAF3 protein, human Triton X-100 Tromethamine Ubiquitin Ubiquitination

Comprehensive Analysis of Salmon DNA Transposons

Cited 7 times

The starting point for this in silico analysis were the sequences for the two known salmon DNA transposons SALT1 [Genbank:L22865] [19 (link)] and Tss [Genbank:L12207] [18 (link)], as well as an analysis of the sequence of the T-cell receptor alpha locus of Salmo salar by RepeatMasker [46 ]. These two transposons as well as the RepeatMasker data were used to find faint similarities which were used in turn to find a larger number of each family in approximately 3 Mbp of sequence. The Dotter program [47 (link)] was used extensively to find regions of similar sequence, which were extracted and stored in an SQL database. The length of the transposon sequences was determined by identifying the inverted terminal repeat sequences where possible. Sequence alignments were performed with ClustalW [48 (link)] and phylogenetic trees generated with MEGA3.1 [49 (link)] using the Unweighted Pair Group Method with Arithmetic Mean (UPGMA), pairwise deletion, and a p-distance model. The entire alignment of the sequences was used in the phylogenetic reconstruction. Our salmon EST database was searched for the presence of sequences that are similar to the DNA transposon sequences that we found in salmon.
The following DNA sequences and BAC clones were used in this analysis. The Salmo salar TCRα locus [30 (link)], the major histocompatibility loci MHC class 1a and 1b [29 ], the growth hormone and interleukin loci (manuscripts in preparation), and zoneadhesin-like genes [Genbank:AY785950] and the Oncorhynchus mykiss sequences for the metallothionein gene [GENBANK:DQ156151], MHC1a [Genbank:AB162342] and MHC1b loci [Genbank:AB162343], and the IgH.A locus [Genbank:AY872256]. Genbank sequence entries were used in this study from a variety of other organisms (table 2): Oncorhynchus mykiss, Ictalurus punctatus, Esox lucius, Cyprinus carpio, Salvelinus namaycush, Salvelinus confluentus, Salvelinus fontinalis, Tanichthys albonus, Carassius auratus, Astatotilapia burtoni, Oryzias latipes, Petromyzon marinus, Danio rerio, Xenopus tropicalis, Xenopus laevis, Rana pipens, and Polypterus bichir. Sequences from Schistosoma japonicum EST Genbank data were found for transposon families as follows: DTSsa1 [Genbank:AY915112, AY809993], DTSsa2 [Genbank:AY816058, AY834394], DTSsa3 [Genbank:AY124772], DTSsa4 [Genbank:AY812589, AY915240], DTSsa5 [Genbank:AY813498], DTSsa6 [Genbank:AY813020], DTSsa7 [Genbank:AY813225, AY915121], SSTN1 [Genbank:AY809988, AY815476, AY915835], Tss [Genbank:AY915400, AY915891], and SALT1 [Genbank:AY223470, AY915102].
Representative sequences from all new families have been deposited in GenBank under accession numbers EF685954 – EF685960, EF685962 – EF685963, and EF685966 – EF685967.

de Boer J.G., Yazawa R., Davidson W.S, & Koop B.F. (2007). Bursts and horizontal evolution of DNA transposons in the speciation of pseudotetraploid salmonids. BMC Genomics, 8, 422.

Publication 2007

Catfishes, Channel Clone Cells Cyprinus carpio Deletion Mutation DNA Transposons Esox lucius Genes Goldfish Growth Hormone Interleukins Inverted Terminal Repeat Jumping Genes Metallothionein Oncorhynchus mykiss Oryzias latipes Petromyzon marinus Rana Salmo salar Salvelinus Schistosoma japonicum Sequence Alignment Sequence Analysis Syncope T Cell Receptor alpha Chain Genes Xenopus laevis Zebrafish

Constructing EB1-GFP and Msps-GFP Fusion Proteins

Cited 5 times

EB1::EB1-GFP was constructed by subcloning ∼1.5 kb of genomic DNA sequence 5′ of the EB1 gene in front of the 5′ start of EB1-GFP (Rogers et al., 2002 (link)). All fragments of Mini spindles were subcloned into a metallothionein promoter, pMT A vector backbone (Invitrogen) that contained a COOH-terminal fusion of TagRFP (a gift from Roger Tsien; Shaner et al., 2008 (link)). A previously described Msps construct (Lee et al., 2001 (link)) was used as a cDNA template, and all constructs were amplified by either Pfu or KOD polymerase (Novagen, Gibbstown, NJ). Full-length Msps-GFP was subcloned using the Gateway TopoD pEntr system (Invitrogen) into a final zeocin-selectable pIZ backbone (Invitrogen) that had both the metallothionein promoter and the Gateway (Invitrogen) LR recombination sites inserted into the multicloning site. Transfections were performed using the Amaxa Nucleofector II transfection system (Lonza, Basel, Switzerland) according to manufacturer's protocols. Constructs were induced 24 h after transfection with 40 μM copper sulfate for ∼12–18 h before imaging.

Currie J.D., Stewman S., Schimizzi G., Slep K.C., Ma A, & Rogers S.L. (2011). The microtubule lattice and plus-end association of Drosophila Mini spindles is spatially regulated to fine-tune microtubule dynamics. Molecular Biology of the Cell, 22(22), 4343-4361.

Publication 2011

Cloning Vectors DNA, Complementary DNA Sequence Genes Genome Metallothionein MST1 protein, human Recombination, Genetic Sulfate, Copper Transfection Vertebral Column Zeocin

Most recents protocols related to «Metallothionein»

Investigating HuR's Role in Metallothionein-Mediated Neuroprotection

This experimental approach was followed to investigate whether hur gene silencing leads to the impairment of metallothionein II (MT)-mediated neuroprotective properties in RGCs in a glaucoma model. For this purpose, 16 animals were divided into two groups: experimental (shRNA-HuR, n = 8) and control (shRNA-scramble control, n = 8) groups. All animals received an AAV injection into the right eye. Eight weeks after the AAV injection, we performed episcleral vein cauterization in the limbal area of the right eye to induce glaucoma. A decrease in the aqueous humor outflow to episcleral veins resulted in an elevated IOP. Simultaneously, following episcleral vein cauterization, rats from each group received an intravitreal injection of 1 μg/mL MT (3 μL per eye) into the right eye. The left eye was untreated. During the follow-up period, ERG measurements were performed. Animals were sacrificed after a follow-up time of 8 weeks, and the retina and optic nerves were processed for quantitative analyses of RGCs and axons, respectively.

Pacwa A., Machowicz J., Akhtar S., Rodak P., Liu X., Pietrucha-Dutczak M., Lewin-Kowalik J., Amadio M, & Smedowski A. (2023). Deficiency of the RNA-binding protein ELAVL1/HuR leads to the failure of endogenous and exogenous neuroprotection of retinal ganglion cells. Frontiers in Cellular Neuroscience, 17, 1131356.

Publication 2023

Animals Aqueous Humor Axon Cauterization Glaucoma Metallothionein Metallothionein II mutalipocin II Neuroprotection Optic Nerve Rattus norvegicus Retina Short Hairpin RNA Veins

Overexpression of Drosophila Ph Proteins

Drosophila S2 cells were procured from Expression Systems and were grown at 27°C in ESF921 media. Stable S2 cell lines overexpressing either PH-WT (BLRP-2XFLAG-Ph) or PH-ML (BLRP-2XFLAG-Ph-L1547/H1552R) under inducible metallothionein promoter were grown as described previously by Wani et al (32 (link)). Expression of PH in Drosophila S2 cells or cell lines expressing PH-WT or PH-ML was checked by immunoblotting using anti-FLAG and anti-PH antibodies (Figs 1 and S1). Given the duplicated nature of ph genes (ph-p and ph-d) and dominant negative nature of PH-ML mutation, overexpression strategy instead of CRISPR-Cas9 strategy was taken.

Amin A., Kadam S., Mieczkowski J., Ahmed I., Bhat Y.A., Shah F., Tolstorukov M.Y., Kingston R.E., Padinhateeri R, & Wani A.H. (2023). Disruption of polyhomeotic polymerization decreases nucleosome occupancy and alters genome accessibility. Life Science Alliance, 6(5), e202201768.

Publication 2023

Anti-Antibodies Cell Lines Cells Clustered Regularly Interspaced Short Palindromic Repeats Drosophila Figs Genes, Duplicate Metallothionein Mutation

Purification of sfGFP-BAF Fusion Proteins

Coding sequences of the sfGFP-BAF and sfGFP-BAF-A13T genes were inserted into the inducible metallothionein-promoter expression vector pMT/V5-HisC (Invitrogen). These transgenes encode inducible sfGFP-tagged constructs of BAF. Briefly, Drosophila S2 cells (Drosophila Genomics Resource Center, S2-DRSC) were cultured in Sf-900II SFM media (Life Technologies) as previously described [42 (link)]. Expression transgenes were transiently transfected into S2 cells by nucleofection (Nucleofector II, Amaxa), as previously described [42 (link)]. Cells were transfected with 2 μg of DNA, allowed 24 h of recovery, and then, gene expression was induced with the addition of 0.5 mM CuSO₄ for 48 h before harvesting for immunoprecipitation.
GFP-binding protein [GBP; [43 (link)]] was fused to the Fc domain of human IgG (pIgtail) (R&D Systems), tagged with His₆ in pET28a (EMD Biosciences), expressed in E. coli and purified on HisPur Cobalt resin (Fisher) according to the manufacturer’s instructions [44 (link)]. Purified His₆- GBP-Fc was bound to magnetic Protein A Dynabeads (ThermoFisher), and then covalently linked to the resin by incubation with 20 mM dimethyl pimelimidate in PBS, pH 8.3, for 2 h at room temperature. The coupling reaction was quenched with 0.2 M ethanolamine, pH 8.3, for 1 h at room temperature. GBP-coupled Dynabeads were stored in PBS, 0.1% Tween-20 at 4˚C. Prior to use, beads were equilibrated in IP buffer (50 mM Tris, pH 7.2, 125 mM NaCl, 1 mM DTT, 0.5% Triton X-100, 1 × SigmaFast protease inhibitors [Sigma], 0.1 mM PMSF, and 1 μg/mL SBTI). Drosophila S2 cells expressing sfGFP-BAF and sfGFP-BAF-A13T were harvested and lysed in IP buffer, the lysate concentrations determined by Bradford assay, and the lysates diluted to 5 mg/mL. Transfected cell lysates were not precleared when preparing samples for mass spectrometry. GBP-conjugated beads were rocked with clarified lysates for 30 min, 4 °C, washed four times by resuspending beads in 1 ml IP buffer, transferred to a new tube during the final wash, and then boiled in an equal volume of 2 × Laemmli sample buffer.

Duan T., Thyagarajan S., Amoiroglou A., Rogers G.C, & Geyer P.K. (2023). Analysis of a rare progeria variant of Barrier-to-autointegration factor in Drosophila connects centromere function to tissue homeostasis. Cellular and Molecular Life Sciences, 80(3), 73.

Publication 2023

Binding Proteins Biological Assay Buffers Cells Cloning Vectors Cobalt Culture Media dimethyl pimelimidate Drosophila Escherichia coli Ethanolamine Exons Gene Expression Genes Homo sapiens Immunoprecipitation Laemmli buffer Mass Spectrometry Metallothionein Protease Inhibitors Resins, Plant Sodium Chloride Staphylococcal Protein A Transgenes Triton X-100 Tromethamine Tween 20

Immunohistochemical Analysis of Heavy Metals

All chemicals and reagents were of analytical grade; zinc chloride (ZnCl₂) and cadmium chloride (CdCl₂) were purchased from Sigma-Aldrich (St Louis, MO, USA); Bcl-2, Ki-67, and metallothionein mouse specific HRP/DAB detection IHC kits were purchased from Abcam, UK. Hematoxylin and eosin (H&E) stain was provided by BDH Chemical Ltd., Poole, UK.

Bayram E.N., Al-Bakri N.A, & Al-Shmgani H.S. (2023). Zinc Chloride Can Mitigate the Alterations in Metallothionein and Some Apoptotic Proteins Induced by Cadmium Chloride in Mice Hepatocytes: A Histological and Immunohistochemical Study. Journal of Toxicology, 2023, 2200539.

Publication 2023

BCL2 protein, human Chloride, Cadmium Eosin Hematoxylin Metallothionein Mice, House zinc chloride

Characterization of Oat Metallothionein Genes

We have previously cloned three oat metallothionein partial cDNA sequences⁶⁶. Since then, the genome assembly of A. sativa has been published in the PanOat database (https://wheat.pw.usda.gov/GG3/PanOat)¹¹⁶. For each AsMT gene, a 1500-bp-long fragment of genomic DNA upstream of the start codon was retrieved from the PanOat database¹¹⁶. The promoters were analysed using the PlantCARE database^{117 (link)}. Molecular masses and pI of putative oat MT proteins were calculated using the Compute pI/Mw tool (ExPaSy)^{118 (link)}.

Konieczna W., Warchoł M., Mierek-Adamska A., Skrzypek E., Waligórski P., Piernik A, & Dąbrowska G.B. (2023). Changes in physio-biochemical parameters and expression of metallothioneins in Avena sativa L. in response to drought. Scientific Reports, 13, 2486.

Publication 2023

Codon, Initiator DNA, A-Form DNA, Complementary Genes Genome inter-alpha-inhibitor Metallothionein Triticum aestivum

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Effectene transfection reagent by Qiagen

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Fetal bovine serum (fbs) by Thermo Fisher Scientific

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Metallothionein by Abcam

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Metallothionein is a low molecular weight, cysteine-rich protein that functions in the regulation of metal homeostasis and the detoxification of heavy metals. It binds to and regulates the availability of essential metals, such as zinc and copper, while also sequestering toxic metals like cadmium, mercury, and lead.

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What are the different types or variations of Metallothionein?

Metallothioneins come in various isoforms and subtypes that are classified based on their amino acid sequence and metal-binding properties. The main types include MT-1, MT-2, MT-3, and MT-4, which are found in different tissues and serve distinct biological functions. Each type can also have multiple subtypes, providing a diverse range of Metallothionein proteins with specialized roles in metal regulation and cellular protection.

How can Metallothionein be used in therapeutic applications?

Metallothioneins have shown promise in therapeutic applications due to their ability to bind and detoxify heavy metals, as well as their anti-oxidant and anti-inflammatory properties. Researchers are exploring the use of Metallothionein supplementation or upregulation to treat metal-related disorders, mitigate the side effects of chemotherapy, and enhance neuroprotection. Additionaly, Metallothionein-based therapies are being investigated for their potential in treating neurodegenerative diseases, liver disease, and cancer.

What are some common challenges in working with Metallothionein?

One of the main challenges in working with Metallothionein is its small size and highly cysteine-rich nature, which can make it difficult to purify and characterize. Researchers may also face difficulties in accurately quantifying Metallothionein levels due to its dynamic expression and metal-binding properties. Additionally, the functional redundancy and overlapping roles of different Metallothionein isoforms can complicate the interpretation of experimental results.

How can PubCompare.ai help optimize Metallothionein research?

PubCompare.ai can assist in optimizing Metallothionein research in several ways. First, the platform allows you to efficiently screen the protocol literature to identify the most effective and reliable methods for working with Metallothionein, whether it's for purification, detection, or functional assays. Second, the AI-driven analysis provided by PubCompare.ai can help you pinpoint the critical insights that differentiate the protocols, enabling you to choose the best option for reproducibility and accuracy in your experiments. This can be particularly helpful when dealing with the challenges of working with this complex protein.

How does Metallothionein contribute to environmental remediation efforts?

Metallothioneins play a crucial role in environmental remediation efforts due to their ability to bind and sequester heavy metals. These proteins can be utilized in bioremediation strategies, such as the development of genetically engineered microorganisms or plants that overexpress Metallothionein to remove toxic metals from contaminated soils and water bodies. Additionally, Metallothionein-based biosensors are being explored for the detection and monitoring of heavy metal pollution in the environment. The unique metal-binding properties of Metallothionein make it a valuable tool in addressing environmental challenges related to metal contamination.

More about "Metallothionein"

Metallothioneins (MTs) are a class of low-molecular-weight, cysteine-rich proteins that play a crucial role in metal homeostasis and detoxification.
These versatile proteins are found in a wide range of organisms, including mammals, plants, and microorganisms.
MTs are known for their ability to bind and sequester heavy metals such as zinc, copper, and cadmium, protecting cells from their toxic effects.
Beyond their metal-binding capabilities, MTs are also involved in the cellular response to oxidative stress and inflammation.
This makes them an important area of study for understanding metal-related diseases, developing therapeutic applications, and enhancing environmental remediation efforts.
Researchers investigating MTs may utilize a variety of tools and techniques, such as Effectene Transfection Reagent for efficient gene delivery, Fetal Bovine Serum (FBS) for cell culture, Phusion polymerase for high-fidelity DNA amplification, and TaqMan Gene Expression Assays for sensitive and specific mRNA quantification.
Additionally, expression vectors like PMT/BiP/V5/His can be used to produce recombinant MT proteins, while TRIzol reagent can be employed for RNA extraction.
Optimization and reproducibility are key considerations when studying MTs, and resources like PubCompare.ai can help researchers identify the most reliable protocols from literature, preprints, and patents.
By leveraging AI-driven comparisons, scientists can enhance the accuracy and consistency of their MT-related experiments.
Whether you're exploring the fundamental biology of MTs, developing MT-based therapeutics, or working on environmental remediation projects, understanding the role of these remarkable proteins is crucial.
Stay up-to-date with the latest advancements in MT research and continue to push the boundaries of what's possible.