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PubMed1998

Antioxidant activity of adrenergic agents derived from catechol.

The ability of adrenergic catechol derivatives, including dobutamine, dopamine, and isoproterenol, to inhibit lipid peroxidation was examined. All the catechol derivatives we tested strongly inhibited lipid peroxidation. Dobutamine was a more powerful inhibitor of iron-catalyzed lipid peroxidation than the other agents, suggesting that part of the antioxidant activity of dobutamine is due to chelating iron. In addition, the catechol derivatives scavenged not only diphenylpicrylhydrazyl (DPPH) free radicals, but also 2,2'-azinobis-(3-ethylbenzothiazoline-6-sulfonic acid) (ABTS) radical cations and 2,2'-azobis-(2-amidinopropane)-dihydrochloride (AAPH) peroxyl radicals, indicating that the antioxidative activities of these agents are evidently due to scavenging free radicals. However, the rate constant of these catechol derivatives in scavenging hydroxyl radicals was < 10(10) M(-1) sec(-1), suggesting that they may not protect against biological damage induced by hydroxyl radicals.

Adrenergic Agents↗
PubMed1997

Oxidation of 4-alkylphenols and catechols by tyrosinase: ortho-substituents alter the mechanism of quinoid formation.

Numerous phenols and catechols are known to be substrates for tyrosinase. While the catalytic mechanism of phenol oxidation by tyrosinase has been well studied, little work has been done to determine the influence of substituents on the reaction. In the present investigation, we explored the effects of changing substituents at the 2 and 6 position on the mechanism of tyrosinase-catalyzed oxidation of 4-allyl and 4-propylphenols and catechols. We have previously demonstrated that tyrosinase initially oxidizes hydroxychavicol (4-allyl-catechol) to an o-quinone (3,5-cyclohexadien-1,2-dione) which because of the relatively acidic protons in the benzyl position, readily isomerizes to the tautomeric p-quinone methide (4-allylidene-2,5-cyclohexadien-1-one, QM) (Bolton et al., 1994). We have confirmed through GSH trapping studies that oxidation of 4-allylphenol by tyrosinase yields the same o-quinone GSH conjugates as hydroxychavicol. In contrast, the presence of additional ortho substituents dramatically alters the mechanism of tyrosinase-catalyzed oxidation of 4-alkylphenols. For example, eugenol (4-allyl-2-methoxyphenol), which possesses 1 ortho-methoxy substituents, is not oxidized to a o-quinone or a QM. However, when both ortho o-quinones or QMs which may be selectively toxic to the malignant melanocyte. Although mammalian tyrosinase is much more substrate specific compared to the mushroom tyrosinase used in this study [42], it should be possible to identify compounds which are substrates for the mammalian form but are otherwise oxidatively stable. In order to develop such target compounds an improved understanding of substituent effects on tyrosinase-catalyzed oxidation of catechols and phenols is necessary. This should for the development of strategies for therapeutic compounds that are selectively toxic toward melanoma.

Basidiomycota↗
PubMed2000

Rostral ventrolateral medulla catechol involvement upon sino-aortic deafferentation: an in vivo voltammetric study.

Pharmacologically-induced hypertension engages few aminergic ventrolateral medullary cells. To further address this issue, reflex hypertension evoked by acute sino-aortic deafferentation was chosen as a model. Adrenergic rostral ventrolateral neurons were recorded with a continuous, catechol-specific tool, i.e. in vivo voltammetry. Controlled hypotension led to the expected increase in catechol signal in sham rats (n = 4) but not in deafferented (vagi, superior laryngeal and glossopharyngeal nerves) rats (n = 5). Thus, the central responsiveness to known stimuli remained intact in this preparation following acute sino-aortic deafferentation. However, acute sino-aortic deafferentation itself induced no increase in catechol signal (n = 4 or 5 respectively). No increase in catechol signal was, observed when deafferentation was performed a) under hyperoxic conditions (O2 = 100%, n = 5) b) by extensive deafferentation involving also the cervical sympathetic trunk under halothane (n = 5) c) upon restrictive deafferentation leaving the vagi intact under pentobarbital (n = 5) d) in decerebrate animals (n = 4). Adrenergic rostral ventrolateral medullary barosensitive bulbospinal neurons may be primarily involved during hypotension.

Afferent Pathways↗
PubMed2003

Photocatalytic oxidation and ozonation of catechol over carbon-black-modified nano-TiO2 thin films supported on Al sheet.

The photocatalytic activity of the carbon-black-modified nano-TiO2) (CB-TiO2) thin films was 1.5 times higher than that of TiO2 thin films in degrading Reactive Brilliant Red X-3B. Photocatalytic oxidation and ozonation of catechol over CB-TiO2 thin films supported on Al sheet was investigated. The experiments showed that ozone concentrations had an important effect on TOC removal. The combined photocatalysis with UV irradiation and ozonation (TiO2/UV/O3) process considerably increased TOC removal rate compared to combined photocatalysis with UV irradiation and oxygen oxidation (TiO2/UV/O2) process, ozonation alone (O3) process, combined ozonation and UV irradiation (UV/O3) process. The complete mineralization of catechol followed pseudo-zero-order kinetics dependent upon ozone (oxygen) concentration and indicated catechol concentration did not affect the kinetics during UV/O3 and TiO2/UV/O3 (O2) processes. The kinetic study showed that the rate constants in the complete mineralization of catechol with TiO2/UV/O3 are 1.32-1.80 times higher than that of UV/O3 with the same concentration of ozone. The rate constants are 2.56-5.36 times higher than the maximal rate constants of TiO2/UV/O2 and 4.68-9.8 times higher than the maximal rate constants of TiO2/UV.

Carbon↗
PubMed2001

Isozymes of Ipomoea batatas catechol oxidase differ in catalase-like activity.

The amino acid sequences of two isozymes of catechol oxidase from sweet potatoes (Ipomoea batatas) were determined by Edman degradation of BrCN cleavage fragments of the native protein and by sequencing of amplified cDNA fragments. Sequence alignment and phylogenetic analysis of plant catechol oxidases revealed about 80% equidistance between the two I. batatas catechol oxidases and approximately 40--60% to catechol oxidases of other plants. When H(2)O(2) was applied as substrate the 39 kDa isozyme, but not the 40 kDa isozyme, showed catalase-like activity. The structure of the 40 kDa isozyme was modeled on the basis of the published crystal structure of the 39 kDa isozyme [T. Klabunde et al., Nat. Struct. Biol. 5 (1998) 1084]. The active site model closely resembled that of the 39 kDa isozyme determined by crystallography, except for a mutation of Thr243 (40 kDa isozyme) to Ile241 (39 kDa isozyme) close to the dimetal center. This residue difference affects the orientation of the Glu238/236 residue, which is thought to be responsible for the catalase-like activity of the 39 kDa isozyme for which a catalytic mechanism is proposed.

Amino Acid Sequence↗
PubMed1996

DNA recovery and PCR quantification of catechol 2,3-dioxygenase genes from different soil types.

With the objective of monitoring xenobiotic degrading bacteria in soil, a method for rapid extraction of DNA from soil, amenable to amplification by PCR, was developed. The method was based on lysis by freeze-thawing and subsequent addition of sodium dodecyl sulfate (SDS), hexadecyltrimethylammonium bromide and proteinase K. The extraction method required 2 h and was tested on six different soils differing in organic content, water holding capacity and pH, including ones from which DNA extraction is difficult. DNA yields from the soils ranged from 6.1 to 54.0 micrograms of DNA per g soil. The efficiency and reproducibility of the DNA extraction method were evaluated by competitive PCR. The organic content in the soils was a major factor affecting the amount of obtained DNA amenable for amplification by PCR. A PCR primer-pair was designed on the basis of the known nucleotide sequences of several catechol 2,3-dioxygenase genes. The specificity of the primer-pair was demonstrated on different sequenced catechol 2,3-dioxygenase genes and on site-specific bacterial isolates from polycyclic aromatic hydrocarbon (PAH)-contaminated soil. The concentration of catechol 2,3-dioxygenase DNA in PAH-contaminated sediment undergoing an ex situ compost process was quantified by competitive PCR over a period of 16 weeks. The concentration of PAHs and catechol 2,3-dioxygenase DNA in the soil samples, was found to correlate.

Catechol 2,3-Dioxygenase↗
PubMed2003

The csbX gene of Azotobacter vinelandii encodes an MFS efflux pump required for catecholate siderophore export.

The csbX gene of Azotobacter vinelandii was regulated in an iron-repressible manner from a divergent promoter upstream of the catecholate siderophore biosynthesis (csb) operon and was predicted to encode an efflux pump of the major facilitator superfamily. Other proteins that were most similar to CsbX were encoded by genes found in the catecholate siderophore biosynthesis operons of Aeromonas hydrophila and Stigmatella aurantiaca. Inactivation of csbX resulted in 57-100% decrease in the amount of catecholates released when compared to the wild-type in iron-limited medium. CsbX was most important for the export of the high affinity chelator protochelin with the majority of the catecholates released by csbX mutants being the protochelin intermediates azotochelin and aminochelin.

Amino Acid Motifs↗
PubMed2002

Catalysis of catechol oxidation by metal-dithiocarbamate complexes in pesticides.

Dithiocarbamate (DTC)-based pesticides have been implicated in Parkinson's disease (PD) through epidemiological links to increased risk of PD, clinical reports of parkinsonism following occupational exposure to the DTC-based pesticide maneb, and experimental studies showing dopaminergic neurodegeneration with combined exposure of rats to maneb and paraquat. We hypothesize that the manganese-ethylene-bis-dithiocarbamate (MnEBDC) complex in maneb may produce oxidative stress by catalyzing catechol oxidation. We tested this hypothesis by performing a structure-function analysis of metal-EBDC and metal-diethyldithiocarbamate (DEDC) complexes of Mn2+, Zn2+, and Cu2+ to catalyze oxidation of N-acetyldopamine (NA-DA) and 3,4-dihydroxyphenylacetic acid (DP) in the presence and absence of N-acetylcysteine (NAC), a model of glutathione. Both Mn-DTCs retained the capacity of the parent ion to catalyze one-electron oxidation of NA-DA, but lost the ability to catalyze DP oxidation. Strikingly, while Zn2+ did not catalyze catechol oxidation, both Zn-DTCs catalyzed one-electron oxidation of NA-DA but not DP. While Cu2+ catalyzed oxidation of both catechols, Cu-DTCs were inert. Similar results were obtained with MnEBDC and dopamine or norepinephrine; however, zinc-ethylene-bis-dithiocarbamate was less efficient at catalyzing oxidation of these catechols. Our results point to the potential for manganese- and zinc-containing EBDC pesticides to promote oxidative stress in catecholaminergic regions of the brain.

Carbamates↗
PubMed2000

Influence of subchronic administration of catechol estrogens on the formation of reactive oxygen species in rat liver microsomes.

Metabolic pathways of estrogens are the formation of catechol estrogens (CE; 2- and 4-hydroxy-estrogens), redox cycling of CE and free radical generation, mediated through cytochrome P450 (P450) oxidase/reductase activity. In previous investigations subchronic administration of estrogens showed prooxidative and antioxidative activities in rat liver microsomes (BARTH et al. 1999). To find out whether or not catechol metabolites are responsible for prooxidative activity, we checked 2- and 4-hydroxy-estradiol (2OH-E2 and 4OH-E2) and the non-catechol metabolite 6alpha-hydroxy-estradiol (6alpha-OH-E2) for formation of reactive oxygen species in liver microsomes of 30-day-old male Wistar rats after 5 days treatment (1, 10 mg/kg b. wt. orally, once a day). The results were compared with those after treatment of the rats with estradiol (E2), estradiol valerate (E2V) and ethinylestradiol (EE2). In liver homogenates glutathione and lipid peroxides were determined, in microsomes NADPH-Fe++-stimulated lipid peroxidation (LPO), H2O2 generation and lucigenin (LUC) and luminol (LUM) amplified chemiluminescence (CL) were investigated. In liver 9000 x g supernatants monooxygenase activities were measured. The two catechol estrogens did not show any antioxidative activity, whereas 6alpha-OH-E2 significantly diminished lipid peroxides in the liver as well as LPO and LUM-CL in liver microsomes. Among estrogens, only EE2 showed antioxidative activity. Both CE inhibited ethoxycoumarin O-deethylation. Peroxidative activity as enhanced LUC-CL was found after 2OH-E2 (1 mg/kg b.wt.) and E2, but 10 times higher doses of both CE did not change LUC-CL. Microsomal H2O2 generation was enhanced by E2, E2V and both CE, not by 6alpha-OH-E2. The lower level of H2O2 enhancement caused by CE in comparison to E2 and E2V together with unchanged LUC-CL after high CE doses did not unequivocally prove the CE to be mainly responsible for the prooxidative activities of E2 and E2V in liver microsomes, at least in 30-day-old male rats. Unchanged GSH in the liver after CE administration supports this hypothesis.

Administration, Oral↗
PubMed2003

Reaction conditions for laccase catalyzed polymerization of catechol.

Poly(catechol) was synthesized in batch runs with laccase from Trametes versicolor (ATCC 200801). The polymerization reaction was conducted in a closed, temperature controlled system containing acetone and sodium acetate buffer for pH control. The effects of the solvent mixture, monomer (catechol), enzyme, medium pH and temperature on the polymerization rate were investigated with respect to initial reaction conditions and depletion rate of dissolved oxygen in the medium. Maximum initial reaction rate was attained with 10% (v/v) acetone-sodium acetate buffer at pH 5.0, 25 degrees C, 0.02 U/ml enzyme and 250 mg/l initial catechol and 10 mg/l dissolved oxygen. A general saturation enzyme kinetics response was observed for catechol substrate. Temperature rise supported the rate increase up to 45 degrees C, after which the rate tended to be stable due to a drop in dissolved oxygen concentration as well as enzyme instability.

Basidiomycota↗
PubMed2000

The 1.8 A crystal structure of catechol 1,2-dioxygenase reveals a novel hydrophobic helical zipper as a subunit linker.

BACKGROUND: Intradiol dioxygenases catalyze the critical ring-cleavage step in the conversion of catecholate derivatives to citric acid cycle intermediates. Catechol 1,2-dioxygenases (1, 2-CTDs) have a rudimentary design structure - a homodimer with one catalytic non-heme ferric ion per monomer, that is (alphaFe(3+))(2). This is in contrast to the archetypical intradiol dioxygenase protocatechuate 3,4-dioxygenase (3,4-PCD), which forms more diverse oligomers, such as (alphabetaFe(3+))(2-12). RESULTS: The crystal structure of 1,2-CTD from Acinetobacter sp. ADP1 (Ac 1,2-CTD) was solved by single isomorphous replacement and refined to 2.0 A resolution. The structures of the enzyme complexed with catechol and 4-methylcatechol were also determined at resolutions of 1.9 A and 1.8 A, respectively. While the characteristics of the iron ligands are similar, Ac 1,2-CTD differs from 3,4-PCDs in that only one subunit is used to fashion each active-site cavity. In addition, a novel 'helical zipper', consisting of five N-terminal helices from each subunit, forms the molecular dimer axis. Two phospholipids were unexpectedly found to bind within an 8 x 35 A hydrophobic tunnel along this axis. CONCLUSIONS: The helical zipper domain of Ac 1, 2-CTD has no equivalent in other proteins of known structure. Sequence analysis suggests the domain is a common motif in all members of the 1,2-CTD family. Complexes with catechol and 4-methylcatechol are the highest resolution complex structures to date of an intradiol dioxygenase. Furthermore, they confirm several observations seen in 3,4-PCDs, including ligand displacement upon binding exogenous ligands. The structures presented here are the first of a new family of intradiol dioxygenases.

Acinetobacter↗
PubMed2002

Oxidative damage shifts from lipid peroxidation to thiol arylation by catechol-containing antioxidants.

Catechol-containing antioxidants are able to protect against lipid peroxidation by nonenzymatic scavenging of free radicals with their catechol moiety. During their antioxidant activity, catechol oxidation products such as semiquinone radicals and quinones are formed. These oxidation products of 4-methylcatechol inactivate the GSH-dependent protection against lipid peroxidation and the calcium sequestration in liver microsomes. This effect is probably due to arylation by oxidation products of 4-methylcatechol of free thiol groups of the enzymes responsible for the GSH-dependent protection and calcium sequestration, i.e. the free radical reductase and calcium ATPase. It is concluded that a catechol-containing antioxidant might shift radical damage from lipid peroxidation to sulfhydryl arylation.

Animals↗
PubMed1999

End-column amperometric detection in capillary electrophoresis: influence of separation-related parameters on the observed half-wave potential for dopamine and catechol.

Capillary electrophoresis (CE) was coupled to a micro-electrode-based end-column amperometric detector. The influences of separation voltage, CE buffer concentration, and capillary-to-electrode distance on the observed hydrodynamic voltammetry of dopamine and catechol were studied using a separation capillary with an i.d. of 25 microns. It was found that an increased CE voltage, increased buffer concentration, or decreased capillary-to-electrode distance resulted in a positive shift of the observed half-wave potentials for both dopamine and catechol. At a constant separation current of 1.6 microA, the observed half-wave potential was found to increase with applied separation voltage. Furthermore, when experiments were carried out with a platinum quasi-reference electrode instead of a Ag/AgCl reference electrode, similar shifts in half-wave potential were observed. These results indicate that the observed shifts are an effect of the separation voltage rather than the separation current or a change in the reference potential. The characteristics of end-column detection with and without a fracture decoupler were compared. It was found that the effects of separation voltage, CE buffer concentration, and capillary-to-electrode distance were minimized by the use of a decoupling device. The observed half-wave potentials for dopamine and catechol were more positive when a CE capillary without a decoupler was employed compared to when a decoupler was used. Additionally, using the fracture decoupler, the observed half-wave potentials for both dopamine and catechol were approximately the same as when no CE voltage was applied (i.e., when the hydrodynamic voltammograms were recorded under flow injection conditions).

Catechols↗
PubMed1995

Resonance Raman studies of catecholate and phenolate complexes of recombinant human tyrosine hydroxylase.

Human tyrosine hydroxylase isoform 1 (hTH1) was expressed in Escherichia coli, purified as the apoenzyme, and reconstituted with iron. The resonance Raman spectra of hTH1 complexed with dopamine, noradrenaline, tyramine, and catechol have been studied and compared to those obtained for TH isolated from bovine adrenal glands or rat phaeochromocytoma tissue. A TH-phenolate complex is reported for the first time. Using dopamine selectively 18O-labeled in the 3-position or both 3- and 4-hydroxy positions, we have been able to assign unambiguously the origin of the low-frequency vibration bands: the band at 631 cm-1 involves the oxygen in the 4-position; the band at 592 cm-1 involves the oxygen in the 3-position, and the band around 528 cm-1 is shifted by both, suggesting a chelated mode vibration. A small shift of the 1275 cm-1 band and no shift of the 1320 cm-1 band were observed, showing that those two bands involve essentially ring vibrations of the catecholate moiety, rather than the C--O stretching vibration as previously suggested. The spectrum of the catechol-d6-hTH1 complex confirms this assignment. The resonance Raman spectra of the 54Fe, 56Fe, or 57Fe isotope-containing enzymes complexed with dopamine are virtually identical, showing that the component of the iron in the approximately 600 cm-1 vibrations is too small to be observed. These results provide a better understanding of the Raman properties of iron-catecholate complexes in this enzyme, as well as in other metalloproteins and model compounds.

Adrenal Gland Neoplasms↗
PubMed1985

Affinity-dependent cross-linking to neurotoxin sites of the acetylcholine receptor mediated by catechol oxidation.

The choline homologue 3-[(trimethylammonio)methyl]catechol (TMC) has been synthesized, and the controllable features of its complex oxidation have been examined spectroscopically and correlated with its toxin binding inactivating reactions with the acetylcholine receptor (AcChR) from Torpedo californica electroplax. Affinity-dependent reactions of early intermediates in the oxidation of TMC are suggested to intercede covalently in this inactivation. At pH 7.4, where the oxidative polymerization of catechols proceeds spontaneously, pyrocatechol produced no effect on the toxin binding function of AcChR, whereas comparable concentrations of TMC led to inactivation of half of all available sites. Lower concentrations of TMC converted via oxidation with ceric salts to an in situ mixture of monohydroxylated catechols were shown to be effective in short-term incubations in inactivating approximately half of the toxin binding sites by covalent labeling of the receptor. Mixtures of dihydroxycatechol intermediates, hydroxy-p-quinones, and polymeric products led to nonspecific toxin binding site inactivation of AcChR in excess of half of all available sites. Collectively, the results suggest that both covalent labeling and oxygen reduction product inactivating mechanisms are operative in these model macromolecular site reactions and that catechol-containing affinity reagents may be useful in elucidating the molecular features of sites to which they are directed.

Animals↗
PubMed2002

Substrate binding in catechol oxidase activity: biomimetic approach.

A series of dicopper(II) complexes have been investigated as model systems for the catechol oxidase active site enzyme, regarding the binding of catechol substrate in the first step of the catalytic cycle. The [Cu(2)(L(R))(mu-OH)](ClO(4))(2) and [Cu(2)(L(R))(H(2)O)(2)](ClO(4))(3) complexes are based on the L(R) ligands (2,6-bis[(bis(2-pyridylmethyl)amino)methyl]-4-R-substituted phenol) with -R = -OCH(3), -CH(3), or -F. Binding studies of diphenol substrates were investigated using UV-vis and EPR spectroscopy, electrochemistry, and (19)F NMR (fluorinated derivatives). All the complexes are able to bind two ortho-diphenol substrates (tetrachlorocatechol and 3,5-di-tert-butylcatechol). Two successive fixation steps, respectively fast and slower, were evidenced for the mu-OH complexes (the bis(aqua) complexes are inactive in catalysis) by stopped-flow measurement and (19)F NMR. From the mu-OH species, the 1:1 complex/substrate adduct is the catalytically active form. In relation with the substrate specificity observed in the enzyme, different substrate/inhibitor combinations were also examined. These studies enabled us to propose that ortho-diphenol binds monodentately one copper(II) center with the concomitant cleavage of the OH bridge. This hydroxo ligand appears to be a key factor to achieve the complete deprotonation of the catechol, leading to a bridging catecholate.

Binding Sites↗
PubMed2005

Quinone methide formations in the Cu(2+)-induced oxidation of a diterpenone catechol and concurrent damage on DNA.

Terpene quinone methides have been isolated from natural resources and exhibit broad biological activities against bacteria, fungi, and tumor cells through the reactive quinone methide (QM) moiety. The biological potential of the oxidation of terpene QM precursors, however, has not been assessed even though Cu(2+)-induced oxidation of catechol shows detrimental effects on cells. In this study, a diterpenone catechol was investigated as a precursor of terpene QM under aqueous conditions in the presence of Cu2+. Direct QM formation was implied in the Cu(2+)-induced oxidation through the study of thiol addition using HPLC and ESI-MS analysis. In addition, oxidation of the initial QM adduct to a second-QM intermediate was observed. The direct QM oxidation pathway may be unique for diterpenone catechol in the Cu(2+)-induced oxidation and is an addition to the reported isomerization pathway of o-quinones to QMs. The DNA damage by the Cu(2+)-induced oxidation of diterpenone catechol was assessed on a short duplex DNA target. Both direct DNA cleavage and nucleobase oxidation were observed extensively by in situ-generated hydroxyl radicals.

Catechols↗
PubMed2004

Metabolism of polychlorinated biphenyls by Gunn rats: identification and serum retention of catechol metabolites.

The tissue distributions of persistent metabolites of polychlorinated biphenyls (PCBs) in Wistar rats and homozygous uridine diphosphate glucuronosyltransferase (UGT) deficient Gunn rats exposed to 2,4,5,2',5'-pentachlorobiphenyl (CB101) and the commercial PCB mixture, Kanechlor-500 (KC500), were investigated. After exposure to CB101, four hydroxy and two methylsulfonyl (MeSO2) metabolites were detected in liver, lung, kidney, blood, and adipose tissues. One was identified as 3',4'-(OH)2-2,4,5,2',5'-pentaCB, which was retained selectively in the serum of Gunn rats. Comparative analysis of the metabolite profiles in both rat strains after exposure to KC500 showed higher formation ratios of several dihydroxy PCB metabolites in the liver of Gunn rats; major metabolites are the catechols from 2,5,3',4'-tetraCB, CB101, 2,3,6,3',4'-pentaCB, and 2,3,6,2',4',5'-pentaCB. Thus, Gunn rats effectively metabolized PCBs with 2,5- or 2,5,6-chlorine substitution to the 3,4-catechol, but less formed MeSO2 metabolites in the liver. Although both rat strains retained 4-OH-2,3,5,3',4'-pentaCB in serum, Gunn rats also retained the catechol PCBs, accounting for about 52% of the total phenolic PCBs. These results suggest that a lack of UGTs markedly alters the formation ratios and retention profiles of catechols and MeSO2 metabolites of PCBs.

Animals↗