|CAS number||(±) , (+) , (-) , (+), hydrate|
|Jmol-3D images||Image 1|
|Molar mass||290.27 g mol−1|
|Melting point||175 to 177 °C (347 to 351 °F; 448 to 450 K)|
|Chiral rotation [α]D||+14.0°|
|Main hazards||Mutagenic for mammalian somatic cells, mutagenic for bacteria and/or yeast|
|LD50||(+)-catechin : 10,000 mg/kg in rat (RTECS)
10,000 mg/kg in mouse
3,890 mg/kg in rat (other source)
|Except where noted otherwise, data are given for materials in their standard state (at 25 °C (77 °F), 100 kPa)|
|(what is: / ?)|
Catechin // is a flavan-3-ol, a type of natural phenol and antioxidant. It is a plant secondary metabolite. It belongs to the group of flavan-3-ols (or simply flavanols), part of the chemical family of flavonoids.
- 1 Chemistry
- 2 History
- 3 Natural occurrences
- 4 Metabolism
- 5 Bioactivity studies
- 6 Health benefits
- 7 Ecological effects
- 8 Other uses
- 9 References
- 10 External links
Catechin possesses two benzene rings (called the A- and B-rings) and a dihydropyran heterocycle (the C-ring) with a hydroxyl group on carbon 3. The A ring is similar to a resorcinol moiety while the B ring is similar to a catechol moiety. There are two chiral centers on the molecule on carbons 2 and 3. Therefore, it has four diastereoisomers. Two of the isomers are in trans configuration and are called catechin and the other two are in cis configuration and are called epicatechin.
The most common catechin isomer is the (+)-catechin. The other stereoisomer is (-)-catechin or ent-catechin. The most common epicatechin isomer is (-)-epicatechin (also known under the names L-epicatechin, epicatechol, (-)-epicatechol, l-acacatechin, l-epicatechol, epi-catechin, 2,3-cis-epicatechin or (2R,3R)-(-)-epicatechin).
Making reference to no particular isomer, the molecule can just be called catechin. Mixtures of the different enantiomers can be called (+/-)-catechin or DL-catechin and (+/-)-epicatechin or DL-epicatechin.
Moreover, the flexibility of the C-ring allows for two conformation isomers, putting the B ring either in a pseudoequatorial position (E conformer) or in a pseudoaxial position (A conformer). Studies confirmed that (+)-catechin adopts a mixture of A- and E-conformers in aqueous solution and their conformational equilibrium has been evaluated to be 33:67.
Regarding the antioxidant activity, (+)-catechin has been found to be the most powerful scavenger between different members of the different classes of flavonoids. The ability to quench singlet oxygen seems to be in relation with the chemical structure of catechin, with the presence of the catechol moiety on ring B and the presence of a hydroxyl group activating the double bond on ring C.
Catechin exists in the form of a glycoside. Antioxidant properties can also be provided using a catechin associated with a sugar. In 1975-76, a group of USSR scientists of Kaz ssr discovered first the catechin rhamnoside using the plants of Filipendula that grow in that region. Pioneer and head of the discovery was PhD N. D. Storozhenko born in 1944. Though not thoroughly studied, the rhamnoside of catechin can enter the blood cell without breaking the outer layer.
Electrochemical experiments show that (+)-catechin oxidation mechanism proceeds in sequential steps, related with the catechol and resorcinol groups and the oxidation is pH-dependent. The oxidation of the catechol 3′,4′-dihydroxyl electron-donating groups occurs first, at very low positive potentials, and is a reversible reaction. The hydroxyl groups of the resorcinol moiety oxidised afterwards were shown to undergo an irreversible oxidation reaction.
|Extinction coefficient (log ε)||4.01|
|Major absorption bands||1600 cm−1(benzene rings)|
2.49 (1H, dd, J = 16.0, 8.6 Hz, H-4a),
|Other NMR data|
|ESI-MS [M+H]+ m/z : 291.0
(+)-Catechin and (-)-epicatechin as well as their gallic acid conjugates are ubiquitous constituents of vascular plants, and frequent components of traditional herbal remedies, such as the Chinese medicine plant Uncaria rhynchophylla and others. The two isomers are mostly associated with cacao and tea constituents, but (+)-catechin is also found in green algae such as Myriophyllum spicatum.
Catechin and Epicatechin can be found in cocoa. The different other enantiomers can as well be found in chocolate where the different processes of fabrication can lead to epimerisation by heating. The kola nut, a related species, contains epicatechin and D-catechin.
Açaí oil, obtained from the fruit of tha açaí palm (Euterpe oleracea), is rich in (+)-catechin (66.7 +/- 4.8 mg/kg). (-)-Epicatechin and (+)-catechin are along the main natural phenols in argan oil.
Unfermented green tea has perhaps the highest concentration of catechin content among naturally occurring foodstuffs, with about 27 percent of its makeup being catechins. Oolong tea has 23 percent, and black tea around 4 percent.
Levels of EC are concentrated in foods like raw apples, apricots, nectarines, pears and plums with skin, blackberries, red raspberries, cranberries, cherries and broad beans. Dark chocolate has approximately twice the amount of EC found in berries. Barley, raisins, red wine and rhubarb are also good sources of catechins.
The taste associated with monomeric (+)-catechin or (-)-epicatechin is described as not exactly astringent, nor exactly bitter. It is envisaged to encapsulate catechin in cyclodextrins to mask its taste to use it as an additive.
The biosynthesis of catechin begins with a 4-hydroxycinnamoyl CoA starter unit which undergoes chain extension by the addition of three malonyl-CoAs through a PKSIII pathway. 4-hydroxycinnamoyl CoA is biosynthesized from L-phenylalanine through the Shikimate pathway. L-phenylalanine is first deaminated by phenylalanine ammonia lyase (PAL) forming cinnamic acid which is then oxidized to 4-hydroxycinnamic acid by cinnamate 4-hydroyxylase. Chalcone synthase then catalyzes the condensation of 4-hydroxycinnamoyl CoA and three molecules of malonyl-CoA to form chalcone. Chalcone is then isomerized to naringenin by chalcone isomerase which is oxidized to eriodictyol by flavonoid 3’- hydroxylase and further oxidized to taxifolin by flavanone 3-hydroxylase. Taxifolin is then reduced by dihydroflavanol 4-reductase and leucoanthocyanidin reductase to yield catechin. The biosynthesis of catechin is shown below
Leucocyanidin reductase (LCR) uses 2,3-trans-3,4-cis-leucocyanidin to produce (+)-catechin and is the first enzyme in the proanthocyanidins (PA)-specific pathway. Its activity has been measured in leaves, flowers, and seeds of the legumes Medicago sativa, Lotus japonicus, Lotus uliginosus, Hedysarum sulfurescens, and Robinia pseudoacacia. The enzyme is also present in Vitis vinifera (grape).
Catechin oxygenase, a key enzyme in the degradation of catechin, is present in fungi and bacteria.
Among bacteria, degradation of (+)-catechin can be achieved by Acinetobacter calcoaceticus. Catechin is metabolized to protocatechuic acid (PCA) and phloroglucinol carboxylic acid (PGCA). It is also degraded by Bradyrhizobium japonicum. Phloroglucinol carboxylic acid is further decarboxylated to phloroglucinol, which is dehydroxylated to resorcinol. Resorcinol is hydroxylated to hydroxyquinol. Protocatechuic acid and hydroxyquinol undergo intradiol cleavage through protocatechuate 3,4-dioxygenase and hydroxyquinol 1,2-dioxygenase to form β-carboxy cis, cis-muconic acid and maleyl acetate.
In rats, all plasma catechin metabolites are present as conjugated forms and mainly constituted by glucuronidated derivatives. In the liver, the concentrations of catechin derivatives are lower than in plasma, and no accumulation is observed when the rats are adapted for 14 days to the supplemented diets. The hepatic metabolites are intensively methylated (90–95%), but in contrast to plasma, some free aglycones can be detected. Rats fed with (+)-catechin and (-)-epicatechin exhibit (+)-catechin 5-O-β-glucuronide and (-)-epicatechin 5-O-β-glucuronide in their body fluids. The primary metabolite of (+)-catechin in plasma is glucuronide in the nonmethylated form. In contrast, the primary metabolites of (-)-epicatechin in plasma are glucuronide and sulfoglucuronide in nonmethylated forms, and sulfate in the 3'-O-methylated forms (3'OMC). Catechin is absorbed into intestinal cells and metabolized extensively because no native catechin can be detected in plasma from the mesenteric vein. Mesenteric plasma contains glucuronide conjugates of catechin and 3'-O-methyl catechin, indicating the intestinal origin of these conjugates. Additional methylation and sulfation occur in the liver, and glucuronide or sulfate conjugates of 3'OMC are excreted extensively in bile. Circulating forms are mainly glucuronide conjugates of catechin and 3'OMC. Another study shows that catechin undergoes enzymatic oxidation by tyrosinase in the presence of glutathione (GSH) to form mono-, bi-, and tri-glutathione conjugates of catechin and mono- and bi-glutathione conjugates of a catechin dimer.
In the crab eating macaque Macaca iris, (+)-catechin administered orally or intraperitonally leads to the formation of 10 metabolites and notably to m-hydroxyphenylhydracrylic acid excreted in the urine.
In man, (+)-catechin absorbed orally is metabolized largely within 24 hours with the production of eleven metabolites detected in the urine.
(+)-Catechin and (-)-epicatechin are transformed by the endophytic filamentous fungus Diaporthe sp. into the 3,4-cis-dihydroxyflavan derivatives, (+)-(2R,3S,4S)-3,4,5,7,3',4'-hexahydroxyflavan (leucocyanidin) and (-)-(2R,3R,4R)-3,4,5,7,3',4'-hexahydroxyflavan, respectively, whereas (-)-catechin and (+)-epicatechin with a 2S-phenyl group resisted the biooxidation.
Leucoanthocyanidin reductase (LAR) uses (2R,3S)-catechin, NADP+ and H2O to produce 2,3-trans-3,4-cis-leucocyanidin, NADPH, and H+. Its gene expression has been studied in developing grape berries and grapevine leaves.
Catechin and epicatechin are the building blocks of the proanthocyanidins, a type of condensed tannin.
- (2R,3S)-Catechin-7-O-β-D-glucopyranoside can be isolated from barley (Hordeum vulgare L.) and malt.
- Epigeoside (Catechin-3-O-alpha-L-rhamnopyranosyl-(1-4)-beta-D-glucopyranosyl-(1-6)-beta-D-glucopyranoside) can be isolated from the rhizomes of Epigynum auritum.
Catechin is reported to induce longevity in the nematode worm Caenorhabditis elegans. Transcriptomic studies shows that catechin reduces atherosclerotic lesion development in apo E-deficient mice. (+)- and (−)-catechin seem to have stereospecific opposite effects on glycogen metabolism in isolated rat hepatocytes. (+)-Catechin inhibits intestinal tumor formation in mice. (+)-Catechin inhibits the oxidation of low density lipoprotein.
(-)-Catechin suppresses expression of Kruppel-like factor 7.
Catechin shows an enhancement of the antifungal effect of amphotericin B against Candida albicans.
Incubation experiments with (+)-catechin show a prevention of human plasma oxidation.
Interactions with human genes
PTGS2 (aka COX-2 for cyclooxygenase-2) is a dioxygenase. The presence of catechin seems to increase its expression.
IL1B induces the formation of cyclooxygenase-2 (PTGS2/COX2). Catechin increases its expression.
CAT is a catalase. Catechin decreases its expression.
CYP1A1 (Cytochrome P450, family 1, member A1) is an enzyme implied in the metabolism of xenobiotics. Catechin decreases its expression.
SOD (Superoxide dismutase) is an enzyme that catalyzes the dismutation of superoxide into oxygen and hydrogen peroxide. Catechin increases its expression.
BAX (Bcl-2–associated X protein) is a protein of the Bcl-2 gene family. It promotes apoptosis by competing with Bcl-2 proper. Catechin increases its expression.
CASP3 (Caspase 3) is a protein that plays a central role in the execution-phase of cell apoptosis. Catechin increases its expression.
MAPK1 (Mitogen-activated protein kinase 1) and MAPK3 (Mitogen-activated protein kinase 3) are enzymes that are extracellular signal-regulated kinases (ERKs) and act as an integration point for multiple biochemical signals, involved in a wide variety of cellular processes such as proliferation, differentiation, transcription regulation, and development. Catechin seems to increase their expression.
S100B (S100 calcium binding protein B) is a pro-inflammatory enzyme specific of mature astrocytes that ensheath the blood vessels. Catechin decreases the expression of the gene and could regulate S100B-activated oxidant stress-sensitive pathways through blocking p47phox protein expression. Treatment with catechin could eliminate reactive oxygen species (ROS) to reduce oxidative stress stimulated by S100B. Catechin decreases its expression.
Experiments on human Caco-2 cells show changes in the expression of genes like STAT1, MAPKK1, MRP1 and FTH1 genes, which are involved in the cellular response to oxidative stress, are in agreement with the antioxidant properties of catechin. In addition, the changes in the expression of genes like C/EBPG, topoisomerase 1, MLF2 and XRCC1 suggest novel mechanisms of action at the molecular level.
Detail for all tested genes :
(dec : decreased expression, inc : increased expression, = : does not affect the activity, expression assayed in human if not specified otherwise)
ABCG2 : (-)-catechin decreases the expression of ABCG2
ACE (in Rattus norvegicus) : (+)-catechin or (-)-epicatechin do not affect the activity of the angiotensin-converting enzyme
ACTB (in Rattus norvegicus) decrease
BAX (rattus norvegicus) increase
CAT (mus musculus) decrease
CYP19A1 (rattus norvegicus) increase
DFFA (mus musculus) decrease
MAP2K1 decrease ?
MAPK1 increase ?
MAPK3 increase ?
NOS2 (mus musculus) increase
PARP1 (mus musculus) increase
SOD (Drosophila melanogaster) increase
SOD2 (Drosophila melanogaster) increase
SULT1A1 increase : sulfation of catechin
Protection of the mouse brain before & after a stroke
Ninety minutes after feeding mice a single modest dose of epicatechin, a compound found naturally in dark chocolate, the scientists induced an ischemic stroke by, in essence, cutting off blood supply to the animals' brains. They found that the animals that had preventively ingested the epicatechin suffered significantly less brain damage than the ones that had not been given the compound. While most treatments against stroke in humans have to be given within a two- to three-hour time window to be effective, epicatechin appeared to limit further neuronal damage when given to mice 3.5 hours after a stroke. Given six hours after a stroke, however, the compound offered no protection to brain cells. A recent study shows that flavanol (-)-epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways.
Histidine decarboxylase inhibitor
(+)-Catechin is a histidine decarboxylase inhibitor. Thus, it inhibits the conversion of histidine to histamine, and, so, is thought to be beneficial through reduction of potentially damaging, histamine-related local immune response(s).
Monoamine oxidase inhibitor
Muscle fatigue resistance
Candidate therapeutic protective for HIV-associated neurocognitive disorders
The catechin family of compounds are strong therapeutic candidates for protection against the cognitive decline caused by HIV. Epicatechin, epigallocatechin gallate (EGCG) and other catechin flavonoids may protect against neurotoxic oxidative stress and caused by the HIV-Tat protein. Epicatechin is able to cross the blood-brain barrier more efficiently than resveratrol (which is more hydrophilic). It activates BDNF pathways.
Suppression heat-induced pain
Scientists have discovered that green tea extract could suppress heat-induced pain.
Catechin also has ecological functions.
It is released into the ground by some plants to hinder the growth of their neighbors, a form of allelopathy. Centaurea maculosa, the spotted knapweed, is the most studied plant showing this behaviour, catechin isomers, both released into the ground through its root exudates, have effects ranging from antibiotic to herbicide. It causes a reactive oxygen species wave through the target plant's root starting in the apical meristem rapidly followed by a Ca2+ spike that kills the root cells through apoptosis. Most plants in the European ecosystem have defenses against catechin, but few plants are protected against it in the North-American ecosystem where Centaurea maculosa has been introduced causing uncontrolled growth of this weed.
(+)-Catechin acts as an infection-inhibiting factor in strawberry leaf. Epicatechin and catechin may prevent coffee berry disease by inhibition of appressorial melanization of Colletotrichum kahawae.
It has been suggested that (+)-catechin could be used as a scavenger for indoor air pollutents such as volatile organic compounds (VOC) to adapt for instance as filters to air conditioners or to air purifiers.
- Zheng LT, Ryu GM, Kwon BM, Lee WH, Suk K (June 2008). "Anti-inflammatory effects of catechols in lipopolysaccharide-stimulated microglia cells: inhibition of microglial neurotoxicity". Eur. J. Pharmacol. 588 (1): 106–13. doi:10.1016/j.ejphar.2008.04.035. PMID 18499097.
- Rinaldo D, Batista JM, Rodrigues J, et al. (August 2010). "Determination of catechin diastereomers from the leaves of Byrsonima species using chiral HPLC-PAD-CD". Chirality 22 (8): 726–33. doi:10.1002/chir.20824. PMID 20143413.
- Kríz Z, Koca J, Imberty A, Charlot A, Auzély-Velty R (July 2003). "Investigation of the complexation of (+)-catechin by β-cyclodextrin by a combination of NMR, microcalorimetry and molecular modeling techniques". Org. Biomol. Chem. 1 (14): 2590–5. doi:10.1039/B302935M. PMID 12956082.
- Tournaire C, Croux S, Maurette MT, et al. (August 1993). "Antioxidant activity of flavonoids: Efficiency of singlet oxygen (1Δg) quenching". J. Photochem. Photobiol. B, Biol. 19 (3): 205–15. doi:10.1016/1011-1344(93)87086-3. PMID 8229463.
- Chumbalov, T. K.; Pashinina, L. T.; Storozhenko, N. D. (1976). "Catechin 7-rhamnoside fromSpiraea hypericifolia". Chemistry of Natural Compounds 12 (2): 232. doi:10.1007/BF00566356.
- Janeiro, Patricia; Oliveira Brett, Ana Maria (2004). "Catechin electrochemical oxidation mechanisms". Analytica Chimica Acta 518: 109. doi:10.1016/j.aca.2004.05.038.
- Lin, Yi-Pei; Chen, Tai-Yuan; Tseng, Hsiang-Wen; Lee, Mei-Hsien; Chen, Shui-Tein (2009). "Neural cell protective compounds isolated from Phoenix hanceana var. Formosana". Phytochemistry 70 (9): 1173–81. doi:10.1016/j.phytochem.2009.06.006. PMID 19628235.
- Freudenberg, Karl; Cox, Richard F. B.; Braun, Emil (1932). "The Catechin of the Cacao Bean1". Journal of the American Chemical Society 54 (5): 1913. doi:10.1021/ja01344a026.
- Adam, W. B.; Hardy, F.; Nierenstein, M. (1931). "The Catechin of the Cacao Bean". Journal of the American Chemical Society 53 (2): 727. doi:10.1021/ja01353a041.
- Nakai, S (2000). "Myriophyllum spicatum-released allelopathic polyphenols inhibiting growth of blue-green algae Microcystis aeruginosa". Water Research 34 (11): 3026. doi:10.1016/S0043-1354(00)00039-7.
- Pacheco-Palencia LA, Mertens-Talcott S, Talcott ST (June 2008). "Chemical composition, antioxidant properties, and thermal stability of a phytochemical enriched oil from Acai (Euterpe oleracea Mart.)". J. Agric. Food Chem. 56 (12): 4631–6. doi:10.1021/jf800161u. PMID 18522407.
- ., Z. Charrouf; ., D. Guillaume (2007). "Phenols and Polyphenols from Argania spinosa". American Journal of Food Technology 2 (7): 679. doi:10.3923/ajft.2007.679.683.
- Browning Potential, Phenolic Composition, and Polyphenoloxidase Activity of Buffer Extracts of Peach and Nectarine Skin Tissue. Guiwen W. Cheng and Carlos H. Crisosto, J. Amer. Soc. Hort. Sci., 1995, 120(5), pages 835-838, (article)
- Gálvez, Miguel Carrero; Barroso, Carmelo García; Pérez-Bustamante, Juan Antonio (1994). "Analysis of polyphenolic compounds of different vinegar samples". Zeitschrift für Lebensmittel-Untersuchung und Forschung 199 (1): 29–31. doi:10.1007/BF01192948.
- http://www.livestrong.com/article/478075-foods-high-in-catechins/[full citation needed]
- Phenolic Compounds of Barley Grain and Their Implication in Food Product Discoloration. Zory Quinde-Axtell and Byung-Kee Baik, J. Agric. Food Chem., 2006, volume 54, issue 26, pages 9978–9984, doi:10.1021/jf060974w
- Kielhorn, S; Thorngate Iii, J.H (1999). "Oral sensations associated with the flavan-3-ols (+)-catechin and (−)-epicatechin". Food Quality and Preference 10 (2): 109. doi:10.1016/S0950-3293(98)00049-4.
- Rani, Arti; Singh, Kashmir; Ahuja, Paramvir S.; Kumar, Sanjay (2012). "Molecular regulation of catechins biosynthesis in tea \Camellia sinensis (L.) O. Kuntze]". Gene 495 (2): 205–10. doi:10.1016/j.gene.2011.12.029. PMID 22226811.
- Punyasiri, P.A.N.; Abeysinghe, I.S.B.; Kumar, V.; Treutter, D.; Duy, D.; Gosch, C.; Martens, S.; Forkmann, G.; Fischer, T.C. (2004). "Flavonoid biosynthesis in the tea plant Camellia sinensis: Properties of enzymes of the prominent epicatechin and catechin pathways". Archives of Biochemistry and Biophysics 431 (1): 22–30. doi:10.1016/j.abb.2004.08.003. PMID 15464723.
- Dewick, Paul M. (2009). Medicinal Natural Products: A Biosynthetic Approach (3rd ed.). UK: John Wiley & Sons. ISBN 978-0-470-74167-2.[page needed]
- Skadhauge, Birgitte; Gruber, Margaret Y.; Thomsen, Karl Kristian; Von Wettstein, Diter (April 1997). "Leucocyanidin Reductase Activity and Accumulation of Proanthocyanidins in Developing Legume Tissues". American Journal of Botany 84 (4): 494–503. doi:10.2307/2446026. JSTOR 2446026.
- Maugé C, Granier T, d'Estaintot BL, et al. (April 2010). "Crystal structure and catalytic mechanism of leucoanthocyanidin reductase from Vitis vinifera". J. Mol. Biol. 397 (4): 1079–91. doi:10.1016/j.jmb.2010.02.002. PMID 20138891.
- Biodegradation of Catechin. M Arunachalam, M Mohan Raj, N Mohan and A Mahadevan, Proc. Indian natn Sci Acad. B69 No. 4 pp 353-370 (2003)
- Arunachalam, M; Mohan, N; Sugadev, R; Chellappan, P; Mahadevan, A (2003). "Degradation of (+)-catechin by Acinetobacter calcoaceticus MTC 127". Biochimica et Biophysica Acta (BBA) - General Subjects 1621 (3): 261. doi:10.1016/S0304-4165(03)00077-1.
- Hopper, Waheeta; Mahadevan, A. (1997). Biodegradation 8 (3): 159. doi:10.1023/A:1008254812074.
- Sambandam, T.; Mahadevan, A. (1993). "Degradation of catechin and purification and partial characterization of catechin oxygenase fromChaetomium cupreum". World Journal of Microbiology & Biotechnology 9: 37. doi:10.1007/BF00656513.
- Manach, Claudine; Texier, Odile; Morand, Christine; Crespy, Vanessa; Régérat, Françoise; Demigné, Christian; Rémésy, Christian (1999). "Comparison of the bioavailability of quercetin and catechin in rats". Free Radical Biology and Medicine 27 (11–12): 1259–66. doi:10.1016/S0891-5849(99)00159-8. PMID 10641719.
- Harada M, Kan Y, Naoki H, et al. (June 1999). "Identification of the major antioxidative metabolites in biological fluids of the rat with ingested (+)-catechin and (-)-epicatechin". Biosci. Biotechnol. Biochem. 63 (6): 973–7. doi:10.1271/bbb.63.973. PMID 10427682.
- Baba S, Osakabe N, Natsume M, Muto Y, Takizawa T, Terao J (November 2001). "In vivo comparison of the bioavailability of (+)-catechin, (-)-epicatechin and their mixture in orally administered rats". J. Nutr. 131 (11): 2885–91. PMID 11694613.
- Donovan JL, Crespy V, Manach C, et al. (June 2001). "Catechin is metabolized by both the small intestine and liver of rats". J. Nutr. 131 (6): 1753–7. PMID 11385063.
- Moridani MY, Scobie H, Salehi P, O'Brien PJ (July 2001). "Catechin metabolism: glutathione conjugate formation catalyzed by tyrosinase, peroxidase, and cytochrome p450". Chem. Res. Toxicol. 14 (7): 841–8. doi:10.1021/tx000235o. PMID 11453730.
- Das NP (1974). "Studies on flavonoid metabolism. Excretion of m-hydroxyphenylhydracrylic acid from (plus)-catechin in the monkey (Macaca iris sp.)". Drug Metab. Dispos. 2 (3): 209–13. PMID 4153081.
- Das NP (December 1971). "Studies on flavonoid metabolism. Absorption and metabolism of (+)-catechin in man". Biochem. Pharmacol. 20 (12): 3435–45. doi:10.1016/0006-2952(71)90449-7. PMID 5132890.
- Matsuda M, Otsuka Y, Jin S, et al. (February 2008). "Biotransformation of (+)-catechin into taxifolin by a two-step oxidation: primary stage of (+)-catechin metabolism by a novel (+)-catechin-degrading bacteria, Burkholderia sp. KTC-1, isolated from tropical peat". Biochem. Biophys. Res. Commun. 366 (2): 414–9. doi:10.1016/j.bbrc.2007.11.157. PMID 18068670.
- Osman, A.M.; Wong, K.K.Y.; Fernyhough, A. (2007). "The laccase/ABTS system oxidizes (+)-catechin to oligomeric products". Enzyme and Microbial Technology 40 (5): 1272. doi:10.1016/j.enzmictec.2006.09.018.
- Shibuya H, Agusta A, Ohashi K, Maehara S, Simanjuntak P (July 2005). "Biooxidation of (+)-catechin and (-)-epicatechin into 3,4-dihydroxyflavan derivatives by the endophytic fungus Diaporthe sp. isolated from a tea plant". Chem. Pharm. Bull. 53 (7): 866–7. doi:10.1248/cpb.53.866. PMID 15997157.
- Bogs J, Downey MO, Harvey JS, Ashton AR, Tanner GJ, Robinson SP (October 2005). "Proanthocyanidin synthesis and expression of genes encoding leucoanthocyanidin reductase and anthocyanidin reductase in developing grape berries and grapevine leaves". Plant Physiol. 139 (2): 652–63. doi:10.1104/pp.105.064238. JSTOR 4281902. PMC 1255985. PMID 16169968.
- Friedrich, Wolfgang; Galensa, Rudolf (2002). "Identification of a new flavanol glucoside from barley ( Hordeum vulgare L.) and malt". European Food Research and Technology 214 (5): 388. doi:10.1007/s00217-002-0498-x.
- Jin QD, Mu QZ (1991). "[Study on glycosidal constituents from Epigynum auritum]". Yao Xue Xue Bao (in Chinese) 26 (11): 841–5. PMID 1823978.
- Saul N, Pietsch K, Menzel R, Stürzenbaum SR, Steinberg CE (August 2009). "Catechin induced longevity in C. elegans: from key regulator genes to disposable soma". Mech. Ageing Dev. 130 (8): 477–86. doi:10.1016/j.mad.2009.05.005. PMID 19501612.
- Auclair, Sylvain; Milenkovic, Dragan; Besson, Catherine; Chauvet, Stéphanie; Gueux, Elyett; Morand, Christine; Mazur, Andrzej; Scalbert, Augustin (2009). "Catechin reduces atherosclerotic lesion development in apo E-deficient mice: A transcriptomic study". Atherosclerosis 204 (2): e21–7. doi:10.1016/j.atherosclerosis.2008.12.007. PMID 19152914.
- Nyfeler, Fritz; Moser, Ulrich K.; Walter, Paul (1983). "Stereospecific effects of (+)- and (−)-catechin on glycogen metabolism in isolated rat hepatocytes". Biochimica et Biophysica Acta (BBA) - Molecular Cell Research 763: 50. doi:10.1016/0167-4889(83)90024-1.
- Weyant MJ, Carothers AM, Dannenberg AJ, Bertagnolli MM (January 2001). "(+)-Catechin inhibits intestinal tumor formation and suppresses focal adhesion kinase activation in the min/+ mouse". Cancer Res. 61 (1): 118–25. PMID 11196148.
- Mangiapane H, Thomson J, Salter A, Brown S, Bell GD, White DA (February 1992). "The inhibition of the oxidation of low density lipoprotein by (+)-catechin, a naturally occurring flavonoid". Biochem. Pharmacol. 43 (3): 445–50. doi:10.1016/0006-2952(92)90562-W. PMID 1540202.
- Cho SY, Park PJ, Shin HJ, et al. (April 2007). "(-)-Catechin suppresses expression of Kruppel-like factor 7 and increases expression and secretion of adiponectin protein in 3T3-L1 cells". Am. J. Physiol. Endocrinol. Metab. 292 (4): E1166–72. doi:10.1152/ajpendo.00436.2006. PMID 17164435.
- Hirasawa M, Takada K (February 2004). "Multiple effects of green tea catechin on the antifungal activity of antimycotics against Candida albicans". J. Antimicrob. Chemother. 53 (2): 225–9. doi:10.1093/jac/dkh046. PMID 14688042.
- Lotito SB, Fraga CG (February 1998). "(+)-Catechin prevents human plasma oxidation". Free Radic. Biol. Med. 24 (3): 435–41. doi:10.1016/S0891-5849(97)00276-1. PMID 9438556.
- catechin on Comparative Toxicogenomics Database
- Noé V, Peñuelas S, Lamuela-Raventós RM, Permanyer J, Ciudad CJ, Izquierdo-Pulido M (October 2004). "Epicatechin and a cocoa polyphenolic extract modulate gene expression in human Caco-2 cells". J. Nutr. 134 (10): 2509–16. PMID 15465739.
- Catechin interactions with genes
- http://beforeitsnews.com/news/40184/Dark_Chocolate_Ingredient_Protects_the_Brain_After_a_Stroke_Say_John_Hopkins_Researchers.html[full citation needed]
- Chang CF, Cho S, Wang J (2014). "(-)-Epicatechin protects hemorrhagic brain via synergistic Nrf2 pathways.". Ann Clin Transl Neurol. 1 (4): 258–271. doi:10.1002/acn3.54. PMC 3984761. PMID 24741667.
- Reimann HJ, Lorenz W, Fischer M, Frölich R, Meyer HJ, Schmal A (March 1977). "Histamine and acute haemorrhagic lesions in rat gastric mucosa: prevention of stress ulcer formation by (+)-catechin, an inhibitor of specific histidine decarboxylase in vitro". Agents Actions 7 (1): 69–73. doi:10.1007/BF01964883. PMID 871094.
- Hou WC, Lin RD, Chen CT, Lee MH (August 2005). "Monoamine oxidase B (MAO-B) inhibition by active principles from Uncaria rhynchophylla". J Ethnopharmacol 100 (1–2): 216–20. doi:10.1016/j.jep.2005.03.017. PMID 15890481.
- Nogueira L, Ramirez-Sanchez I, Perkins GA, et al. (September 2011). "(-)-Epicatechin enhances fatigue resistance and oxidative capacity in mouse muscle". J. Physiol. (Lond.) 589 (Pt 18): 4615–31. doi:10.1113/jphysiol.2011.209924. PMC 3208228. PMID 21788351.
- Nath S, Bachani M, Harshavardhana D, Steiner JP (December 2012). "Catechins protect neurons against mitochondrial toxins and HIV proteins via activation of the BDNF pathway". J. Neurovirol. 18 (6): 445–55. doi:10.1007/s13365-012-0122-1. PMID 22886603.
- http://sciencelinks.jp/j-east/article/200707/000020070707A0194418.php[full citation needed]
- Secondary Metabolites and Allelopathy in Plant Invasions: A Case Study of Centaurea maculosa. Amanda K. Broz and Jorge M. Vivanco, 2006
- Bais HP, Vepachedu R, Gilroy S, Callaway RM, Vivanco JM (September 2003). "Allelopathy and exotic plant invasion: from molecules and genes to species interactions". Science 301 (5638): 1377–80. doi:10.1126/science.1083245. PMID 12958360.
- Yamamoto M, Nakatsuka S, Otani H, Kohmoto K, Nishimura S (June 2000). "(+)-catechin acts as an infection-inhibiting factor in strawberry leaf". Phytopathology 90 (6): 595–600. doi:10.1094/PHYTO.2000.90.6.595. PMID 18944538.
- Chen Z, Liang J, Zhang C, Rodrigues CJ (October 2006). "Epicatechin and catechin may prevent coffee berry disease by inhibition of appressorial melanization of Colletotrichum kahawae". Biotechnol. Lett. 28 (20): 1637–40. doi:10.1007/s10529-006-9135-2. PMID 16955359.
- Takano, Toshiyuki; Murakami, Tomomi; Kamitakahara, Hiroshi; Nakatsubo, Fumiaki (2008). "Mechanism of formaldehyde adsorption of (+)-catechin". Journal of Wood Science 54 (4): 329–31. doi:10.1007/s10086-008-0946-8.
|Look up Catechin or catechine in Wiktionary, the free dictionary.|