Molecular cloning and expression analysis of Bro-GS-elong and Bro-myro from Brassica oleracea

Dinkova-Kostova AT, Jenkins SN, Fahey JW, Ye L, Wehage SL, Liby KT, Stephenson KK, Wade KL and Talalay P (2006) Protection against UV-light-induced skin carcinogenesis in SKH-1 high-risk mice by sulforaphane-containing broccoli sprout extracts. Cancer Lett. Epub. 240: 243–252

Doares SH, Narvaez-Vasquez J, Conconi A, and Ryan CA (1995) Salicylic acid inhibits synthesis of proteinase inhibitors in tomato leaves induced by systemin and jasmonic acid. Plant Physiol. 108: 1741–1746

Doughty KJ, Kiddle GA, Pye BJ, Wallsgrove RM and Pickett JA (1995) Selective induction of glucosinolates in oilseed rape leaves by methyl jasmonate. Phytochemistry 38: 347–350

Engstrand L, Graham D, Scheynius A, Genta RM and El-Zaatari F (1997) Is the anctuary where Helicobacter pylori avoids antibacterial treatment intracellular? Am. J. Clin. Pathol. 108: 504–509

Fahey JW, Haristoy X, Dolan PM, Kensler TW, Scholtus I, Stephenson KK, Talalay P and Lozniewski A (2002) Sulforaphane inhibits extracellular, intracellular, and antibiotic-resistant strains of Helicobacter pylori and prevents benzo[a]pyrene-induced stomach tumors. Proc. Natl. Acad. Sci. 99: 7610–7615

Fahey JW and Talalay P (1999) Antioxidant functions of sulforaphane: a potent inducer of phase II detoxication enzymes. Food Chem. Toxicol. 37: 973–979

Felton G and Korth K (2000) Trade-offs between pathogen and herbivore resistance. Curr. Opin. Plant Biol. 3: 309–314

Gao X, Dinkova-Kostova AT and Talalay P (2001) Powerful and prolonged protection of human retinal pigment epithelial cells, keratinocytes, and mouse leukemia cells against oxidative damage: The indirect antioxidant effects of sulforaphane. Proc. Natl. Acad. Sci. 94(26): 15221–15226

Giamoustaris A and Mithen R (1996) Genetics of aliphatic glucosinolates. IV. Side-chain modification in Brassica oleracea. Theor. Appl. Genet. 93: 1006–1010

Gills JJ, Jeffery EH, Matusheski NV, Moon RC, Lantvit DD and Pezzuto JM (2006) Sulforaphane prevents mouse skin tumorigenesis during the stage of promotion. Cancer Lett. 236: 72–79

Grubb CD and Abel S (2006) Glucosinolate metabolism and its control. Trends Plant Sci. 11(2): 89–100

Howe GA (2004) The roles of hormones in defense against insects and disease; in Plant hormones: Biosynthesis, signal transduction, action! (Davies PJ ed.) Kluwer Academic Publishers. pp. 610–634

Kim SH and Hamada T (2005) Rapid and reliable method of extracting DNA and RNA from sweetpotato, Ipomoea batatas (L). Lam. Biotech. Lett. 27: 1841–1845

Koritsas VM, Lewis JA and Fenwick GR (1991) Glucosinolate responses of oil seed rape, mustard and kale to mechanical wounding and infestation by cabbage stem flea beetle (Psylliodes chuysocephala). Ann. Appl. Biol. 118: 209–221

Kroymann J, Textor S, Tokuhisa JG, Falk KL, Bartram S, Gershenzon J and Mitchell-Olds T (2001) A gene controlling variation in Arabidopsis glucosinolate composition is part of the methionine chain elongation pathway. Plant Physiol. 127: 1077–1088

Lenman M, Falk A, Xue J and Rask L (1993) Characterization of a Brassica napus myrosinase pseudogene: myrosinases are members of the BGA family of b-glycosidases. Plant Mol. Biol. 21: 463–474.

Magrath R, Bano F, Morgner M, Parkin I, Sharpe A, Lister C, Dean C, Turner J, Lydiate D and Mithen R (1994) Genetics of aliphatic glucosinolates. I. Side chain elongation in Brassica napus and Arabidopsis thaliana. Heredity 72: 290–299

Mewis I, Tokuhisa JG, Schultz JC, Appel HM, Ulrichs C and Gershenzon J (2006) Gene expression and glucosinolate accumulation in Arabidopsis thaliana in response to generalist and specialist herbivores of different feeding guilds and the role of defense signaling pathways. Phytochemistry 67: 2450–2462

Ohtsuru M, Hata T (1972) Molecular properties of multiple forms of plant myrosinase. Agric. Biol. Chem. 36: 2495–2503.

Sambrook J and Russell DW (2001) Molecular Cloning: A Laboratory Manual, 3rd ed., Cold Spring Harbor, New York

Sato K, Kawakami N, Ohtsu T, Tsutsumi A, Miyazaki S, Masumoto T, Horie S, Haratani T, Kobayashi F and Araki S (2004) Broccoli consumption and chronic atrophic gastritis among Japanese males: an epidemiological investigation. Acta Med. Okayama 58: 127–133

Pena-Cortes H, Fisahn J and Willmitzer L (1995) Signals involved in wound-induced proteinase inhibitor II gene expression in tomato and potato plants. Proc. Natl. Acad. Sci. USA 92: 4106–4113

Taipalensuu J, Falk A and Rask L (1996) A wound- and methyl jasmonate-inducible transcript coding for a myrosinase-associated protein with similarities to an early nodulin. Plant Physiol. 110: 483–491

Taipalensuu J, Andréasson E, Eriksson S and Rask L (1997) Regulationof the wound-induced myrosinase-associated protein transcript in Brassica napus plants. Eur. J. Biochem. 247: 963–971

Textor S, de Kraker JW, Hause B, Gershenzon J and Tokuhisa JG (2007) MAM3 catalyzes the formation of all aliphatic glucosinolate chain lengths in Arabidopsis. Plant Physiol. 144: 60–71

Thangstad OP, Winge P, Husebye H and Bones A (1993) The thioglucoside glucohydrolase (myrosinase) gene family in Brassicaceae. Plant Mol. Biol. 23: 511–524

Versalovic J and Fox JG (1999) In “Manual of Clinical Microbiology” (Murray PR, Baron EJ, Pfaller MA, Tenover FC, Yolken RH, eds). Am.Soc. Microbiol. pp. 727–738

Wittstock U and Halkier BA (2002) Glucosinolate research in the Arabidopsis era. Trends plant sci. 7(6): 263–270

Xue J, Jorgensen M, Pihlgren, U and Rask L (1995) The myrosinase gene family in Arabidopsis thaliana: gene organization, expression and evolution. Plant Mol. Biol. 27: 911–922

Yan X and Chen S (2007) Regulation of glucosinolate metabolism. Planta 226: 1343–1352

Zhang Y, Talalay P, Cho CG and Posner GH (1992) A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure. Proc. Natl. Acad. Sci. 89: 2399–2403

Zhang J, Pontoppidan B, Xue J, Rask L and Meijer J (2002) The third myrosinase gene TGG3 in Arabidopsis thaliana is a pseudogene specifically expressed in stamen and petal. Physiol. Plant. 115: 25–34