April Journal-2009.p65 - Association of Biotechnology and Pharmacy

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Current Trends in Biotechnology and Pharmacy Vol. 3 (2) 172-180, April 2009. ISSN 0973-8916 K. (2004). Characterization of á- glucosidase production from recombinant Aspergillus oryzae by membrane surface liquid culture in comparison with various cultivation methods. J. Biosci. Bioengg., 98 (3): 200-206, 29. Morita, H. and Fujio, Y. (1999). Polygalacturonase production of Rhizopus sp.MKU 18 using a metal ion regulated liquid medium. J. Gen. Appl. Microbiol., 45 (4): 199- 201. 30. Selvakumar, P., Ashakumary, L. and Pandey, A. (1996). Microbial synthesis of starch saccharifying enzyme in solid-state fermentation, J. Sci. Ind. Res., 55, 443-449. 31. Adams, P.R. (1981). Amylase production by Mucor pusillus and Humicola lanuginosa as related to mycelial growth. Biomed. Life Scien., 76 (2): 97-101. 32. Kamra, P. and Satyanarayana, T. (2004). Xylanase production by the thermophilic mold Humicola lanuginosa in solid-state fermentation. App. Biochem. Biotechnol., 119: 145-157. 33. Morinaga, T., Kanda, S. and Nori, R. (1986). Lipase production of a new thermophilic fungus, Humicola lanuginosa var. catenulate. J. Fermentation Technolo., 64 (5) : 451-453. 34. Miller, G.L. (1959). Use of dinitrosalicylic acid reagent for determination of reducing sugar. Anal. Chem, 31: 426-429. 35. Satyanarayana, T. (1994). Production of bacterial extracellular enzymes by solid-state fermentation, 122-129, In Pandey, A. (ed.) 180 solid-state fermentation, Wiley Eastern Limited, New Delhi. 36. Beckord, L.D., Kneen, E. and Lewis, K.H. (1945). Bacterial amylases production on wheat bran. Ind. Eng. Chem.,Ind. Ed., 37: 692-696. 37. Ellaiah, P., Adinarayana, K., Bhavani, Y., Padmaja, P. and Srinivasulu, B. (2002). Optimization of process parameters for glucoamylase production under solid-state fermentation by a newly isolated Aspergillus sp., Process Biochem., 38 (4): 615-620. 38. Pandey, A. (1990). Improvement in solid state fermentation for glucoamylase production. Biol. Wastes, 34: 11-19. 39. Feniksova, R.V., Tikhomirova, A.S. and Rakhleeva, E.E., (1960). Conditions for forming amylase and proteinase in surface cultures of Bacillus subtilis. Microbiologia, 29: 745-748. 40. Kashyap, P., Sabu, A., Pandey, A., Szakas, G. and Soccol, C.R. (2002). Extracellurar L-glutaminase production by Zygosaccharomyce rouxii under solid-state fermentation. Process Biochem., 38: 307-312. 41. Goto, C.E., Barbosa, E.P., Kistner, L.C.L., Gandra, R.F., Arrias, V.L. and Peralta, R.M. (1998). Production of amylase by Aspergillus fumigates. Revista de Microbiologia, 29: 99- 103. 42. Mukherjee, S.K. and Majomdar, S.K. (1993). Fermentative production of á-amylase by Aspergillus flavus, Indian J. Exp. Biol., 11: 436-438. Production of á-amylase
Current Trends in Biotechnology and Pharmacy Vol. 3 (2) 181-187, April 2009. ISSN 0973-8916 Association of CYP3A5*3 and CYP3A5*6 Polymorphisms with Breast Cancer Risk Surekha D, Sailaja K, Nageswara Rao D, Padma T, Raghunadharao D 1 and Vishnupriya S* Department of Genetics, Osmania University, Hyderabad, India 1 Department of Medical Oncology, Nizams Institute of Medical Sciences Hyderabad, India *For Correspondence - sattivishnupriya@gmail.com Abstract CYP3A5 gene is located on chromosome 7q21.1 and is responsible for the metabolism of over 50% of all clinically used drugs. 250 breast cancer and same number of healthy age matched controls were analyzed for the polymorphisms of CYP3A5*3 and CYP3A5*6 by polymerase chain reaction-restriction fragment length polymorphism. The normal wild type allele CYP3A5*1 produces correct transcript and individuals with at least one CYP3A5*1 allele can express CYP3A5 at higher levels. In the present study, the frequency of heterozygotes for CYP3A5*1 (1/3) was significantly increased in breast cancer (53.0%) when compared to controls (41.4%) with corresponding increase in CYP3A5*1 allele frequency. The frequency of 3/3 genotype was increased in postmenopausal (40.0%) patients with high BMI, ER, PR and HER2/neu positive status and in housewife group. There was an increase of 1/3 genotype frequency in patients with positive family history and agricultural laborers (55.6%). In conclusion our results suggested that the CYP3A5*3 polymorphism might influence the breast cancer etiology which mainly depends on the type of exposure. CYP3A5*6 allele was not observed in cases as well as in controls. Keywords: Polymorphisms; Breast cancer; Receptor status Introduction CYP3A enzymes are the most abundantly expressed cytochrome P450 enzymes in liver and are responsible for the metabolism of over 50% of all clinically used drugs (1) Gellner et al (2) had identified a 231-kb region on chromosome 7q21.1 containing 3 CYP3A genes: CYP3A4, CYP3A5 and CYP3A7, as well as 3 pseudogenes and a novel CYP3A gene, which they termed CYP3A43. Jounaidi et al (3), isolated the 5-prime flanking region of CYP3A5 from a genomic clone on chromosome 7. Promoter analysis determined that CYP3A5 uses a CATAA box, rather than a TATA box at positions -23 to -28 and has a basic transcription element from -35 to -50. Kuehl et al (4) stated that variation in the CYP3A enzymes could influence circulating steroid levels and responses to 50% of oxidatively metabolised drugs. CYP3A activity was the sum activity of the family of CYP3A genes, including CYP3A5, which was polymorphically expressed at high levels in a minority of Caucasians. Only individuals with at least one CYP3A5*1 (wild type) allele express large amounts of CYP3A5. Kuehl et al (4) demonstrated that SNPs in CYP3A5*3 (6986A-G) and CYP3A5*6 (a G- to-A transition in exon 7 resulting in deletion of that exon) cause alternative splicing and protein truncation, resulting in the absence of CYP3A5 from tissues of some people. Because CYP3A5 CYP3A5*3 and CYP3A5*6 Polymorphisms and Breast Cancer
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April Journal-2009.p65 - Association of Biotechnology and Pharmacy

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