Publications
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“Conjugated linoleic acid-induced milk fat reduction associated with depressed expression of lipogenic genes in lactating Holstein mammary glands”, vol. 11, pp. 4754-4764, 2012.
, Barber MC, Vallance AJ, Kennedy HT and Travers MT (2003). Induction of transcripts derived from promoter III of the acetyl-CoA carboxylase-alpha gene in mammary gland is associated with recruitment of SREBP-1 to a region of the proximal promoter defined by a DNase I hypersensitive site. Biochem. J. 375: 489-501.
http://dx.doi.org/10.1042/BJ20030480
PMid:12871210 PMCid:1223696
Bauman DE and Griinari JM (2003). Nutritional regulation of milk fat synthesis. Annu. Rev. Nutr. 23: 203-227.
http://dx.doi.org/10.1146/annurev.nutr.23.011702.073408
PMid:12626693
Bauman DE, Perfield JW, Harvatine KJ and Baumgard LH (2008). Regulation of fat synthesis by conjugated linoleic acid: lactation and the ruminant model. J. Nutr. 138: 403-409. Baumgard LH, Corl BA, Dwyer DA, Saebo A, et al. (2000). Identification of the conjugated linoleic acid isomer that inhibits milk fat synthesis. Am. J. Physiol. Regul. Integr. Comp Physiol. 278: R179-R184.
Baumgard LH, Sangster JK and Bauman DE (2001). Milk fat synthesis in dairy cows is progressively reduced by increasing supplemental amounts of trans-10, cis-12 conjugated linoleic acid (CLA). J. Nutr. 131: 1764-1769.
PMid:11385065
Baumgard LH, Matitashvili E, Corl BA, Dwyer DA, et al. (2002). trans-10, cis-12 conjugated linoleic acid decreases lipogenic rates and expression of genes involved in milk lipid synthesis in dairy cows. J. Dairy Sci. 85: 2155-2163.
http://dx.doi.org/10.3168/jds.S0022-0302(02)74294-X
Belury MA (2002). Dietary conjugated linoleic acid in health: physiological effects and mechanisms of action. Annu. Rev. Nutr. 22: 505-531.
http://dx.doi.org/10.1146/annurev.nutr.22.021302.121842
PMid:12055356
Bernard L, Leroux C and Chilliard Y (2008). Expression and nutritional regulation of lipogenic genes in the ruminant lactating mammary gland. Adv. Exp. Med. Biol. 606: 67-108.
http://dx.doi.org/10.1007/978-0-387-74087-4_2
PMid:18183925
Bionaz M and Loor JJ (2008). Gene networks driving bovine milk fat synthesis during the lactation cycle. BMC. Genomics 9: 366.
http://dx.doi.org/10.1186/1471-2164-9-366
PMid:18671863 PMCid:2547860
Chouinard PY, Corneau L, Barbano DM, Metzger LE, et al. (1999). Conjugated linoleic acids alter milk fatty acid composition and inhibit milk fat secretion in dairy cows. J Nutr. 129: 1579-1584.
PMid:10419994
Gervais R, McFadden JW, Lengi AJ, Corl BA, et al. (2009). Effects of intravenous infusion of trans-10, cis-12 18:2 on mammary lipid metabolism in lactating dairy cows. J. Dairy Sci. 92: 5167-5177.
http://dx.doi.org/10.3168/jds.2009-2281
PMid:19762835
Giesy JG, McGuire MA, Shafii B and Hanson TW (2002). Effect of dose of calcium salts of conjugated linoleic acid (CLA) on percentage and fatty acid content of milk fat in midlactation holstein cows. J. Dairy Sci. 85: 2023-2029.
http://dx.doi.org/10.3168/jds.S0022-0302(02)74279-3
Griinari JM, Corl BA, Lacy SH, Chouinard PY, et al. (2000). Conjugated linoleic acid is synthesized endogenously in lactating dairy cows by Delta(9)-desaturase. J. Nutr. 130: 2285-2291.
PMid:10958825
Harvatine KJ and Bauman DE (2006). SREBP1 and thyroid hormone responsive spot 14 (S14) are involved in the regulation of bovine mammary lipid synthesis during diet-induced milk fat depression and treatment with CLA. J. Nutr. 136: 2468-2474.
PMid:16988111
Huang Y, Schoonmaker JP, Bradford BJ and Beitz DC (2008). Response of milk fatty acid composition to dietary supplementation of soy oil, conjugated linoleic acid, or both. J. Dairy Sci. 91: 260-270.
http://dx.doi.org/10.3168/jds.2007-0344
PMid:18096948
Kadegowda AK, Bionaz M, Thering B, Piperova LS, et al. (2009). Identification of internal control genes for quantitative polymerase chain reaction in mammary tissue of lactating cows receiving lipid supplements. J. Dairy Sci. 92: 2007-2019.
http://dx.doi.org/10.3168/jds.2008-1655
PMid:19389958
Kadegowda AK, Connor EE, Teter BB, Sampugna J, et al. (2010). Dietary trans fatty acid isomers differ in their effects on mammary lipid metabolism as well as lipogenic gene expression in lactating mice. J. Nutr. 140: 919-924.
http://dx.doi.org/10.3945/jn.109.110890
PMid:20220207
Khan SA and Vanden Heuvel JP (2003). Role of nuclear receptors in the regulation of gene expression by dietary fatty acids (review). J. Nutr. Biochem. 14: 554-567.
http://dx.doi.org/10.1016/S0955-2863(03)00098-6
Lock AL, Teles BM, Perfield JW, Bauman DE, et al. (2006). A conjugated linoleic acid supplement containing trans-10, cis-12 reduces milk fat synthesis in lactating sheep. J. Dairy Sci. 89: 1525-1532.
http://dx.doi.org/10.3168/jds.S0022-0302(06)72220-2
Loor JJ, Ferlay A, Ollier A, Doreau M, et al. (2005). Relationship among trans and conjugated fatty acids and bovine milk fat yield due to dietary concentrate and linseed oil. J. Dairy Sci. 88: 726-740.
http://dx.doi.org/10.3168/jds.S0022-0302(05)72736-3
Perfield JW, Bernal-Santos G, Overton TR and Bauman DE (2002). Effects of dietary supplementation of rumen-protected conjugated linoleic acid in dairy cows during established lactation. J. Dairy Sci. 85: 2609-2617.
http://dx.doi.org/10.3168/jds.S0022-0302(02)74346-4
Peterson DG, Baumgard LH and Bauman DE (2002). Milk fat response to low doses of trans-10, cis-12 conjugated linoleic acid(CLA). J. Dairy Sci. 85: 1764-1766.
http://dx.doi.org/10.3168/jds.S0022-0302(02)74250-1
Peterson DG, Matitashvili EA and Bauman DE (2004). The inhibitory effect of trans-10, cis-12 CLA on lipid synthesis in bovine mammary epithelial cells involves reduced proteolytic activation of the transcription factor SREBP-1. J. Nutr. 134: 2523-2527.
PMid:15465741
Pfaffl MW (2001). A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29: e45.
http://dx.doi.org/10.1093/nar/29.9.e45
PMid:11328886 PMCid:55695
Piperova LS, Teter BB, Bruckental I, Sampugna J, et al. (2000). Mammary lipogenic enzyme activity, trans fatty acids and conjugated linoleic acids are altered in lactating dairy cows fed a milk fat-depressing diet. J. Nutr. 130: 2568-2574.
PMid:11015491
Vandesompele J, De Preter K, Pattyn F, Poppe B, et al. (2002). Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3: RESEARCH0034.
Viswanadha S, Giesy JG, Hanson TW and McGuire MA (2003). Dose response of milk fat to intravenous administration of the trans-10, cis-12 isomer of conjugated linoleic acid. J. Dairy Sci. 86: 3229-3236.
http://dx.doi.org/10.3168/jds.S0022-0302(03)73926-5
Yang T, Espenshade PJ, Wright ME, Yabe D, et al. (2002). Crucial step in cholesterol homeostasis: sterols promote binding of SCAP to INSIG-1, a membrane protein that facilitates retention of SREBPs in ER. Cell 110: 489-500.
http://dx.doi.org/10.1016/S0092-8674(02)00872-3
“Leptin mRNA expression in the rat mammary gland at different activation stages”, vol. 10, pp. 3657-3663, 2011.
,
Ahima RS and Flier JS (2000). Adipose tissue as an endocrine organ. Trends Endocrinol. Metab. 11: 327-332.
http://dx.doi.org/10.1016/S1043-2760(00)00301-5
Amico JA, Thomas A, Crowley RS and Burmeister LA (1998). Concentrations of leptin in the serum of pregnant, lactating, and cycling rats and of leptin messenger ribonucleic acid in rat placental tissue. Life Sci. 63: 1387-1395.
http://dx.doi.org/10.1016/S0024-3205(98)00405-6
Aoki N, Kawamura M and Matsuda T (1999). Lactation-dependent down regulation of leptin production in mouse mammary gland. Biochim. Biophys. Acta 1427: 298-306.
http://dx.doi.org/10.1016/S0304-4165(99)00029-X
Baratta M, Grolli S and Tamanini C (2003). Effect of leptin in proliferating and differentiated HC11 mouse mammary cells. Regul. Pept. 113: 101-107.
http://dx.doi.org/10.1016/S0167-0115(03)00006-5
Bartha T, Sayed-Ahmed A and Rudas P (2005). Expression of leptin and its receptors in various tissues of ruminants. Domest. Anim. Endocrinol. 29: 193-202.
http://dx.doi.org/10.1016/j.domaniend.2005.03.010
PMid:15878255
Bonnet M, Gourdou I, Leroux C, Chilliard Y, et al. (2002). Leptin expression in the ovine mammary gland: putative sequential involvement of adipose, epithelial, and myoepithelial cells during pregnancy and lactation. J. Anim. Sci. 80: 723-728.
PMid:11890408
Butte NF, Hopkinson JM, Mehta N, Moon JK, et al. (1999). Adjustments in energy expenditure and substrate utilization during late pregnancy and lactation. Am. J. Clin. Nutr. 69: 299-307.
PMid:9989696
Clevenger CV and Plank TL (1997). Prolactin as an autocrine/paracrine factor in breast tissue. J. Mammary Gland. Biol. Neoplasia 2: 59-68.
http://dx.doi.org/10.1023/A:1026325630359
PMid:10887520
Elias JJ, Pitelka DR and Armstrong RC (1973). Changes in fat cell morphology during lactation in the mouse. Anat. Rec. 177: 533-547.
http://dx.doi.org/10.1002/ar.1091770407
PMid:4762729
Farooqi IS, Keogh JM, Kamath S, Jones S, et al. (2001). Partial leptin deficiency and human adiposity. Nature 414: 34-35.
http://dx.doi.org/10.1038/35102112
PMid:11689931
Feuermann Y, Mabjeesh SJ and Shamay A (2004). Leptin affects prolactin action on milk protein and fat synthesis in the bovine mammary gland. J. Dairy Sci. 87: 2941-2946.
http://dx.doi.org/10.3168/jds.S0022-0302(04)73425-6
Houseknecht KL, Baile CA, Matteri RL and Spurlock ME (1998). The biology of leptin: a review. J. Anim. Sci. 76: 1405- 1420.
PMid:9621947
Hu X, Juneja SC, Maihle NJ and Cleary MP (2002). Leptin - a growth factor in normal and malignant breast cells and for normal mammary gland development. J. Natl. Cancer Inst. 94: 1704-1711.
http://dx.doi.org/10.1093/jnci/94.22.1704
PMid:12441326
Jin LL, Zhang S, Burguera BG, Couce ME, et al. (2000). Leptin and leptin receptor expression in rat and mouse pituitary cells. Endocrinology 141: 333-339.
http://dx.doi.org/10.1210/en.141.1.333
PMid:10614655
Lin Y and Li Q (2007). Expression and function of leptin and its receptor in mouse mammary gland. Sci. China C Life Sci. 50: 669-675.
http://dx.doi.org/10.1007/s11427-007-0077-2
PMid:17879067
Malik NM, Carter ND, Murray JF, Scaramuzzi RJ, et al. (2001). Leptin requirement for conception, implantation, and gestation in the mouse. Endocrinology 142: 5198-5202.
http://dx.doi.org/10.1210/en.142.12.5198
PMid:11713215
Mol JA, Lantinga-van L, I, van Garderen E and Rijnberk A (2000). Progestin-induced mammary growth hormone (GH) production. Adv. Exp. Med. Biol. 480: 71-76.
http://dx.doi.org/10.1007/0-306-46832-8_8
PMid:10959411
Neville MC, McFadden TB and Forsyth I (2002). Hormonal regulation of mammary differentiation and milk secretion. J. Mammary Gland. Biol. Neoplasia 7: 49-66.
http://dx.doi.org/10.1023/A:1015770423167
PMid:12160086
O'Brien SN, Welter BH and Price TM (1999). Presence of leptin in breast cell lines and breast tumors. Biochem. Biophys. Res. Commun. 259: 695-698.
http://dx.doi.org/10.1006/bbrc.1999.0843
PMid:10364481
Sayed-Ahmed A, Kulcsar M, Rudas P and Bartha T (2004). Expression and localisation of leptin and leptin receptor in the mammary gland of the dry and lactating non-pregnant cow. Acta Vet. Hung. 52: 97-111.
http://dx.doi.org/10.1556/AVet.52.2004.1.10
PMid:15119791
Smith-Kirwin SM, O'Connor DM, De JJ, Lancey ED, et al. (1998). Leptin expression in human mammary epithelial cells and breast milk. J. Clin. Endocrinol. Metab. 83: 1810-1813.
http://dx.doi.org/10.1210/jc.83.5.1810
PMid:9589698
Smith JL and Sheffield LG (2002). Production and regulation of leptin in bovine mammary epithelial cells. Domest. Anim. Endocrinol. 22: 145-154.
http://dx.doi.org/10.1016/S0739-7240(02)00121-2
Woodside B, Abizaid A and Walker C (2000). Changes in leptin levels during lactation: implications for lactational hyperphagia and anovulation. Horm. Behav. 37: 353-365.
http://dx.doi.org/10.1006/hbeh.2000.1598
PMid:10860679
Zhang Y, Proenca R, Maffei M, Barone M, et al. (1994). Positional cloning of the mouse obese gene and its human homologue. Nature 372: 425-432.
http://dx.doi.org/10.1038/372425a0
PMid:7984236
“mRNA abundance and expression of SLC27A, ACC, SCD, FADS, LPIN, INSIG, and PPARGC1 gene isoforms in mouse mammary glands during the lactation cycle”, vol. 9, pp. 1250-1257, 2010.
, Abu-Elheiga L, Brinkley WR, Zhong L, Chirala SS, et al. (2000). The subcellular localization of acetyl-CoA carboxylase 2. Proc. Natl. Acad. Sci. U. S. A. 97: 1444-1449.
http://dx.doi.org/10.1073/pnas.97.4.1444
PMid:10677481 PMCid:26453
Abu-Elheiga L, Matzuk MM, Abo-Hashema KA and Wakil SJ (2001). Continuous fatty acid oxidation and reduced fat storage in mice lacking acetyl-CoA carboxylase 2. Science 291: 2613-2616.
http://dx.doi.org/10.1126/science.1056843
PMid:11283375
Bernard L, Leroux C and Chilliard Y (2008). Expression and nutritional regulation of lipogenic genes in the ruminant lactating mammary gland. Adv. Exp. Med. Biol. 606: 67-108.
http://dx.doi.org/10.1007/978-0-387-74087-4_2
PMid:18183925
Bionaz M and Loor JJ (2008a). Gene networks driving bovine milk fat synthesis during the lactation cycle. BMC Genomics 9: 366.
http://dx.doi.org/10.1186/1471-2164-9-366
PMid:18671863 PMCid:2547860
Bionaz M and Loor JJ (2008b). ACSL1, AGPAT6, FABP3, LPIN1, and SLC27A6 are the most abundant isoforms in bovine mammary tissue and their expression is affected by stage of lactation. J. Nutr. 138: 1019-1024.
PMid:18492828
Cho HP, Nakamura MT and Clarke SD (1999a). Cloning, expression, and nutritional regulation of the mammalian Delta-6 desaturase. J. Biol. Chem. 274: 471-477.
http://dx.doi.org/10.1074/jbc.274.1.471
PMid:9867867
Cho HP, Nakamura M and Clarke SD (1999b). Cloning, expression, and fatty acid regulation of the human delta-5 desaturase. J. Biol. Chem. 274: 37335-37339.
http://dx.doi.org/10.1074/jbc.274.52.37335
PMid:10601301
Donkor J, Sariahmetoglu M, Dewald J, Brindley DN, et al. (2007). Three mammalian lipins act as phosphatidate phosphatases with distinct tissue expression patterns. J. Biol. Chem. 282: 3450-3457.
http://dx.doi.org/10.1074/jbc.M610745200
PMid:17158099
Donkor J, Sparks LM, Xie H, Smith SR, et al. (2008). Adipose tissue lipin-1 expression is correlated with peroxisome proliferator-activated receptor alpha gene expression and insulin sensitivity in healthy young men. J. Clin. Endocrinol. Metab. 93: 233-239.
http://dx.doi.org/10.1210/jc.2007-1535
PMid:17925338 PMCid:2190746
Harvatine KJ and Bauman DE (2006). SREBP1 and thyroid hormone responsive spot 14 (S14) are involved in the regulation of bovine mammary lipid synthesis during diet-induced milk fat depression and treatment with CLA. J. Nutr. 136: 2468-2474.
PMid:16988111
Kast-Woelbern HR, Dana SL, Cesario RM, Sun L, et al. (2004). Rosiglitazone induction of Insig-1 in white adipose tissue reveals a novel interplay of peroxisome proliferator-activated receptor gamma and sterol regulatory element-binding protein in the regulation of adipogenesis. J. Biol. Chem. 279: 23908-23915.
http://dx.doi.org/10.1074/jbc.M403145200
PMid:15073165
Kgwatalala PM, Ibeagha-Awemu EM, Mustafa AF and Zhao X (2009). Influence of stearoyl-coenzyme A desaturase 1 genotype and stage of lactation on fatty acid composition of Canadian Jersey cows. J. Dairy Sci. 92: 1220-1228.
http://dx.doi.org/10.3168/jds.2008-1471
PMid:19233815
Marquardt A, Stohr H, White K and Weber BH (2000). cDNA cloning, genomic structure, and chromosomal localization of three members of the human fatty acid desaturase family. Genomics 66: 175-183.
http://dx.doi.org/10.1006/geno.2000.6196
PMid:10860662
Medina-Gomez G, Gray S and Vidal-Puig A (2007). Adipogenesis and lipotoxicity: role of peroxisome proliferator-activated receptor gamma (PPARgamma) and PPARgammacoactivator-1 (PGC1). Public Health Nutr. 10: 1132-1137.
http://dx.doi.org/10.1017/S1368980007000614
PMid:17903321
Miyazaki M, Jacobson MJ, Man WC, Cohen P, et al. (2003). Identification and characterization of murine SCD4, a novel heart-specific stearoyl-CoA desaturase isoform regulated by leptin and dietary factors. J. Biol. Chem. 278: 33904-33911.
http://dx.doi.org/10.1074/jbc.M304724200
PMid:12815040
Ntambi JM, Miyazaki M and Dobrzyn A (2004). Regulation of stearoyl-CoA desaturase expression. Lipids 39: 1061-1065.
http://dx.doi.org/10.1007/s11745-004-1331-2
PMid:15726820
Pfaffl MW (2001). A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29: e45.
http://dx.doi.org/10.1093/nar/29.9.e45
PMid:11328886 PMCid:55695
Rudolph MC, McManaman JL, Phang T, Russell T, et al. (2007). Metabolic regulation in the lactating mammary gland: a lipid synthesizing machine. Physiol. Genomics 28: 323-336.
http://dx.doi.org/10.1152/physiolgenomics.00020.2006
PMid:17105756
Schwertfeger KL, McManaman JL, Palmer CA, Neville MC, et al. (2003). Expression of constitutively activated Akt in the mammary gland leads to excess lipid synthesis during pregnancy and lactation. J. Lipid Res. 44: 1100-1112.
http://dx.doi.org/10.1194/jlr.M300045-JLR200
PMid:12700340
Stahl A (2004). A current review of fatty acid transport proteins (SLC27). Pflugers Arch. 447: 722-727.
http://dx.doi.org/10.1007/s00424-003-1106-z
PMid:12856180
Sun LP, Li L, Goldstein JL and Brown MS (2005). Insig required for sterol-mediated inhibition of Scap/SREBP binding to COPII proteins in vitro. J. Biol. Chem. 280: 26483-26490.
http://dx.doi.org/10.1074/jbc.M504041200
PMid:15899885
Vandesompele J, De PK, Pattyn F, Poppe B, et al. (2002). Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3: RESEARCH0034.
Yabe D, Brown MS and Goldstein JL (2002). Insig-2, a second endoplasmic reticulum protein that binds SCAP and blocks export of sterol regulatory element-binding proteins. Proc. Natl. Acad. Sci. U. S. A. 99: 12753-12758.
http://dx.doi.org/10.1073/pnas.162488899
PMid:12242332 PMCid:130532
“Selection and use of reference genes in mouse mammary glands”, vol. 9, pp. 449-456, 2010.
, Bernard L, Leroux C, Bonnet M, Rouel J, et al. (2005). Expression and nutritional regulation of lipogenic genes in mammary gland and adipose tissues of lactating goats. J. Dairy Res. 72: 250-255.
http://dx.doi.org/10.1017/S0022029905000786
PMid:15909692
Bionaz M and Loor JJ (2007). Identification of reference genes for quantitative real-time PCR in the bovine mammary gland during the lactation cycle. Physiol. Genomics 29: 312-319.
http://dx.doi.org/10.1152/physiolgenomics.00223.2006
PMid:17284669
Bionaz M and Loor JJ (2008). Gene networks driving bovine milk fat synthesis during the lactation cycle. BMC Genomics 9: 366.
http://dx.doi.org/10.1186/1471-2164-9-366
PMid:18671863 PMCid:2547860
Bustin SA, Benes V, Nolan T and Pfaffl MW (2005). Quantitative real-time RT-PCR - a perspective. J. Mol. Endocrinol. 34: 597-601.
http://dx.doi.org/10.1677/jme.1.01755
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PMid:16324220 PMCid:1315359
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Modha G, Blanchard A, Iwasiow B, Mao XJ, et al. (2004). Developmental changes in insulin-like growth factor I receptor gene expression in the mouse mammary gland. Endocr. Res. 30: 127-140.
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Pfaffl MW (2001). A new mathematical model for relative quantification in real-time RT-PCR. Nucleic Acids Res. 29: e45.
http://dx.doi.org/10.1093/nar/29.9.e45
PMid:11328886 PMCid:55695
Pfaffl MW, Wittmann SL, Meyer HH and Bruckmaier RM (2003). Gene expression of immunologically important factors in blood cells, milk cells, and mammary tissue of cows. J. Dairy Sci. 86: 538-545.
http://dx.doi.org/10.3168/jds.S0022-0302(03)73632-7
Schmittgen TD and Zakrajsek BA (2000). Effect of experimental treatment on housekeeping gene expression: validation by real-time, quantitative RT-PCR. J. Biochem. Biophys. Methods 46: 69-81.
http://dx.doi.org/10.1016/S0165-022X(00)00129-9
Tramontana S, Bionaz M, Sharma A, Graugnard DE, et al. (2008). Internal controls for quantitative polymerase chain reaction of swine mammary glands during pregnancy and lactation. J. Dairy Sci. 91: 3057-3066.
http://dx.doi.org/10.3168/jds.2008-1164
PMid:18650282
Tricarico C, Pinzani P, Bianchi S, Paglierani M, et al. (2002). Quantitative real-time reverse transcription polymerase chain reaction: normalization to rRNA or single housekeeping genes is inappropriate for human tissue biopsies. Anal. Biochem. 309: 293-300.
http://dx.doi.org/10.1016/S0003-2697(02)00311-1
Vandesompele J, De Preter K, Pattyn F, Poppe B, et al. (2002). Accurate normalization of real-time quantitative RT-PCR data by geometric averaging of multiple internal control genes. Genome Biol. 3: 0034.1-0034-11.