Publications

Found 9 results
Filters: Author is H.P. Li  [Clear All Filters]
2012
H. P. Li, Guo, Y. J., Zhu, H. S., Zhong, K., Zha, G. M., Wang, L. F., Wang, Y. L., Lu, W. F., Wang, Y. Y., and Yang, G. Y., IL-8 mRNA expression in the mouse mammary glands during pregnancy and lactation, vol. 11, pp. 4746-4753, 2012.
Baggiolini M (2001). Chemokines in pathology and medicine. J. Intern. Med. 250: 91-104. http://dx.doi.org/10.1046/j.1365-2796.2001.00867.x PMid:11489059   Baggiolini M, Dewald B and Moser B (1994). Interleukin-8 and related chemotactic cytokines - CXC and CC chemokines. Adv. Immunol. 55: 97-179. http://dx.doi.org/10.1016/S0065-2776(08)60509-X   Bek EL, McMillen MA, Scott P, Angus LD, et al. (2002). The effect of diabetes on endothelin, interleukin-8 and vascular endothelial growth factor-mediated angiogenesis in rats. Clin. Sci. 103 (Suppl 48): 424S-429S. PMid:12193137   Ben-Baruch A, Michiel DF and Oppenheim JJ (1995). Signals and receptors involved in recruitment of inflammatory cells. J. Biol. Chem. 270: 11703-11706. http://dx.doi.org/10.1074/jbc.270.20.11703 PMid:7744810   Bruun JM, Verdich C, Toubro S, Astrup A, et al. (2003). Association between measures of insulin sensitivity and circulating levels of interleukin-8, interleukin-6 and tumor necrosis factor-alpha. Effect of weight loss in obese men. Eur. J. Endocrinol. 148: 535-542. http://dx.doi.org/10.1530/eje.0.1480535 PMid:12720537   Dinarello CA (1989). Interleukin-1 and its biologically related cytokines. Adv. Immunol. 44: 153-205. http://dx.doi.org/10.1016/S0065-2776(08)60642-2   Gelaleti GB, Jardim BV, Leonel C, Moschetta MG, et al. (2012). Interleukin-8 as a prognostic serum marker in canine mammary gland neoplasias. Vet. Immunol. Immunopathol. 146: 106-112. http://dx.doi.org/10.1016/j.vetimm.2012.02.005 PMid:22405680   Hallgren J and Gurish MF (2011). Mast cell progenitor trafficking and maturation. Adv. Exp. Med. Biol. 716: 14-28. http://dx.doi.org/10.1007/978-1-4419-9533-9_2 PMid:21713649 PMCid:3554263   Hamed EA, Zakhary MM and Maximous DW (2012). Apoptosis, angiogenesis, inflammation, and oxidative stress: basic interactions in patients with early and metastatic breast cancer. J. Cancer Res. Clin. Oncol. 138: 999-1009. http://dx.doi.org/10.1007/s00432-012-1176-4 PMid:22362301   Hoffmann E, Dittrich-Breiholz O, Holtmann H and Kracht M (2002). Multiple control of interleukin-8 gene expression. J. Leukoc. Biol. 72: 847-855. PMid:12429706   Hunt KM, Williams JE, Shafii B, Hunt MK, et al. (2012). Mastitis Is Associated with Increased Free Fatty Acids, Somatic Cell Count, and Interleukin-8 Concentrations in Human Milk. Breastfeed. Med. [Ahed of Print].   Ju D, Sun D, Xiu L, Meng X, et al. (2012). Interleukin-8 is associated with adhesion, migration and invasion in human gastric cancer SCG-7901 cells. Med. Oncol. 29: 91-99. http://dx.doi.org/10.1007/s12032-010-9780-0 PMid:21191670   Kaplan AP (2001). Chemokines, chemokine receptors and allergy. Int. Arch. Allergy Immunol. 124: 423-431. http://dx.doi.org/10.1159/000053777 PMid:11340325   Kitadai Y, Takahashi Y, Haruma K, Naka K, et al. (1999). Transfection of interleukin-8 increases angiogenesis and tumorigenesis of human gastric carcinoma cells in nude mice. Br. J. Cancer 81: 647-653. http://dx.doi.org/10.1038/sj.bjc.6690742 PMid:10574250 PMCid:2362886   Koçak H, Oner-Iyidogan Y, Kocak T and Oner P (2004). Determination of diagnostic and prognostic values of urinary interleukin-8, tumor necrosis factor-alpha, and leukocyte arylsulfatase-A activity in patients with bladder cancer. Clin. Biochem. 37: 673-678. http://dx.doi.org/10.1016/j.clinbiochem.2004.02.005 PMid:15302609   Liskmann S, Vihalemm T, Salum O, Zilmer K, et al. (2006). Correlations between clinical parameters and interleukin-6 and interleukin-10 levels in saliva from totally edentulous patients with peri-implant disease. Int. J. Oral Maxillofac. Implants 21: 543-550. PMid:16955604   Matsuo Y, Ochi N, Sawai H, Yasuda A, et al. (2009). CXCL8/IL-8 and CXCL12/SDF-1alpha co-operatively promote invasiveness and angiogenesis in pancreatic cancer. Int. J. Cancer 124: 853-861. http://dx.doi.org/10.1002/ijc.24040 PMid:19035451 PMCid:2684108   Meade KG, O'Gorman GM, Narciandi F, Machugh DE, et al. (2012). Functional characterisation of bovine interleukin 8 promoter haplotypes in vitro. Mol. Immunol. 50: 108-116. http://dx.doi.org/10.1016/j.molimm.2011.12.011 PMid:22244152   Ning Y, Manegold PC, Hong YK, Zhang W, et al. (2011). Interleukin-8 is associated with proliferation, migration, angiogenesis and chemosensitivity in vitro and in vivo in colon cancer cell line models. Int. J. Cancer 128: 2038-2049. http://dx.doi.org/10.1002/ijc.25562 PMid:20648559 PMCid:3039715   Ramírez-Santana C, Perez-Cano FJ, Audi C, Castell M, et al. (2012). Effects of cooling and freezing storage on the stability of bioactive factors in human colostrum. J. Dairy Sci. 95: 2319-2325. http://dx.doi.org/10.3168/jds.2011-5066 PMid:22541460   Sabroe I, Lloyd CM, Whyte MK, Dower SK, et al. (2002). Chemokines, innate and adaptive immunity, and respiratory disease. Eur. Respir. J. 19: 350-355. http://dx.doi.org/10.1183/09031936.02.00253602 PMid:11871367 PMCid:3428840   Sagnak L, Ersoy H, Ozok U, Senturk B, et al. (2009). Predictive value of urinary interleukin-8 cutoff point for recurrences after transurethral resection plus induction bacillus Calmette-Guerin treatment in non-muscle-invasive bladder tumors. Clin. Genitourin. Cancer 7: E16-E23. http://dx.doi.org/10.3816/CGC.2009.n.016 PMid:19692317   Sheryka E, Wheeler MA, Hausladen DA and Weiss RM (2003). Urinary interleukin-8 levels are elevated in subjects with transitional cell carcinoma. Urology 62: 162-166. http://dx.doi.org/10.1016/S0090-4295(03)00134-1   Song JH, Kim SG, Jung SA, Lee MK, et al. (2010). The interleukin-8-251 AA genotype is associated with angiogenesis in gastric carcinogenesis in Helicobacter pylori-infected Koreans. Cytokine 51: 158-165. http://dx.doi.org/10.1016/j.cyto.2010.05.001 PMid:20621718   Sordillo LM and Streicher KL (2002). Mammary gland immunity and mastitis susceptibility. J. Mammary Gland. Biol. Neoplasia 7: 135-146. http://dx.doi.org/10.1023/A:1020347818725 PMid:12463736   Taub DD and Oppenheim JJ (1994). Chemokines, inflammation and the immune system. Ther. Immunol. 1: 229-246. PMid:7584498   Vernay MC, Wellnitz O, Kreipe L, van Dorland HA, et al. (2012). Local and systemic response to intramammary lipopolysaccharide challenge during long-term manipulated plasma glucose and insulin concentrations in dairy cows. J. Dairy Sci. 95: 2540-2549. http://dx.doi.org/10.3168/jds.2011-5188 PMid:22541481   Zhu YH, Liu PQ, Weng XG, Zhuge ZY, et al. (2012). Short communication: Pheromonicin-SA affects mRNA expression of toll-like receptors, cytokines, and lactoferrin by Staphylococcus aureus-infected bovine mammary epithelial cells. J. Dairy Sci. 95: 759-764. http://dx.doi.org/10.3168/jds.2011-4703 PMid:22281341   Zuccari DA, Leonel C, Castro R, Gelaleti GB, et al. (2012). An immunohistochemical study of interleukin-8 (IL-8) in breast cancer. Acta Histochem. 114: 571-576. http://dx.doi.org/10.1016/j.acthis.2011.10.007 PMid:22244449
2011
Y. Lu, Xu, W. H., Xie, Y. X., Zhang, X., Pu, J. J., Qi, Y. X., and Li, H. P., Isolation and characterization of nucleotide-binding site and C-terminal leucine-rich repeat-resistance gene candidates in bananas, vol. 10, pp. 3098-3108, 2011.
Aarts MG, te Lintel HB, Holub EB, Beynon JL, et al. (1998). Identification of R-gene homologous DNA fragments genetically linked to disease resistance loci in Arabidopsis thaliana. Mol. Plant Microbe Interact. 11: 251-258. http://dx.doi.org/10.1094/MPMI.1998.11.4.251 PMid:9530866 Agrios GN (1997). Plant Pathology. 4th edn. Academic Press, New York. Altschul SF, Madden TL, Schaffer AA, Zhang J, et al. (1997). Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res. 25: 3389-3402. http://dx.doi.org/10.1093/nar/25.17.3389 PMid:9254694    PMCid:146917 Anderson PA, Lawrence GJ, Morrish BC, Ayliffe MA, et al. (1997). Inactivation of the flax rust resistance gene M associated with loss of a repeated unit within the leucine-rich repeat coding region. Plant Cell 9: 641-651. PMid:9144966    PMCid:156945 Bai J, Pennill LA, Ning J, Lee SW, et al. (2002). Diversity in nucleotide binding site-leucine-rich repeat genes in cereals. Genome Res. 12: 1871-1884. http://dx.doi.org/10.1101/gr.454902 PMid:12466291    PMCid:187567 Bailey TL and Elkan C (1994). Fitting a mixture model by expectation maximization to discover motifs in biopolymers. Proc. Int. Conf. Intell. Syst. Mol. Biol. 2: 28-36. PMid:7584402 Bent AF, Kunkel BN, Dahlbeck D, Brown KL, et al. (1994). RPS2 of Arabidopsis thaliana: a leucine-rich repeat class of plant disease resistance genes. Science 265: 1856-1860. http://dx.doi.org/10.1126/science.8091210 PMid:8091210 Carlier J, Fouré E, Gauhl F and Jones DR (2000). Fungal Diseases of the Foliage. In: Diseases of Banana Abacá and Enset (Jones DR, ed.). CABI Publishing, Wallingford, 37-141. Dixon MS, Jones DA, Keddie JS, Thomas CM, et al. (1996). The tomato Cf-2 disease resistance locus comprises two functional genes encoding leucine-rich repeat proteins. Cell 84: 451-459. http://dx.doi.org/10.1016/S0092-8674(00)81290-8 Eddy SR (2007). HMMER: Profile Hidden Markov Models for Biological Sequence Analysis. Available at [http://hmmer.janelia.org]. Accessed March 15, 2010. FAO (2005). (Food and Agricultural Organization). Available at [http://www.fao.org/lim500/nphwrap.pi?productioncrops. primary&Domain=SUA&]. Accessed December 3, 2009. Feuillet C, Schachermayr G and Keller B (1997). Molecular cloning of a new receptor-like kinase gene encoded at the Lr10 disease resistance locus of wheat. Plant J. 11: 45-52. http://dx.doi.org/10.1046/j.1365-313X.1997.11010045.x PMid:9025301 Grant MR, Godiard L, Straube E, Ashfield T, et al. (1995). Structure of the Arabidopsis RPM1 gene enabling dual specificity disease resistance. Science 269: 843-846. http://dx.doi.org/10.1126/science.7638602 PMid:7638602 Jeong SC, Hayes AJ, Biyashev RM and Saghai MMA (2001). Diversity and evolution of a non-TIR-NBS sequence family that clusters to a chromosomal “hotspot” for disease resistance genes in soybean. Theor. Appl. Genet. 103: 406-414. http://dx.doi.org/10.1007/s001220100567 Jones DA, Thomas CM, Hammond-Kosack KE, Balint-Kurti PJ, et al. (1994). Isolation of the tomato Cf-9 gene for resistance to Cladosporium fulvum by transposon tagging. Science 266: 789-793. http://dx.doi.org/10.1126/science.7973631 PMid:7973631 Jones DR (2000). Introduction of Banana. In: Diseases of Banana, Abacá and Enset (Jones DR, ed.). CABI Publishing, Wallingford, 1-36. Joshi RK, Mohanty S, Subudhi E and Nayak S (2010). Isolation and characterization of NBS-LRR- resistance gene candidates in turmeric (Curcuma longa cv. surama). Genet. Mol. Res. 9: 1796-1806. http://dx.doi.org/10.4238/vol9-3gmr910 PMid:20830672 Lawrence GJ, Finnegan EJ, Ayliffe MA and Ellis JG (1995). The L6 gene for flax rust resistance is related to the Arabidopsis bacterial resistance gene RPS2 and the tobacco viral resistance gene N. Plant Cell 7: 1195-1206. PMid:7549479    PMCid:160944 Leister D, Kurth J, Laurie DA, Yano M, et al. (1999). RFLP- and physical mapping of resistance gene homologues in rice (O. sative) and Barley (H. vulgare). Theor. Appl. Genet. 98: 509-520. http://dx.doi.org/10.1007/s001220051099 Marín DH, Romero RA, Guzmán M and Sutton TB (2003). Black sigatoka: an increasing threat to banana cultivation. Plant Disease 87: 208-222. http://dx.doi.org/10.1094/PDIS.2003.87.3.208 Martín GB, Brommonschenkel SH, Chunwongse J, Frary A, et al. (1993). Map-based cloning of a protein kinase gene conferring disease resistance in tomato. Science 262: 1432-1436. http://dx.doi.org/10.1126/science.7902614 PMid:7902614 Meyers BC, Dickerman AW, Michelmore RW, Sivaramakrishnan S, et al. (1999). Plant disease resistance genes encode members of an ancient and diverse protein family within the nucleotide-binding superfamily. Plant J. 20: 317-332. http://dx.doi.org/10.1046/j.1365-313X.1999.t01-1-00606.x PMid:10571892 Meyers BC, Morgante M and Michelmore RW (2002). TIR-X and TIR-NBS proteins: two new families related to disease resistance TIR-NBS-LRR proteins encoded in Arabidopsis and other plant genomes. Plant J. 32: 77-92. http://dx.doi.org/10.1046/j.1365-313X.2002.01404.x PMid:12366802 Michelmore R (2000). Genomic approaches to plant disease resistance. Curr. Opin. Plant Biol. 3: 125-131. http://dx.doi.org/10.1016/S1369-5266(99)00050-3 Michelmore RW and Meyers BC (1998). Clusters of resistance genes in plants evolve by divergent selection and a birth-and-death process. Genome Res. 8: 1113-1130. PMid:9847076 Noel L, Moores TL, van Der Biezen EA, Parniske M, et al. (1999). Pronounced intraspecific haplotype divergence at the RPP5 complex disease resistance locus of Arabidopsis. Plant Cell 11: 2099-2112. PMid:10559437    PMCid:144120 Ori N, Eshed Y, Paran I, Presting G, et al. (1997). The I2C family from the wilt disease resistance locus I2 belongs to the nucleotide binding, leucine-rich repeat superfamily of plant resistance genes. Plant Cell 9: 521-532. PMid:9144960    PMCid:156936 Page RD (1996). TreeView: an application to display phylogenetic trees on personal computers. Comput. Appl. Biosci. 12: 357-358. PMid:8902363 Pan Q, Wendel J and Fluhr R (2000). Divergent evolution of plant NBS-LRR resistance gene homologues in dicot and cereal genomes. J. Mol. Evol. 50: 203-213. PMid:10754062 Pei X, Li S, Jiang Y, Zhang Y, et al. (2007). Isolation, characterization and phylogenetic analysis of the resistance gene analogues (RGAs) in banana (Musa spp.). Plant Sci. 172: 1166-1174. http://dx.doi.org/10.1016/j.plantsci.2007.02.019 Penuela S, Danesh D and Young ND (2002). Targeted isolation, sequence analysis, and physical mapping of nonTIR NBS-LRR genes in soybean. Theor. Appl. Genet. 104: 261-272. http://dx.doi.org/10.1007/s00122-001-0785-0 Peraza-Echeverria S, James-Kay A, Canto-Canche B and Castillo-Castro E (2007). Structural and phylogenetic analysis of Pto-type disease resistance gene candidates in banana. Mol. Genet. Genom. 278: 443-453. http://dx.doi.org/10.1007/s00438-007-0262-9 PMid:17587056 Robert NGM, David JB, Franc CB, Candice MRS, et al. (2008). Analysis of non-TIR NBS-LRR resistance gene analogs in Musa acaminata Colla: isolation, RFLP marker development, and physical mapping. BMC Plant Biol. 8: 15. http://dx.doi.org/10.1186/1471-2229-8-15 PMid:18234103    PMCid:2262081 Saitou N and Nei M (1987). The neighbor-joining method: a new method for reconstructing phylogenetic trees. Mol. Biol. Evol. 4: 406-425. PMid:3447015 Salmeron JM, Oldroyd GE, Rommens CM, Scofield SR, et al. (1996). Tomato Prf is a member of the leucine-rich repeat class of plant disease resistance genes and lies embedded within the Pto kinase gene cluster. Cell 86: 123-133. http://dx.doi.org/10.1016/S0092-8674(00)80083-5 Sambrook J and Russell DW (2001). Molecular Cloning: A Laboratory Manual. 3rd edn. Cold Spring Harbor, USA, Cold Spring Harbor Laboratory, New York. SanMiguel P, Tikhonov A, Jin YK, Motchoulskaia N, et al. (1996). Nested retrotransposons in the intergenic regions of the maize genome. Science 274: 765-768. http://dx.doi.org/10.1126/science.274.5288.765 PMid:8864112 Song WY, Wang GL, Chen LL, Kim HS, et al. (1995). A receptor kinase-like protein encoded by the rice disease resistance gene, Xa21. Science 270: 1804-1806. http://dx.doi.org/10.1126/science.270.5243.1804 PMid:8525370 Staden R (1996). The Staden sequence analysis package. Mol. Biotechnol. 5: 233-241. http://dx.doi.org/10.1007/BF02900361 PMid:8837029 Tai TH, Dahlbeck D, Clark ET, Gajiwala P, et al. (1999). Expression of the Bs2 pepper gene confers resistance to bacterial spot disease in tomato. Proc. Natl. Acad. Sci. U. S. A. 96: 14153-14158. http://dx.doi.org/10.1073/pnas.96.24.14153 Thevissen K, Cammue BP, Lemaire K, Winderickx J, et al. (2000). A gene encoding a sphingolipid biosynthesis enzyme determines the sensitivity of Saccharomyces cerevisiae to an antifungal plant defensin from dahlia (Dahlia merckii). Proc. Natl. Acad. Sci. U. S. A. 97: 9531-9536. http://dx.doi.org/10.1073/pnas.160077797 PMid:10931938 van Der Biezen EA and Jones JD (1998). The NB-ARC domain: a novel signalling motif shared by plant resistance gene products and regulators of cell death in animals. Curr. Biol. 8: R226-R227. http://dx.doi.org/10.1016/S0960-9822(98)70145-9 Wang ZX, Yano M, Yamanouchi U, Iwamoto M, et al. (1999). The Pib gene for rice blast resistance belongs to the nucleotide binding and leucine-rich repeat class of plant disease resistance genes. Plant J. 19: 55-64. http://dx.doi.org/10.1046/j.1365-313X.1999.00498.x PMid:10417726 Whitham S, Dinesh-Kumar SP, Choi D, Hehl R, et al. (1994). The product of the tobacco mosaic virus resistance gene N: similarity to toll and the interleukin-1 receptor. Cell 78: 1101-1115. http://dx.doi.org/10.1016/0092-8674(94)90283-6 Wiame L, Swennen R and Sági L (2000). PCR-based cloning of candidate disease resistance genes from banana (Musa acuminata). Acta Hortic. 521: 51-57. Xie YB, Tang DZ, Zhang YS and Li WM (1998). Isolation of homologous sequences of R gene from rice. Chin. Sci. Bull. 43: 277-281. Yamanashi Y, Okada M, Semba T, Yamori T, et al. (1993). Identification of HS1 protein as a major substrate of protein-tyrosine kinase(s) upon B-cell antigen receptor-mediated signaling. Proc. Natl. Acad. Sci. U. S. A. 90: 3631-3635. http://dx.doi.org/10.1073/pnas.90.8.3631 Yoshimura S, Yamanouchi U, Katayose Y, Toki S, et al. (1998). Expression of Xa1, a bacterial blight-resistance gene in rice, is induced by bacterial inoculation. Proc. Natl. Acad. Sci. 95: 1663-1668. http://dx.doi.org/10.1073/pnas.95.4.1663
Y. Y. Wang, Wang, Y. L., Li, H. P., Zhu, H. S., Jiang, Q. D., Zhang, L., Wang, L. F., Han, L. Q., Zhong, K., Guo, Y. J., Lu, W. F., Li, H. J., and Yang, G. Y., 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