(3.235.108.188) 您好!臺灣時間:2021/03/03 20:53
字體大小: 字級放大   字級縮小   預設字形  
回查詢結果

詳目顯示:::

我願授權國圖
: 
twitterline
研究生:高春成
研究生(外文):Chuen-cherng Kao
論文名稱:梅花鹿泌乳素基因之選殖及其重組蛋白質的表現
論文名稱(外文):Molecular cloning of prolactin cDNA from sika deer and expression of the recombinant prolactin in Escherichia coli
指導教授:楊 錫 坤
指導教授(外文):Shyi-Kuen Yang
學位類別:碩士
校院名稱:東海大學
系所名稱:畜產學系
學門:農業科學學門
學類:畜牧學類
論文種類:學術論文
論文出版年:1999
畢業學年度:87
語文別:中文
論文頁數:75
中文關鍵詞:泌乳素大腸桿菌
外文關鍵詞:prolactinEscherichia coli
相關次數:
  • 被引用被引用:0
  • 點閱點閱:202
  • 評分評分:系統版面圖檔系統版面圖檔系統版面圖檔系統版面圖檔系統版面圖檔
  • 下載下載:0
  • 收藏至我的研究室書目清單書目收藏:0
本試驗之目的係自梅花鹿腦垂腺 cDNA 基因庫選殖梅花鹿之泌乳素 cDNA。萃取自梅花鹿腦垂腺之總 RNA,利用反轉錄使之成為cDNA,再以 PCR 的方法擴增之,並再將此cDNA兩端加以修飾,接上EcoRI 的切位,嵌入λgt11 噬菌體之DNA 中,以此方式完成梅花鹿腦垂腺 cDNA 基因庫之構築,以梅花鹿泌乳素cDNA 835 bp 當探針,篩選完整之泌乳素基因。本試驗所得之泌乳素 cDNA與山羊相比較後發現,兩者之胺基酸長度相同,皆含有30個胺基酸之訊號與199個胺基酸之成熟。梅花鹿與山羊在訊號有一個胺基酸不同,而成熟中有10個胺基酸不同,其胺基酸之相似性為94.8%,核酸之相似性為95.2%。在基因的表現試驗中,將鹿泌乳素成熟之cDNA,接入 pTrc99A 原核表現載體中,使菌體大量表現梅花鹿泌乳素重組蛋白質,經西方吸漬法證實可產生一分子量為 23 kDa 之泌乳素。利用RT-PCR的方法分析,顯示腦垂體為唯一表現泌乳素基因之組織。

This study was attempted to clone prolactin cDNA from pituitary cDNA library of sika deer. Total RNA was extracted from pituitary of sika deer then the cDNA library was constructed. The full length of prolactin cDNA was screened by using 835 bp of prolactin PCR product as screening probe. The coding region of prolactin cDNA from sika deer showed high homology to that from goat with 95.2% homology in nucleotide sequence and 94.8% homology in amino acid sequence. The amino acid sequence of pituitary prolactin from sika deer deduced from cDNA suggested that it is consisted of 30 amino acids of signal peptide and 199 amino acid of mature peptide. Moreover, one amino acid from signal peptide and 10 amino acids from mature peptides were different between sika deer and caprine. The coding region of prolactin cDNA was then subcloned into prokaryotic expression vector pTrc99A and the recombinant prolactin was expression in E. coli . The result from Western Blot analysis showed that the molecular weight of this recombinant prolactin is 23 kDa. Analysis by RT-PCR showed that the pituitary is the only tissue expressing prolactin gene.

壹、 摘要…………………………………………………………………………………………1
貳、 前言…………………………………………………………………………………………2
參、 文獻檢討…………………………………………………………………………………4
一. 泌乳素之研究歷史……………………………………………………….………… 4
二. 泌乳素的基因序列及蛋白質構造……………………… ……………………7
(一) 泌乳素之蛋白質構造與cDNA………………… ……… ………………7
(二) 泌乳素基因組DNA 之序列………………… …………………………10
(三) 醣化的變異………………………………………… ………… … …………… 12
(四) 泌乳素的裂解產物…………………………………… …… ……… ………13
(五) 泌乳素家族之其他成員…………………………… ……… …… ……… 13
三. 泌乳素之合成與調節………………………………………………………………16
(一) 泌乳素的轉錄與合成路徑…………… …… …… ……………………… 16
1. 轉錄作用………………………… ………………… ………… …………………16
2. 泌乳素的生物合成……………………… ……… ……… …… …………… 18
(二) 泌乳素分泌的內分泌控制……………………………… ………………… 19
1. 泌乳素抑制的因子……………………… …… ………………………………19
(1 ) 度巴胺………………………… ………………………………………………19
(2 ) 內皮素………………………………… ………………… ……………………21
( 3 ) 降鈣素…………………………………………………………………… 21
2 . 泌乳素釋放因子………… …………………………………………………22
( 1 ) 激甲狀腺素…………………………………………………………… 22
( 2 ) 小腸收縮………………………………………………… …… ……23
肆、 材料與方法……………………………………………………………………………25
伍、 結果……………………………………………………………….………………………44
陸、 討論………………………………………………… ……………………………………53
柒、 結論…………………………………………… …… ……………………………………61
捌、 參考文獻…………………………………… …… …… ………………………………62
玖、 英文摘要…………………………………………………………………………………75

楊錫坤與馬春祥。1990。控制牡鹿生殖季節之機制。科學農業 38:373-
392。
陳俊吉、林武霆、劉漢根與楊錫坤。1998。類固醇與度巴胺拮抗劑給
予對梅花鹿鹿茸生產之影響。中畜會誌 27:383-393。
Amann, E., L. K. Mark and G. M. Willam. 1988. A Expression Vector pTrc99A.
Gene 69: 301-304.
Azad, N., J. P. Luckey and A. M. Lawance. 1988. Posterior pituitary lobectomy chronically attenuates the nocturnal surge of prolactin in early pregnancy .
70 th Annual Meeting of the Endocrine Society. pp. 63-64.
Barrera-Saldana, H. A., D. L. Robberson and G. F. Saunders. 1982.
Transcriptional products of the human placental lactogen gene. J. Biol.
Chem. 257:12399-12404.
Ben-Jonathan, N. 1985. Dopamine: a prolactin-inhibiting hormone. Endocr.
Reviews 6:564-589.
Boutin, J. M., C. Jolicoeur, H. Okamura, J. Gagnon, M. Edery, M. Shirota, D.
Banville, I., Djiane, J. Dusanter-Fourt and P. A. Kelly. 1988. Cloning and
expression of the rat prolactin receptor, a member of the growth
hormone/prolactin receptor gene family. Cell 53:69-77.
Bunzow, J. R., H. H. Van Tol, D. K. Grandy, P. Albert, J. Salon, M. Christie, C.
A. Machida, K. A. Neve and O. Civelli. 1988. Cloning and expression of a
rat D2 dopamine receptor cDNA. Nature 336: 783-787.
Carrillo, A. J., T. B. Pool and Z. D. Sharp. 1985. Vasoactive intestinal peptide
increases prolactin messenger ribonucleic acid content in GH3 cells.
Endocrinology 116: 202-206.
Chiu, S., R. D. Koos and P. M. Wise. 1992. Detection of prolactin receptor
(PRL-R) mRNA in the rat hypothalamus and pituitary gland.
Endocrinology 130: 1747-1749.
Chou, P. Y. and G. D. Fasman. 1978. Prediction of the secondary structure of
proteins from their amino acid sequence. Advances in Enzymology &
Related Areas of Molecular Biology 47: 145-148.
Clapp, C. 1987. Analysis of the proteolytic cleavage of prolactin by the
mammary gland and liver of the rat: characterization of the cleaved and
16K forms. Endocrinology 121: 2055-2064.
Compton, M. M. and R. J. Witorsch. 1984. Proteolytic degradation and
modification of rat prolactin by subcellular fractions of the rat ventral
prostate gland. Endocrinology 115: 476-484.
Connor, M. G., K. K. Frank and J. P. Johan. 1989. Proliferin gene and function.
Endocrinology 125: 334-337.
Cooke, N. E. and J. D. Baxter. 1982. Structural analysis of the prolactin gene
suggests a separate origin for its 5' end. Nature 297: 603-606.
Cooke, N. E., D. Coit, J. Shine, J. D. Baxter and J. A. Martial. 1981. Human
prolactin. cDNA structural analysis and evolutionary comparisons. J. Biol.
Chem. 256: 4007-4016.
Cooke, N. E., J. Ray, J. G. Emery and S. A. Liebhaber. 1988. Two distinct
species of human growth hormone-variant mRNA in the human placenta
predict the expression of novel growth hormone proteins. J. Biol. Chem.
263: 9001-9006.
Cooper, C. W., T. C. Peng, J. F. Obie and S. C. Garner. 1980. Calcitonin
immunoreactivity in rat and human pituitary glands: histochemical, in
vitro, and in vivo studies. Endocrinology 107: 98-107.
Crenshaw, E. B., D. Kalla, K. Simmons, D. M. Swanson and M. G. Rosenfeld.
1989. Cell-specific expression of the prolactin gene in transgenic mice is
controlled by synergistic interactions between promoter and enhancer
elements. Gene Develop. 3: 959-972.
Curlewis, J. D., A. S. I. Loudon, J. A. Milne and A. S. McNeilly. 1988. Effects
of chronic long-acting bromocriptine treatment on body weight, voluntary
food intake, coat growth and breeding season in non-pregnant red deer
hinds. J. Endocr. 119: 413-420.
Day, R. N., S. Koike, M. Sakai, M. Muramatsu and R. A. Maurer. 1990. Both
Pit-1 and the estrogen receptor are required for estrogen responsiveness of
the rat prolactin gene. Mol. Endocr. 4: 1964-1971.
Day, R. N. and R. A. Maurer. 1989. The distal enhancer region of the rat
prolactin gene contains elements conferring response to multiple hormones. Mol. Endocr. 3:3-9.
Demarest, K. T., G. D. Riegle and K. E. Moore. 1984. Prolactin-induced
activation of tuberoinfundibular dopaminergic neurons: evidence for both
a rapid 'tonic' and a delayed 'induction' component. Neuroendocrinology
38: 467-475.
Denoto, F. M., D. D. Moore and H. M. Goodman. 1981. Human growth hormone
DNA sequence and mRNA structure: possible alternative splicing. Nucleic
Acids Res. 9:3719-3730.
Diamond, S. E., M. Chiono and A. G. Hartmann. 1998. Reconstitution of the
protein kinase A response of the rat prolactin promoter: Differential
effects of distinct pit-1 isoform and functional interaction with Oct-1. Mol.
Endocr. 13: 228-238.
DiMattia, G. E., B. Gellersen., M. L. Duckworth and H. G. Friesen. 1990.
Human prolactin gene expression. J. Biol. Chem. 265: 16412-16421.
Djiane, J., H. Clauser and P. A. Kelly. 1986. Rapid down-regulation of prolactin
receptors in mammary gland and liver. Biochem. Biophysi. Res. Commun.
90: 1371-1378.
Duckworth, M. L., L. M. Peden and H. G. Friesen. 1986. Isolation of a novel
prolactin-like cDNA clone from developing rat placenta. J. Biol. Chem.
261: 10879-10884.
Dymshitz, J., M. Laudon and N. Ben-Jonathan. 1992. Endothelin-induced
biphasic response of lactotrophs cultured under different conditions.
Neuroendocrinology 55: 724-729.
Hadlay, M. E. 1992. Endocrinology third edition. pp. 139.
Emanuele, N. V., J. K. Jurgens., M. M. Halloran., J. J. Tentler., A. M. Lawrence
and M. R. Kelly. 1992. The rat prolactin gene is expression in brain tissue:
detection of normal and alternatively spliced prolactin m RNA. Mol. Endocr.
6: 35-42.
Ferrara, N., C. Clapp and R. I. Weiner. 1988. The 16k fragment of PRL regulate
in the proliferation of various cells. J. Biol. Chem. 324:231-237.
Fox, S. R., M. T. Jong, J. Casanova, Z. S Ye, F. Stanley and H. H. Samuels.
1990. The homeodomain protein, Pit-1/GHF-1, is capable of binding to and
activating cell-specific elements of both the growth hormone and prolactin
gene promoters. Mol. Endocr. 4: 1069-1080.
Frankenne, F., F. Rentier-Delrue, M. L. Scippo, J. Martial and G. Hennen. 1987.
Expression of the growth hormone variant gene in human placenta. J. Clin.
Endocr. Meta. 64: 635-637
Frawley, L. S and J. D. Neill. 1981. Stimulation of prolactin secretion in rhesus
monkeys by vasoactive intestinal polypeptide. Neuroendocrinology 33: 79-
83.
Garris, P. A. and N. Ben-Jonathan. 1991. Estradiol rapidly stimulates dopamine
release from the posterior pituitary in vitro. Neuroendocrinology 53: 601-
607.
Gourdji, D., D. Bataille, N. Vauclin, D. Grouselle, G. Rosselin and A. Tixier-
Vidal. 1979. Vasoactive intestinal peptide (VIP) stimulates prolactin (PRL)
release and cAMP production in a rat pituitary cell line (GH3/B6). Additive
effects of VIP and TRH on PRL release. FEBS. 104: 165-168.
Greenblatt, J. 1991. RNA polymerase-associated transcription factors. Tren.
Biochem. Sci. 16: 408-411.
Grosvenor, C. E and F. Mena. 1980. Evidence that thyrotropin-releasing
hormone and a hypothalamic prolactin-releasing factor may function in the
release of prolactin in the lactating rat. Endocrinology 107: 863-868.
Grumbach, M. M. and S. Kaplan. 1985. The PL of physiological role. Trans. NY.
Acad. Sci. 27: 167-188.
Haeuptle, M. T., M. L. Aubert, J. Djiane and J. P. Kraehenbuhl. 1983. Binding
sites for lactogenic and somatogenic hormones from rabbit mammary gland
and liver. J. Biol. Chem. 258: 305-314.
Haisenleder, D. J., J. A. Moy, R. R. Gala and D. M. Lawson. 1986. The effect of
transient dopamine antagonism on thyrotropin-releasing hormone-induced
prolactin release in ovariectomized rats treated with estradiol and/or
progesterone. Endocrinology 119: 1996-2003.
Hanks, M. C., R. T. Talbot and H. M. Sang.1989. Expression of biological active
recombinant-derved chicken prolactin in E. coli. J. Mol. Endocr. 3: 15-21.
Hashimoto, S., G. Fumagalli, A. Zanini and J. Meldolesi. 1987. Sorting of three
secretory proteins to distinct secretory granules in acidophilic cells of cow
anterior pituitary. J. Cell. Chem. 105: 1579-1586.
Healy, D. L. 1984. The clinical significance of endometrial prolactin. Australian
& New Zealand Journal of Obstetrics & Gynaecology 24: 111-116.
Hinkle, P. M. and A. H. Tashjian. 1973. Receptors for thyrotropin-releasing
hormone in prolactin producing rat pituitary cells in culture. J. Biol. Chem.
248: 6180-6186.
Hiraoka, Y., Y. Nomata., K. Matsuo., N. Tsubota., K. Tanbe and T. Fukasawa.
1991. Efficient production of biologically active human prolactin in E. coli .
Mol. Endocr. 5: 1763-1768.
Hoggard, N., J. R. Davis, M. Berwaer, P. Monget, B. Peers, A. Belayew and J. A
Martial. 1991. Pit-1 binding sequences permit calcium regulation of human
prolactin gene expression. Mol. Endocr. 5: 1748-1754.
Ingraham, H. A., R. P. Chen, H. J. Mangalam, H. P. Elsholtz, S. E. Flynn,, C. R. Lin, D. M. Simmons, L. Swanson and M. G. Rosenfeld. 1988. A tissue-specific transcription factor containing a homeodomain specifies a pituitary phenotype. Cell 55: 519-529.
Iverson, R. A., K. H. Day, M. d'Emden, R. N. Day and R. A. Maurer. 1990. Clustered point mutation analysis of the rat prolactin promoter. Mol. Endocr. 4: 1564-1571.
Jabbour, H. N., L. A. Clarke, S. Boddy, A. Pezet, M. Edery and P. A. Kelly. 1996. Cloning, sequencing and functional analysis of a truncated cDNA encoding red deer prolactin receptor: an alternative tyrosine residue mediates beta-casein promoter activation. Mol & Cell Endocr. 123: 17-26.
Kanyicska, B., T. P. Burris and M. E. Freeman. 1991. The effects of endothelins on the secretion of prolactin, luteinizing hormone, and follicle-stimulating hormone are mediated by different guanine nucleotide-binding proteins. Endocrinology 129: 2607-2613.
Karaseva, L. I. and A. Pankov. 1985. Primary structure of whale prolactin. Biochimie 50: 1528-1534.
Keyes P.L. and M. C. Wiltbank. 1988. Endocrine regulation of the corpus luteum. Annual Review of Physiology. 50: 465-482.
Kraeling, R. R., D. N. Marple, G. B. Rampacek, C. H. Rahe and J. L. Sartin.
1987. Effect of photoperiod and temperature on prolactin secertion in
ovariectomized gilt. J. Anim. Sci. 64: 1690-1695.
Laemmli, T. E. 1970. The new way "SDS-PAGE". J. Biol. Chem. 133: 145-
146.
Lam, K. S. 1991. Vasoactive intestinal peptide in the hypothalamus and pituitary.
Neuroendocrinology 53: 45-51.
Lechan, R. M. and I. M. Jackson. 1982. Immunohistochemical localization of thyrotropin-releasing hormone in the rat hypothalamus and pituitary. Endocrinology 111: 55-65.
Lewis, U. J., R. N. Singh, Y. N. Sinha and W. P. Vanderlaan. 1985. Glycosylated human prolactin. Endocrinology 116: 359-363.
Li, C. H. 1976. Studies on pituitary lactogenic hormone. The primary structure of
the ovine hormone. Inter. J. Pro. Res. 8: 205-224.
Li, C. H., J. S. Dixon., T. B. Lo., K. D. Schmidt and Y. A. Pankov. 1970. The
primary structure of the sheep hormone. Archives of Biochemistry&
Biophysics. 141: 705-707.
Linzer, D. I. and D. Nathans. 1985. A new member of the prolactin-growth
hormone gene family expressed in mouse placenta. EMBO 4: 1419-1423.
Linzer, D. I. and F. Talamantes. 1985. Nucleotide sequence of mouse prolactin and growth hormone mRNAs and expression of these mRNAs during pregnancy. J. Biol. Chem. 260: 9574-9579.
Linzer, D. I., S. J. Lee, L. Ogren, F. Talamantes and D. Nathans. 1985.
Identification of proliferin mRNA and protein in mouse placenta. Proc. Natl
Acad Sci USA 82: 4356-4359.
Lister, R. C., L. E. Underwood, R. N. Marshall and H. G. Friesen. 1974. Evidence
for a direct effect of thyrotropin-releasing hormone (TRH) on prolactin
release in humans. J. Clin. Endocr. Meta. 39: 1148-1150.
Lopez, K. L., L. J. Hill and J. P. Duncan. 1988. The dopamine inhibit the
prolactin by D2 receptor. Endocrinology 133: 147-149.
Luck, D. N. J. K. Rottman., F. M. Linzer and M. R. Smith. 1986. Synthesis of
bovine prolactin in E. coli. DNA 5: 24-28.
Mangalam, H. J., V. R. Albert, H. A. Ingraham, M. Kapiloff, L. Wilson, C.
Nelson and M. G. Rosenfeld. 1989. A pituitary POU domain protein, Pit-1,
activates both growth hormone and prolactin promoters transcriptionally.
Gene Develop. 3: 946-958.
Manku, M. S., D. F. Horrobin, H. Zinner, M. Karmazyn, R. O. Morgan, A. I. Ally and R. A. Karmali. 1977. Dopamine enhances the action of prolactin on rat blood vessels. Implications for dopamine effects on plasma prolactin. Endocrinology 101: 1343-1345.
Markoff, E. and D. W. Lee. 1987. Glycosylated prolactin is a major circulating variant in human serum. J. Clin. Endo. Meta. 65: 1102-1106.
Martin, T. F. 1992. Calcitonin peptide inhibition of TRH-stimulated prolactin secretion. TEME. 3: 82-85.
Martinez de la Escalera, G. and R. I. Weiner. 1988. Mechanism(s) by which the transient removal of dopamine regulation potentiates the prolactin-releasing action of thyrotropin-releasing hormone. Neuroendocrinology 47: 186-193.
Meuris, S., M. Svoboda, M. Vilamala, J. Christophe and C. Robyn. 1983.
Monomeric pituitary growth hormone and prolactin variants in man
characterized by immunoperoxidase electrophoresis. FEBS. 154:11-
17.
Morin, A., E. Rosenbaum and A. Tixier-Vidal. 1984. Effects of thyrotropin-
releasing hormone on prolactin compartments in normal rat pituitary cells in
primary culture. Endocrinology 115: 2278-2284.
Nagy, G., J. J. Mulchahey and J. D. Neill. 1988. Autocrine control of prolactin secretion by vasoactive intestinal peptide. Endocrinology 122: 364-366.
Nelson, C., E. B. Crenshaw, R. Franco, S. A. Lira, V. R. Albert, R. M. Evans and M. G. Rosenfeld. 1986. Discrete cis-active genomic sequences dictate the pituitary cell type-specific expression of rat prolactin and growth hormone genes. Nature 322: 557-562.
Nicoll, C. S. 1967. Bioassay of prolactin: analysis of the pigeon crop sac response to local prolactin injection by an objective and quantitative method. Endocrinology 80: 641-655.
Nielsen, P. V., H. Pedersen and E. M. Kampmann. 1979. Absence of human placental lactogen in an otherwise uneventful pregnancy. J. Obstetrics& Gynecology. 135: 322-326.
Owerbach, D., W. J. Rutter, N. E. Cooke, J. A. Martial and T. B. Shows. 1981. The prolactin gene is located on chromosome 6 in humans. Science 212: 815-816.
Owerbach, D., W. J. Rutter, J. A. Martial, J. D. Baxter and T. B. Shows. 1980.
Genes for growth hormone, chorionic somatommammotropin, and growth
hormones-like gene on chromosome 17 in humans. Science 209: 289-292.
Peers, B., M. L. Voz, P. Monget, M. Mathy-Hartert, M. Berwaer, A. Belayew and J. A. Martial. 1990. Regulatory elements controlling pituitary-specific expression of the human prolactin gene. Mol. Cell. Biol. 10: 4690-4700.
Provost, F., C. Leroux., P. Martin., P. Gaye and J. Djiane. 1994. Prolactin gene
expression in ovine and caprine mammary gland. Neuroendocrinology 60:
305-313.
Riddick, D. H. 1985. Studies of prolactin binding: tissue distribution, species variation and characterization.69 th annual Meeting of the Endocrine Society. New Orleans . Abstr. pp. 166.
Riddle, O., R. W. Bates and S. W. Dykshorn. 1933. The novel hormone in the pituitary. Am. J. Physiol. 105: 191-216.
Rosa, P., G. Fumagalli, A. Zanini and W. B. Huttner. 1985. The major tyrosine-sulfated protein of the bovine anterior pituitary is a secretory protein present in gonadotrophs, thyrotrophs,mammotrophs, and corticotrophs. J. Cell. Biol. 100: 928-937.
Roberson, M. C. and H. G. Friesen. 1981. Two form of rat placental lactogen
revealed by radioimmunoassay. Endocrinology 108: 2388-2390.
Russel, D. H., H. A. Bern and K. T. Mills. 1988. PRL location and secreation
70 th Annual Meeting of the Endocrine Society. Abstr. pp. 251.
Said, S. I. and J. C. Porter. 1979. Vasoactive intestinal polypeptide: release into hypophyseal portal blood. Life Sciences 24: 227-230.
Said and Mutt. 1970. Cited by Frawley, L. S. 1981. Stimulation of prolactin
secretion in rhesus monkey by vasoactive intestinal polypeptide.
Neuroendocrinology 33: 79-80.
Samson, W. K., S. I. Said and S. M. McCann. 1979. Radioimmunologic
localization of vasoactive intestinal polypeptide in hypothalamic and
extrahypothalamic sites in the rat brain. Neuroscience Letters 12: 265-269.
Sarkar, D. K. 1989. Evidence for prolactin feedback actions on hypothalamic oxytocin, vasoactive intestinal peptide and dopamine secretion. Neuroendocrinology 49: 520-524.
Sasavage, N. L., J. H. Nilson, S. Horowitz and F. M. Rottman. 1982. Nucleotide sequence of bovine prolactin messenger RNA. Evidence for sequence polymorphism. J. Biol. Chem. 257: 678-681.
Scott, H. P., K. L. Johan and K. K. Kelly. 1987. Dopamine for the prolactin signal transduction. J. Biol. Chem. 399: 1356-1359.
Seeburg, P. H., J. Shine., J. A. Martial., J. D. Baxter and H. M. Goodman. 1977.
Nucleotide sequence and amplification in bacteria of structural gene for rat
growth hormone. Nature 270: 486-494.
Shah, G.V., W. Wang, C. E. Grosvenor and W. R. Crowley. 1990. Calcitonin
inhibits basal and thyrotropin-releasing hormone-induced release of
prolactin from anterior pituitary cells: evidence for a selective action
exerted proximal to secretagogue-induced increases in cytosolic Ca2+.
Endocrinology 127: 621-628.
Shiu, R. P and J. A. Paterson. 1984. Alteration of cell shape, adhesion, and lipid accumulation in human breast cancer cells (T-47D) by human prolactin and growth hormone. Cancer Research 44: 1178-1186.
Sinha, Y. N., T. A. Gilligan, D. W. Lee, D. Hollingsworth and E. Markoff. 1985.
cleaved prolactin: evidence for its occurrence in human pituitary gland and
plasma. J. Clin. Endocr. Meta. 60: 239-243.
Shull, J. D and J. Gorski. 1986. The different hormone in the pituitary. Vitamin
and Hormones 43: 197-204.
Sinha, Y. N. and B. P. Jacobsen. 1987. Glycosylated prolactin in the murine
pituitary: detection by a novel assay and alteration of concentrations by
physiological and pharmacological stimuli. Biochem. Biophy. Res. Commun.
148: 505-514.
Seeburg, P. H., J. Shine., J. A. Martial., J. D. Baxter and H. M. Goodman. 1977.
Nucleotide sequence and amplification in bacteria of structural gene for rat
growth hormone. Nature 270: 486-494.
Stricker and Grueter 1928. Cited by Cooke, N. E., J. Ray, J. G. Emery and J. A. Martial. 1981. Human prolactin cDNA structural analysis and evolutionary comparison. J. Biol. Chem. 256: 4007-4008.
Theill, L. E., J. L. Castrillo, D. Wu and M. Karin. 1989. Dissection of functional domains of the pituitary-specific transcription factor GHF-1. Nature 342: 945-948.
Thomas, G. B., J. T. Cummins, B. Yao, K. Gordon and I. J. Clarke. 1988. Release of prolactin is independent of the secretion of thyrotrophin-releasing hormone into hypophysial portal blood of sheep. J. Endocr. 117: 115-122.
Tixier-Vidal, A., C. Tougard, B. Dufy and J. D. Vincent. 1982. The mechanism of signal transduction in PRL. Elsevier Biomedical. 1: 211-251.
Towin, M. M., J. P. Gordon and K. P. Jason. 1979. The new method "Western
blotting"J. Biol. Chem. 371: 334-338.
Vila-Porcile, E., R. Picart, A. Tixier-Vidal and C. Tougard. 1987. Cellular and
subcellular distribution of laminin in adult rat anterior pituitary. J. Histochem.
Cytochem. 35: 287-299.
Watahiki, M., M. Tanaka, N. Masuda, K. Sugisaki, M. Yamamoto, M. Yamakawa,
J. Nagai and K. Nakashima. 1989. Primary structure of chicken pituitary
prolactin deduced from the cDNA sequence. Conserved and specific amino
acid residues in the domains of the prolactins. J. Biol. Chem. 264: 5535-
5539.
Wallis, M. 1981. The molecular evolution of pituitary growth hormone、prolactin
and placental lactogen. J. Mol. Evol. 17: 10-18.
West, N. O. and H. C. Nordan. 1976 a. Hormonal regulation of reproduction and
the antler cycle in the male Columbian black-tauled deer . Part Ⅱ. The
effect of methallibure and hormone treatment. Can. J. Zool. 54: 1637-1656.
Yamamoto, M., T. Harigaya., T. Ichikawa and K. Hoshino. 1991. Recombinant
mouse prolactin: expression in E. coli , purification and biological activity.
J. Mol. Endocr. 8: 165-172.
Yasuda, A., H. Itoh and H. Kawauchi. 1986. Primary structure of chum salmon prolactins: occurrence of highly conserved regions. Arch. Biochem. Biophy. 244: 528-541.
Yoshizawa, T., O. Shinmi, A. Giaid, M. Yanagisawa, S. J. Gibson, S. Kimura, Y. Uchiyama, J. M. Polak, T. Masaki and I. Kanazawa. 1990. Endothelin: a novel peptide in the posterior pituitary system. Science 247: 462-464.

連結至畢業學校之論文網頁點我開啟連結
註: 此連結為研究生畢業學校所提供,不一定有電子全文可供下載,若連結有誤,請點選上方之〝勘誤回報〞功能,我們會盡快修正,謝謝!
QRCODE
 
 
 
 
 
                                                                                                                                                                                                                                                                                                                                                                                                               
第一頁 上一頁 下一頁 最後一頁 top
系統版面圖檔 系統版面圖檔