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| DC 欄位 | 值 | 語言 |
|---|---|---|
| dc.contributor.advisor | 宋延齡 | |
| dc.contributor.author | Chun-Yu Lin | en |
| dc.contributor.author | 林均郁 | zh_TW |
| dc.date.accessioned | 2021-06-13T04:23:18Z | - |
| dc.date.available | 2011-07-28 | |
| dc.date.copyright | 2006-07-28 | |
| dc.date.issued | 2006 | |
| dc.date.submitted | 2006-07-21 | |
| dc.identifier.citation | [1] Perona JJ, Craik CS. Structural basis of substrate specificity in the serine proteases. Protein Sci 1995;4:337-360.
[2] Branden C, Tooze J. Introduction to Protein Structure. Garland Publishing, Inc: New York,1998. [3] Ross J, Jiang H, Kanost MR, Wang Y. Serine proteases and their homologs in the Drosophila melanogaster genome: an initial analysis of sequence conservation and phylogenetic relationships. Gene 2003;304:117-131. [4] Rawlings ND, Barrett AJ. Families of serine peptidases. Methods Enzymol 1994;244:19-61. [5] Jiang H, Kanost MR. The clip-domain family of serine proteinases in arthropods. Insect Biochem Mol Biol 2000;30:95-105. [6] Muta T, Hashimoto R, Miyata T, Nishimura H, Toh Y, Iwanaga S. Proclotting enzyme from horseshoe crab hemocytes. cDNA cloning, disulfide locations, and subcellular localization. J Biol Chem 1990;265:22426-22433. [7] Iwanaga S, Kawabata S, Muta T. New types of clotting factors and defense molecules found in horseshoe crab hemolymph: their structures and functions. J Biochem (Tokyo) 1998;123:1-15. [8] Smith CL, Giordano H, Schwartz M, DeLotto R. Spatial regulation of Drosophila snake protease activity in the generation of dorsal-ventral polarity. Development 1995;121:4127-4135. [9] Piao S, Song YL, Kim JH, Park SY, Park JW, Lee BL, Oh BH, Ha NC. Crystal structure of a clip-domain serine protease and functional roles of the clip domains. Embo J 2005;24:4404-4414. [10] Murugasu-Oei B, Rodrigues V, Yang X, Chia W. Masquerade: a novel secreted serine protease-like molecule is required for somatic muscle attachment in the Drosophila embryo. Genes Dev 1995;9:139-154. [11] Kawabata S, Tokunaga F, Kugi Y, Motoyama S, Miura Y, Hirata M, Iwanaga S. Limulus factor D, a 43-kDa protein isolated from horseshoe crab hemocytes, is a serine protease homologue with antimicrobial activity. FEBS Lett 1996;398:146-150. [12] Huang TS, Wang H, Lee SY, Johansson MW, Soderhall K, Cerenius L. A cell adhesion protein from the crayfish Pacifastacus leniusculus, a serine proteinase homologue similar to Drosophila masquerade. J Biol Chem 2000;275:9996-10001. [13] Lee SY, Soderhall K. Characterization of a pattern recognition protein, a masquerade-like protein, in the freshwater crayfish Pacifastacus leniusculus. J Immunol 2001;166:7319-7326. [14] Kwon TH, Kim MS, Choi HW, Joo CH, Cho MY, Lee BL. A masquerade-like serine proteinase homologue is necessary for phenoloxidase activity in the coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem 2000;267:6188-6196. [15] Lee KY, Zhang R, Kim MS, Park JW, Park HY, Kawabata S, Lee BL. A zymogen form of masquerade-like serine proteinase homologue is cleaved during pro-phenoloxidase activation by Ca2+ in coleopteran and Tenebrio molitor larvae. Eur J Biochem 2002;269:4375-4383. [16] Zhang G, Lu ZQ, Jiang H, Asgari S. Negative regulation of prophenoloxidase (proPO) activation by a clip-domain serine proteinase homolog (SPH) from endoparasitoid venom. Insect Biochem Mol Biol 2004;34:477-483. [17] Asgari S, Zhang G, Zareie R, Schmidt O. A serine proteinase homolog venom protein from an endoparasitoid wasp inhibits melanization of the host hemolymph. Insect Biochem Mol Biol 2003;33:1017-1024. [18] Yu XQ, Jiang H, Wang Y, Kanost MR. Nonproteolytic serine proteinase homologs are involved in prophenoloxidase activation in the tobacco hornworm, Manduca sexta. Insect Biochem Mol Biol 2003;33:197-208. [19] Buda ES, Shafer TH. Expression of a serine proteinase homolog prophenoloxidase-activating factor from the blue crab, Callinectes sapidus. Comp Biochem Physiol B Biochem Mol Biol 2005;140:521-531. [20] Simser JA, Mulenga A, Macaluso KR, Azad AF. An immune responsive factor D-like serine proteinase homologue identified from the American dog tick, Dermacentor variabilis. Insect Mol Biol 2004;13:25-35. [21] Sricharoen S, Kim JJ, Tunkijjanukij S, Soderhall I. Exocytosis and proteomic analysis of the vesicle content of granular hemocytes from a crayfish. Dev Comp Immunol 2005;29:1017-1031. [22] Veiga AB, Ribeiro JM, Guimaraes JA, Francischetti IM. A catalog for the transcripts from the venomous structures of the caterpillar Lonomia obliqua: identification of the proteins potentially involved in the coagulation disorder and hemorrhagic syndrome. Gene 2005;355:11-27. [23] Thompson JD, Higgins DG, Gibson TJ. CLUSTAL W: improving the sensitivity of progressive multiple sequence alignment through sequence weighting, position-specific gap penalties and weight matrix choice. Nucleic Acids Res 1994;22:4673-4680. [24] Falquet L, Pagni M, Bucher P, Hulo N, Sigrist CJ, Hofmann K, Bairoch A. The PROSITE database, its status in 2002. Nucleic Acids Res 2002;30:235-238. [25] Altschul SF, Madden TL, Schaffer AA, Zhang J, Zhang Z, Miller W, Lipman DJ. Gapped BLAST and PSI-BLAST: a new generation of protein database search programs. Nucleic Acids Res 1997;25:3389-3402. [26] Letunic I, Copley RR, Pils B, Pinkert S, Schultz J, Bork P. SMART 5: domains in the context of genomes and networks. Nucleic Acids Res 2006;34:D257-260. [27] Schultz J, Milpetz F, Bork P, Ponting CP. SMART, a simple modular architecture research tool: identification of signaling domains. Proc Natl Acad Sci U S A 1998;95:5857-5864. [28] Thompson JD, Gibson TJ, Plewniak F, Jeanmougin F, Higgins DG. The CLUSTAL_X windows interface: flexible strategies for multiple sequence alignment aided by quality analysis tools. Nucleic Acids Res 1997;25:4876-4882. [29] Kumar S, Tamura K, Nei M. MEGA3: Integrated software for Molecular Evolutionary Genetics Analysis and sequence alignment. Brief Bioinform 2004;5:150-163. [30] Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976;72:248-254. [31] Kim MS, Baek MJ, Lee MH, Park JW, Lee SY, Soderhall K, Lee BL. A new easter-type serine protease cleaves a masquerade-like protein during prophenoloxidase activation in Holotrichia diomphalia larvae. J Biol Chem 2002;277:39999-40004. [32] Muta T, Oda T, Iwanaga S. Horseshoe crab coagulation factor B. A unique serine protease zymogen activated by cleavage of an Ile-Ile bond. J Biol Chem 1993;268:21384-21388. [33] Jiang H, Wang Y, Kanost MR. Pro-phenol oxidase activating proteinase from an insect, Manduca sexta: a bacteria-inducible protein similar to Drosophila easter. Proc Natl Acad Sci U S A 1998;95:12220-12225. [34] Lee SY, Cho MY, Hyun JH, Lee KM, Homma KI, Natori S, Kawabata SI, Iwanaga S, Lee BL. Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae. Eur J Biochem 1998;257:615-621. [35] Satoh D, Horii A, Ochiai M, Ashida M. Prophenoloxidase-activating enzyme of the silkworm, Bombyx mori. Purification, characterization, and cDNA cloning. J Biol Chem 1999;274:7441-7453. [36] Klein SL, Strausberg RL, Wagner L, Pontius J, Clifton SW, Richardson P. Genetic and genomic tools for Xenopus research: The NIH Xenopus initiative. Dev Dyn 2002;225:384-391. [37] Leclerc V, Pelte N, El Chamy L, Martinelli C, Ligoxygakis P, Hoffmann JA, Reichhart JM. Prophenoloxidase activation is not required for survival to microbial infections in Drosophila. EMBO Rep 2006;7:231-235. [38] Jiang H, Wang Y, Yu XQ, Zhu Y, Kanost M. Prophenoloxidase-activating proteinase-3 (PAP-3) from Manduca sexta hemolymph: a clip-domain serine proteinase regulated by serpin-1J and serine proteinase homologs. Insect Biochem Mol Biol 2003;33:1049-1060. [39] Jiang H, Wang Y, Yu XQ, Kanost MR. Prophenoloxidase-activating proteinase-2 from hemolymph of Manduca sexta. A bacteria-inducible serine proteinase containing two clip domains. J Biol Chem 2003;278:3552-3561. [40] Chasan R, Anderson KV. The role of easter, an apparent serine protease, in organizing the dorsal-ventral pattern of the Drosophila embryo. Cell 1989;56:391-400. [41] DeLotto R, Spierer P. A gene required for the specification of dorsal-ventral pattern in Drosophila appears to encode a serine protease. Nature 1986;323:688-692. [42] Nagai T, Kawabata S. A link between blood coagulation and prophenol oxidase activation in arthropod host defense. J Biol Chem 2000;275:29264-29267. [43] Field SG, Kurtz J, Cooper EL, Michiels NK. Evaluation of an innate immune reaction to parasites in earthworms. J Invertebr Pathol 2004;86:45-49. [44] Lo CF, Ho C, H., Chen CH, Liu KF, Chiu YL, Yeh PY, Prng SE, Hsu HC, Liu HC, Chang CF, Su MS, Wang CH, Kou GH. Detection and tissue tropism of white spot syndrome baculovirus (WSBV) in captured brooders of Penaeus monodon with a special emphasis on reproductive organs. Dis Aquat Org 1997;30:53-72. [45] Song YL, Liu JJ, Chan LC, Sung HH. Glucan-induced disease resistance in tiger shrimp (Penaeus monodon). Dev Biol Stand 1997;90:413-421. [46] Smith VJ, Brown JH, Hauton C. Immunostimulation in crustaceans: does it really protect against infection? Fish Shellfish Immunol 2003;15:71-90. [47] Sritunyalucksana K, Wongsuebsantati K, Johansson MW, Soderhall K. Peroxinectin, a cell adhesive protein associated with the proPO system from the black tiger shrimp, Penaeus monodon. Dev Comp Immunol 2001;25:353-363. [48] Supungul P, Klinbunga S, Pichyangkura R, Hirono I, Aoki T, Tassanakajon A. Antimicrobial peptides discovered in the black tiger shrimp Penaeus monodon using the EST approach. Dis Aquat Organ 2004;61:123-135. [49] Steiner H. Peptidoglycan recognition proteins: on and off switches for innate immunity. Immunol Rev 2004;198:83-96. [50] Bachere E, Gueguen Y, Gonzalez M, de Lorgeril J, Garnier J, Romestand B. Insights into the anti-microbial defense of marine invertebrates: the penaeid shrimps and the oyster Crassostrea gigas. Immunol Rev 2004;198:149-168. [51] Johansson MW, Soderhall K. Isolation and purification of a cell adhesion factor from crayfish blood cells. J Cell Biol 1988;106:1795-1803. [52] Johansson MW, Lind MI, Holmblad T, Thornqvist PO, Soderhall K. Peroxinectin, a novel cell adhesion protein from crayfish blood. Biochem Biophys Res Commun 1995;216:1079-1087. [53] Ruoslahti E. RGD and other recognition sequences for integrins. Annu Rev Cell Dev Biol 1996;12:697-715. [54] Cheng W, Liu CH, Tsai CH, Chen JC. Molecular cloning and characterisation of a pattern recognition molecule, lipopolysaccharide- and beta-1,3-glucan binding protein (LGBP) from the white shrimp Litopenaeus vannamei. Fish Shellfish Immunol 2005;18:297-310. [55] Sritunyalucksana K, Lee SY, Soderhall K. A beta-1,3-glucan binding protein from the black tiger shrimp, Penaeus monodon. Dev Comp Immunol 2002;26:237-245. [56] Ling E, Yu XQ. Prophenoloxidase binds to the surface of hemocytes and is involved in hemocyte melanization in Manduca sexta. Insect Biochem Mol Biol 2005;35:1356-1366. | |
| dc.identifier.uri | http://tdr.lib.ntu.edu.tw/jspui/handle/123456789/33053 | - |
| dc.description.abstract | 含迴紋針功能區塊絲胺酸蛋白酶類似物（c-SPH）與節肢動物的多項先天性免疫反應有關；像是抗菌活性、細胞附著、病原模式辨認、調理作用、以及對原酚氧化酵素系統的調控。在本篇論文中，我們從草蝦血球中選殖出一段c-SPH的cDNA。這段cDNA全長1337 bp，包含一段1068 bp的載碼區，可轉譯出一段長355 個胺基酸的蛋白質；推繹出的蛋白質包含一段迴紋針功能區塊（clip domain）及一段不具催化活性的類絲胺酸蛋白酶功能區塊（SP-like domain）。此蛋白質的分子量推測為38 kDa、等電點推測為7.9。預測的signal peptide切位位於Gly21Gln22之間。我們從12種節肢動物中挑選出15條單一clip domain的SPHs進行多重序列比對分析；clip domains間的一致性低，而SP-like domains間的一致性大約在34%-46%。序列上較保守的區域位於一些特殊的胺基酸附近，這些胺基酸在有酵素活性的絲胺酸蛋白酶中負責與受質進行交互作用。親緣分析上，草蝦c-SPH與同樣是十足目中淡水螯蝦的低分子量mas-like protein最為相似，而比較不像鋏角亞門或是昆蟲綱的c-SPHs。巢狀反轉錄聚合酶連鎖反應顯示c-SPH mRNA的訊號在血球中最為強烈。該分子的抗菌活性、調理活性以及對原酚氧化酵素系統的調控則沒有被偵測到。草蝦c-SPH mRNA的表現量在葡聚醣浸泡後12天表現量上升，而在熱去活性弧菌浸泡後半小時表現量下降。重組c-SPH能夠顯著增強血球細胞的附著。這些結果顯示草蝦c-SPH參與了先天性的免疫反應。 | zh_TW |
| dc.description.abstract | Abstract
Clip domain serine protease homologs (c-SPHs) are involved in various innate immune functions in arthropods such as antimicrobial activity, cell adhesion, pattern recognition, opsonization, and regulation of the prophenoloxidase system. In the present study, we cloned a c-SPH cDNA from tiger shrimp (Penaeus monodon) hemocytes. It is 1337 bp in length with a coding region of 1068 bp consisting a protein of 355 amino acid residues. The deduced protein includes one clip domain and one catalytically inactive serine protease-like (SP-like) domain. Its molecular weight is estimated to be 38 kDa with an isoelectric point of 7.9. The predicted cutting site of the signal peptide is located between Gly21 and Gln22. We aligned 15 single clip domain SPH protein sequences from 12 arthropod species; the similarity of these clip domains is low and that of SP-like domains is from 34%-46%. The conserved regions are located near the amino acid residues which served as substrate interaction sites in catalytically active serine protease. Phylogenetically, the tiger shrimp c-SPH is most similar to a low molecular mass masquerade-like protein of crayfish, also a member of Decapoda, but less similar to c-SPHs in Chelicerata and Insecta. Nested reverse transcription polymerase chain reaction (RT-PCR) revealed that c-SPH mRNA is expressed most in tissues with the highest hemocyte abundance. Antimicrobial, opsonization and proPO regulation of the molecule were not detected. The expression of c-SPH mRNA in hemocytes was up-regulated at the 12 day post β-glucan immersion and down-regulated at 0.5 hr post heat-inactivated Vibrio immersion. Recombinant c-SPH could significantly enhance hemocyte adhesion. The results suggest that the shrimp c-SPH protein plays a role in innate immunity. | en |
| dc.description.provenance | Made available in DSpace on 2021-06-13T04:23:18Z (GMT). No. of bitstreams: 1 ntu-95-R94b41008-1.pdf: 761066 bytes, checksum: cda8e3a9229181496614c326c9c55937 (MD5) Previous issue date: 2006 | en |
| dc.description.tableofcontents | 頁數
誌謝...................................................i 中文摘要...............................................iv 英文摘要...............................................v 目錄...................................................vi 圖表目次...............................................vii 略稱對照...............................................viii 緒論...................................................1 材料和方法.............................................5 結果...................................................15 討論...................................................20 結語...................................................27 參考文獻...............................................28 表.....................................................35 圖.....................................................39 附錄...................................................50 | |
| dc.language.iso | zh-TW | |
| dc.subject | 類似物 | zh_TW |
| dc.subject | 草蝦 | zh_TW |
| dc.subject | 迴紋針功能區塊 | zh_TW |
| dc.subject | 絲胺酸蛋白酶 | zh_TW |
| dc.subject | serine protease homolog | en |
| dc.subject | tiger shrimp | en |
| dc.subject | clip domain | en |
| dc.title | 草蝦含迴紋針功能區塊絲胺酸蛋白酶類似物之選殖及定性 | zh_TW |
| dc.title | Cloning and Characterization of a Clip Domain Serine Protease Homolog in Tiger Shrimp (Penaeus monodon) | en |
| dc.type | Thesis | |
| dc.date.schoolyear | 94-2 | |
| dc.description.degree | 碩士 | |
| dc.contributor.oralexamcommittee | 宋宏紅,胡光宇,陳俊宏 | |
| dc.subject.keyword | 草蝦,迴紋針功能區塊,絲胺酸蛋白酶,類似物, | zh_TW |
| dc.subject.keyword | tiger shrimp,clip domain,serine protease homolog, | en |
| dc.relation.page | 52 | |
| dc.rights.note | 有償授權 | |
| dc.date.accepted | 2006-07-23 | |
| dc.contributor.author-college | 生命科學院 | zh_TW |
| dc.contributor.author-dept | 動物學研究研究所 | zh_TW |
| 顯示於系所單位： | 動物學研究所 | |
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