杨卫军
海洋生物化学及分子生物学
个性化签名
- 姓名:杨卫军
- 目前身份:
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学术头衔:
博士生导师
- 职称:-
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学科领域:
有机化学
- 研究兴趣:海洋生物化学及分子生物学
1992-1997年,在日本东京大学获得硕士和博士学位。在世界上首次在对虾的眼柄中成功地分离、纯化了6种具有血糖上升生理活性的CHH、一种具有蜕皮抑制生理活性MIH及具有色素调节作用的RPCH和PDH,阐明了它们所有的分子的一级结构、并且研究阐明了这些分子的生理活性与分子构造的相互关系。 1997-1998年,在日本理化学研究所博士后,进行了海洋甲壳类病毒的复制机理的分子生物学的研究。进行了病毒复制的功能基因组的构造解析。 1998-2000年,在日本科技厅任研究员,进行了有关对虾类卵黄蛋白的纯化,构造解析,产生部位解析及卵巢成熟过程中卵黄蛋白的形成与变化的研究。 2000-2002年,在美国西佛罗里达大学从事研究与教学工作,从海洋对虾类眼柄cDNA基因文库中克隆了2种与MIH/VIH相关的神经多肽基因并阐明了它们的mRNA产生部位。并从事了生物化学教学工作。 2002-,浙江大学教授并获得国家杰出青年基金,继续从事海洋生物化学及分子生物学的研究工作。在海洋极端环境下生物的对应性及特异性的研究上取得了初步的研究成果,获得了几种特异性功能基因,目前正在进行结果与功能的解析工作。 以上的研究成果在国际学术会议上作学术报告十余次。研究主要成果在国际上此领域的核心刊物上发表论文19篇(SCI),被引用次数超过200次,并且在日本获得了一项专利。申请者在这个领域上的研究受到世界同行的认可。特别是对神经多肽的分离纯化、分子构造解析、基因的克隆及表达的调控机理的研究有着丰富的经验。并且与日本、美国及德国的世界一流的研究室有着密切合作及交流,掌握着这个领域的最新发展动态及急需解决的问题。
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成果数
10
杨卫军, WEI-JUNG YANG, * KATSUMI AIDA, * AKIKO TERAUCHI, † HAFtUYUKI SONOBE† AND HIROMICHI NAGASAWAS‡
SSDI 01%-9781(95)02122-l,-0001,():
-1年11月30日
The characteristics and primary structure of AJL-1, one of the lectins in the skin mucus of the Japanese eel (Anguilla japonica), were examined. This lectin exhibited b-galactoside specific activity in a Ca2
Lectin, Ca2+, independent, b-Galactoside specific activity, Galectin, Skin mucus, The Japanese eel, Body surface, Streptococcus difficile
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杨卫军, N. K. Karouna-Renier*†, W.-J. Yang* and K. Ranga Rao*
Insect Molecular Biology (2003) 12(1), 19-26,-0001,():
-1年11月30日
In the present study we carried out the isolation and characterization of an HSC70 gene from two midges, Chironomus tentans and C. yoshimatsui. The HSC70 cDNAs are approximately 2424 (C. tentans) and 2464 bp (C. yoshimatsui) long, and contain 1950 and 1956 bp open reading frames, respectively. Analysis of genomic DNA revealed the presence of two introns in these genes. The 5' untranslated regions of the HSC70 genes are adenosine-rich, a feature found in inducible HSP70 genes. The nucleotide and amino acid sequences exhibit high identity with cytosolic HSC70s from other Dipterans. Northern hybridization indicated that HSC70 is expressed at all developmental stages, from embryo to adult, and Southern hybridization confirmed the presence of multiple HSP70 genes in Chironomus.
Chironomus,, HSC70,, midge,, stress proteins.,
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杨卫军, ATSURO OKUNO, WEI-JUN YANG, VIDYA JAYASANKAR, HISAKO SAIDO-SAKANAKA, DO THI THANH HUONG, SAFIAH JASMANI, MUHARIJADI ATMOMARSONO, THANUMALAYAPERUMAL SUBRAMONIAM, NAOAKI TSUTSUI, TSUYOSHI OHIRA, ICHIRO KAWAZOE, KATSUMI AIDA, AND MARCY N. WILDER*
JOURNAL OF EXPERIMENTAL ZOOLOGY 292: 417-429(2002),-0001,():
-1年11月30日
A cDNA encoding vitellogenin (Vg) in the giant freshwater prawn, Macrobrachium rosenbergii, was cloned based on the cDNA sequence of vitellin (Vn) fragments A-N and B-42 determined previously, and its amino acid sequence deduced. The open reading frame (ORF) encoded 2,537 amino acid residues and its deduced amino acid sequence possessed three consensus cleavage sites, R-X-R-R, similar to those reported in Vgs of insects. The deduced primary structure of Vg in M. rosenbergii was seen to be similar to that of Penaeus japonicus, especially in the N-terminal region. It is therefore likely that Vgs in crustacean species including prawns and other related decapods exhibit a similar structural pattern. Based on the deduced primary structure of Vg and analysis of the various Vg and Vn subunits found in the hemolymph and ovary during ovarian maturation, we demonstrated the post-translational processing of Vg in M. rosenbergii. This is the first time that Vg processing has been clearly demonstrated in a crustacean species. Vg, after being synthesized in the hepatopancreas, is considered to be cleaved by a subtilisin-like endoprotease to form two subunits, A and proB, which are then released into the hemolymph. In the hemolymph, proB is possibly cleaved by a processing enzyme of unknown identity to give rise to subunits B and C/D. The three processed subunits A, B, and C/D are sequestered by the ovary to give rise to three yolk proteins, Macr-VnA, VnB, and VnC/D. J. Exp. Zool. 292: 417-429, 2002.
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【期刊论文】Cloning of Precursors for Two MIH/VIH-Related Peptides in the Prawn, Macrobrachium rosenbergii
杨卫军, Wei-Jun Yang and K. Ranga Rao
Biochemical and Biophysical Research Communications 289, 407-413(2001),-0001,():
-1年11月30日
Two cDNA clones (634 and 1366 bp) encoding MIH/VIH (molt-inhibiting hormone/vitellogenesisinhibiting hormone)-related peptides were isolated and sequenced from a Macrobrachium rosenbergii eyestalk ganglia cDNA library. The clones contain a 360 and 339 bp open-reading frame, and their conceptually translated peptides consist of a 41 and 34 amino acid signal peptide, respectively, and a 78 amino acid residue mature peptide hormone. The amino acid sequences of the peptides exhibit higher identities with other known MIHs and VIH (44-69%) than with CHHs (28-33%). This is the first report describing the cloning and sequencing of two MIH/VIH-related peptides in a single crustacean species. Transcription of these mRNAs was detected in the eyestalk ganglia, but not in the thoracic ganglia, hepatopancreas, gut, gill, heart, or muscle.
Macrobrachium rosenbergii, eyestalk ganglia, molt-inhibiting hormone, vitellogenesisinhibiting hormone, cDNA sequence.,
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杨卫军, Do Thi Thanh Huong, Wei-Jun Yang, Atsuro Okuno, Marcy N. Wilder
Comparative Biochemistry and Physiology Part A 128(2001)317-326,-0001,():
-1年11月30日
Changes in free amino acidsŽFAA.in the hemolymph of the giant freshwater prawn, Macrobrachium rosenbergii, were examined in individuals exposed to varying salinities for up to 1 week. In freshwater and under conditions of low salinity, total FAA concentrations were maintained between approximately 0.85 and 1 mM and did not exhibit changes in response to salinity exposure. Under high salinities, total FAA concentrations increased dramatically, reaching up to 2.1 mM depending on treatment. Examination of individual amino acid concentrations revealed that these increases were based on specific changes in glycine, arginine, alanine, proline and lysine. Among these, alanine showed the greatest increases, resulting in levels six-fold higher under high salinity than in freshwater and under low salinity. The other amino acid species showed increases of 2.5-fold compared to original values. These five FAAs in freshwater and under low salinity together occupied approximately 45% of total FAA contents and under high salinity comprised more than 70% of total FAA contents. These results suggest that specific hemolymph FAAs are involved in mediating response to salinity exposure in freshwater prawns.
Crustacea, Free amino acids, Freshwater prawns, Hemolymph, Macrobrachium rosenbergii, Osmoeffectors, Osmoregulation, Salinity
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杨卫军, WEI-JUN YANG, TSUYOSHI OHIRA, NAOAKI TSUTSUI, THANUMALAYAPERUMAL SUBRAMONIAM, DO THI THANH HUONG, KATSUMI AIDA, AND MARCY N. WILDER*
JOURNAL OF EXPERIMENTAL ZOOLOGY 287: 413-422(2000),-0001,():
-1年11月30日
Four major yolk proteins, designated as vitellins (Vns) Macr-VnA, B, C, and D, were extracted from mature ovaries of Macrobrachium rosenbergii. These were purified to homogeneity by reversed-phase high performance liquid chromatography (HPLC) employing a unique separation system based on the hydrophobic properties of the Vn molecule. Using standard techniques of protein sequencing, more than 33 N-terminal and 57 internal amino acid residues were determined for each of the four Vns. The cDNA fragments encoding the four Vns were amplified by PCR using degenerate oligonucleotide primers derived from the N-terminal and internal amino acid sequences. These cDNA fragments were cloned, sequenced, and used as probes to examine the transcription of mRNAs encoding the four Vns. Significant accumulations of these mRNAs were observed in female hepatopancreas only, while mRNA expression was not detected in male hepatopancreas or any other female tissue including ovary, subepidermal adipose tissue, gill, and muscle. This is the first occasion in Crustacea in which multiple Vns were demonstrated to be synthesized simultaneously in a single tissue. J. Exp. Zool. 287: 413-422, 2000.
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【期刊论文】Characterization of Chromatophorotropic Neuropeptides from the Kuruma Prawn Penaeus japonicus
杨卫军, Wei-Jun Yang, *, Katsumi Aida, * and Hiromichi Nagasawa†,
General and Comparative Endocrinology 114, 415-424(1999),-0001,():
-1年11月30日
Three chromatophorotropic neuropeptide hormones were purified from an aqueous extract of the sinus glands of the kuruma prawn Penaeus japonicus by two steps of reverse-phase HPLC and their amino acid sequences determined. One of them was found to show pigment concentrating activity and to have an amino acid sequence identical with that of the known red pigment oncentrating hormone (RPCH), and therefore it was named Pej-RPCH. The other two peptides showed pigment dispersing hormone (PDH) activity and were named Pej-PDH-I and-II. They both consisted of 18 amino acid residues with a free amino-terminus and an amidated carboxyl-terminus, the sequences of Pej-PDH-I and-II being NSELINSLLGIPKVMTDAamide and NSELINSLLGLPKFMIDAamide, respectively. Three amino acid residues at positions 11, 14, and 16 differed between the two PDHs. Pej-PDH-II was about 5-, 7-, and 10-fold more potent than Pej-PDH-I for erythrophores, xanthophores, and melanophores, respectively. The major reason for the difference in potency between the two PDHs was attributed to differences in residues at position 16. In addition, they were found to be produced by a single individual. The order of sensitivity of the four types of chromatophores to Pej-RPCH and both PDHs was found to be erythrophores=xanthophores>melanophores>leukophores.
kuruma prawn, Penaeus japonicus, red pigment concentrating hormone, pigment dispersing hormone.,
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杨卫军, M. Khayat, *, † W.-J. Yang, ‡ K. Aida, ‡ H. Nagasawa, § A. Tietz, * B. Funkenstein, † and E. Lubzens†
General and Comparative Endocrinology 110, 307-318(1998),-0001,():
-1年11月30日
The present work shows for the first time that peptides belonging to the Crustacean hyperglycaemic hormone family (CHH-family hormones) from Penaeus japonicus affect protein and mRNA synthesis in in vitro-incubated ovarian explant fragments removed from vitellogenic females of Penaeus semisulcatus. Reduced levels of protein synthesis, determined by TCA-precipitable 35Slabeled proteins, were found in the presence of crude sinus gland extracts from both P. semisulcatus and P. japonicus. A similar inhibitory effect compared to controls was found with each of the seven CHH-family peptides. Non-CHH-family peptides did not reduce protein synthesis. Crude sinus gland extracts prepared from P. semisulcatus were at least 20-fold more effective than sinus gland extracts of P. japonicus. The inhibition level was directly related to the concentration of the peptide in the incubation media, but its degree varied among the different tested peptides. The profile of proteins synthesized during in vitro incubation was analyzed using polyacrylamide gel electrophoresis under denatured and reduced conditions (SDS-PAGE), followed by autoradiography. Synthesis of several proteins was reduced, including proteins with electrophoretic mobility similar to that of vitellin. mmunoprecipitation with antiserum prepared against native ovarian vitellin confirmed the inhibitory effect of CHH-family peptides on vitellin synthesis. The crude sinus gland extract and CHH-family peptides also inhibited RNA synthesis, as determined by [3H]uridine incorporation into mRNA of ovarian fragments. It is concluded that in addition to their role in carbohydrate metabolism, CHH-family peptides may also influence ovarian physiology in crustaceans.
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杨卫军, WEI-JUN YANG, * KATSUMI AIDA* AND HIROMICHI NAGASAWA†
PII S0196-9781(96)00332-4,-0001,():
-1年11月30日
YANG, W.-J., K. AIDA AND H. NAGASAWA. Amino acid sequences and activities of multiple hyperglycemic hormones from the Kuruma prawn, Penaeus japonicus. PEPTIDES 18(4) 479-485, 1997.-By means of a single-step reversed-phase HPLC, six CHH family peptides were isolated from sinus gland extracts of the kuruma prawn, Penaeus japonicus. Five of these peptides (Pej-SGP-Ⅰ,-Ⅱ,-Ⅲ,-Ⅴ, and -Ⅵ) expressed hyperglycemic activity and were considered to be the hyperglycemic hormones of this prawn. The amino acid sequences of the five peptides were determined (the amino acid sequence of Pej-SGP-III had been previously determined), revealing that all consisted of 72 amino acid residues with a free amino-terminus and an amidated carboxyl-terminus. They showed considerable sequence similarity to one another, but much less similarity to Pej-SGP-IV with molt-inhibiting activity, the sequence of which had also been determined previously. Examination of the dose-response relationship of these peptides showed that they were equally potent but had different efficacies, which were in the order of Pej-SGP-Ⅴ,-Ⅵ>-Ⅲ,-Ⅰ>-Ⅱ, corresponding well with their sequence characteristics.
Crustacean hyperglycemic hormone, Amino acid sequence, Sinus gland Kuruma prawn, Penaeus japonicus, Hyperglycemic activity
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杨卫军, WEI-JUNG YANG, * KATSUMI AIDA, * AKIKO TERAUCHI, † HARUYUKI SONOBE† AND HIROMICHI NAGASAWA†
SSDI 01%-9781(95)02122-l,-0001,():
-1年11月30日
YANG, W.-J., K. AIDA, A. TERAUCHI, H. SONOBE AND H. NAGASAWA. Amino acid sequence of a peptide with moltinhibiting activity from the kuruma prawn Penaeus japonicus. PEPTIDES 17(2) 197-202, 1996.--Six major peptides (Pej-SGP-I-VI) that belong to the CHH family have been isolated from the sinus gland extracts of the kuruma prawn Penaeusjaponicus. By in vitro assay using the Y-organ of the crayfish Procambarus clarkii, Pej-SGP-IV was found to be active in inhibiting ecdysteroid synthesis. We determined the complete amino acid sequence. Pej-SGP-IV consists of 77 amino acid residues, with both free aimno-and carboxyl-termini. The sequence of Pej-SGP-IV shows considerable similarity to that of MIH of the shore crab Carcinus maenas and less similarity to Pej-SGP-III, whose sequence has been previously determined.
Molt-inhibiting hormone, Penaeus japonicus, Y-organ, Sinus gland, Ecdysteroid, Kuruma prawn
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