梁宋平
长期从事蛋白质及多肽结构与功能研究。
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- 姓名:梁宋平
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学术头衔:
博士生导师
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学科领域:
生物化学
- 研究兴趣:长期从事蛋白质及多肽结构与功能研究。
梁宋平,男,1946年生。1970年毕业于北京大学生物学系,1983年获北京大学生物化学硕士学位,1986年获北京大学生物化学博士学位,1986--1990年在美国波士顿大学化学系进行博士后研究。曾获北京大学王式仪化学奖,国家教委科技进步一等奖(集体),1991年国家学会部员会授予“中国有突出贡献博士学位获得者”称号,1993年国家劳动人事部授予“有突出贡献中青年专家”称号。1999年被国家教育部和国家人事部评为全国模范教师。
曾担任过湖南师范大学生命科学学院院长。现任湖南师范大学副校长、教授、博士生导师、湖南师范大学蛋白质组学及发育生物学教育部重点实验室主任,湖南省生物化学与分子生物学学会理事长,中国生物化学与分子生物学学会理事,北京大学生命科学学院生物化学系兼职教授、生物化学与分子生物学专业兼职博士生导师。
长期从事蛋白质及多肽结构与功能研究,近年来在蜘蛛毒素和蛋白质组学研究领域连续获得6项国家自然科学基金项目和两项“863”项目及一项“973”项目资助。获湖南省科技进步一等奖,获得国家发明专利5项,国际专利一项,先后在J. Biol. Chem, Peptides, Analytical Biochemistry, J, Protein Chmistry中国科学等刊物上发表论文七十余篇,被国内外同引用三百余次,两次应邀出席国际生物毒素学术会议作大会发言。梁宋平教授已在北京大学和湖南师范大学共培养出博士研究生7人,硕士生52人。
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梁宋平, Songping Liang*
Toxicon 43(2004)575-585,-0001,():
-1年11月30日
The bird spider Selenocosmia huwena Wang [=Ornithoctonus huwena (Wang)] is one of the most venomous spiders in China. The venom of this spider contains a mixture of compounds with different types of biological activity. About 400 proteins and peptides from the venom can be separated and detected by 2D electrophoresis. Of these, 14 peptide toxins have been purified and characterized from the venom of this spider, with several peptide toxins exhibiting structural similarity but high functional diversity. Most of these huwentoxins (HWTX) contain 30–40 amino acids with three disulfide bonds and adopt an‘inhibitor cystine-knot'(ICK) motif in their three dimensional structure, except for huwentoxin-II (HWTX-II) which adopts a novel scaffold different from the ICK motif. As a group, the toxins possess quite different biological activities including inhibition of voltage-gated calcium and sodium channels, insecticidal activity, lectin-like agglutination, and inhibition of trypsin. Eight cDNAs encoding seven toxins, HWTX-I, -II, -III, -IIIa, -IV -V, and, -VII and one lectin, S. huwena lectin-I (SHL-I), have been cloned and sequenced. Comparison of the cDNA sequences of the eight peptides from S. huwena indicates that they can be classified into two different superfamilies according to the‘prepro'region of their cDNA sequences.q 2004 Elsevier Ltd. All rights reserved.
Selenocosmia huwena, Ornithoctonus huwena, Spider, cDNA, Peptite toxin, Three-dimensional structure
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梁宋平, Yucheng Xiao, Jianzhou Tang, Yuejun Yang, Meichi Wang, Weijun Hu, Jinyun Xie, Xiongzhi Zeng, and Songping Liang‡
THE JOURNAL OF BIOLOGICAL CHEMISTRY 279(2004)26220-26226,-0001,():
-1年11月30日
We have isolated a cardiotoxin, denoted jingzhaotoxin-III (JZTX-III), from the venom of the Chinese spider Chilobrachys jingzhao. The toxin contains 36 residues stabilized by three intracellular disulfide bridges (I-IV, II-V, and III-VI), assigned by a chemical strategy of partial reduction and sequence analysis. Cloned and sequenced using 3 -rapid amplification of cDNA ends and 5 -rapid amplification of cDNA ends, the full-length cDNA encoded a 63-residue precursor of JZTX-III. Different from other spider peptides, it contains an uncommon endoproteolytic site (-X-Ser-) anterior to mature protein and the intervening regions of 5 residues, which is the smallest in spider toxin cDNAs identified to date.Under whole cell recording, JZTX-III showed no effects on voltage-gated sodium channels (VGSCs) or calcium channels in dorsal root ganglion neurons, whereas it significantly inhibited tetrodotoxin-resistant VGSCs with an IC50 value of0.38M in rat cardiac myocytes.Different from scorpion -toxins, it caused a 10-mV depolarizing shift in the channel activation threshold. The binding site for JZTX-III on VGSCs is further suggested to be site 4 with a simple competitive assay, which at 10M eliminated the slowing currents induced by Buthus martensi Karsch I (BMK-I, scorpion-like toxin) completely.JZTX-III shows higher selectivity for VGSC isoforms than other spider toxins affecting VGSCs, and the toxin hopefully represents an important ligand for discriminating cardiac VGSC subtype.
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梁宋平, Dongling Li‡, Yucheng Xiao§, Xia Xu§, Xia Xiong§, Shanyun Lu‡, Zhonghua Liu§, Qi Zhu§, Meichi Wang§, Xiaocheng Gu‡, and Songping Liang§¶
THE JOURNAL OF BIOLOGICAL CHEMISTRY 279(2004)37734-37740,-0001,():
-1年11月30日
Hainantoxin-IV (HNTX-IV) can specifically inhibit the neuronal tetrodotoxin-sensitive sodium channels and defines a new class of depressant spider toxin. The se-quence of native HNTX-IV is ECLGFGKGCNPSNDQCCKSSNLVCSRKHRWCKYEI-NH2. In the present study,to obtain further insight into the primary and tertiary structural requirements of neuronal sodium channel blockers, we determined the solution structure of HNTX-IV as a typical inhibitor cystine knot motif and synthesized four mutants designed based on the predicted sites followed by structural elucidation of two inactive mutants. Pharmacological studies indicated that the S12A and R26A mutants had activities near that of native HNTX-IV, while K27A and R29A demonstrated activities reduced by 2 orders of magnitude. 1H MR analysis showed the similar molecular conformations for native HNTX-IV and four synthetic mutants. Furthermore,in the determined structures of K27A and R29A,the side chains of residues 27 and 29 were located in the identical spatial position to those of native HNTX-IV.These results suggested that residues Ser12, Arg26, Lys27,and Arg29 were not responsible for stabilizing the distinct conformation of HNTX-IV, but Lys27 and Arg29 were critical for the bioactivities. The potency reductions produced by Ala substitutions were primarily due to the direct interaction of the essential residues Lys27 and Arg29 with sodium channels rather than to a conformational change. After comparison of these structures and activities with correlated toxins, we hypothesized that residues Lys27, Arg29, His28, Lys32, Phe5, and Trp30 clustered on one face of HNTX-IV were responsible for ligand binding.
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梁宋平, Lingyun Huang, Bingxia Li, Chen Luo, Jinyun Xie, Ping Chen, Songping Liang
Proteomics 4(2004)235-243,-0001,():
-1年11月30日
Recently, it was found that in the gynogenetic haploid and diploid embryos of goldfish, which have exactly the same genome, the haploid condition results in obstruction of gene expression and abnormal development while the diploid embryos have normal gene expression and development. A diploid-dependent regulatory apparatus was proposed to regulate gene expression. To study the difference at the protein expression level of the embryos of haploid and diploid in development, we extracted the total proteins of both the gynogenetic haploid and diploid embryos of goldfish in the same eye formation stage. Two-dimensional polyacrylamide gel electrophoresis was used to separate proteins. The stained gel images were analyzed with the PDQUEST software.A part of protein spots that were differentially expressed in haploid and diploid embryos were identified by matrix assisted laser desorption/ionisation-time of flightmass spectrometry and database analysis. Sixteen protein spots that were absolutely different (only expressed in diploid embryos but not in haploid embryos or vice versa)and 16 protein spots that were up- and downregulated were identified unambiguously,which include some proteins that are correlative with eyes development, nerve development,developing regulation, cell differentiation, and signal transduction. The different significantly gene expression during embryos developing between diploid and haploid is demonstrated.
Goldfish embryo, Mass spectrometry, Proteome analysis, Two-dimensional gel electrophoresis
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梁宋平, Yucheng Xiao, Songping Liang*
European Journal of Pharmacology 477(2003)1-7,-0001,():
-1年11月30日
Hainantoxin-III and hainantoxin-IV, isolated from the venom of the Chinese bird spider Seleconosmia hainana, are neurotoxic peptides composed of 33–35 residues with three disulfide bonds. Using whole-cell patch-clamp technique, we investigated their action on ionic channels of adult rat dorsal root ganglion neurons. It was found that the two toxins did not affect Ca2+channels (both high voltage activated and low voltage activated types) nor tetrodotoxin-resistant voltage-gated Na+ channels (VGSCs). However, hainantoxin-III and hainantoxin-IV strongly depressed the amplitude of tetrodotoxin-sensitive Na+ currents with IC50 values of 1.1 and 44.6nM, respectively. Both hainantoxin-III (1nM) and hainantoxin-IV (50nM) caused a hyperpolarizing shift of about 10mV in the voltage midpoint of steady-state Na+ channel inactivation, but they showed difference in the reprime kinetics of VGSCs: hainantoxin-III significantly decreased the recovery rate from inactivation at a prepulse potential of 80mV while hainantoxin-IV did not do. It is interesting to note that similar to huwentoxin-IV, the two hainantoxins did not affect the activation and inactivation kinetics of Na+ currents and at a concentration of 1AM they completely inhibited the slowing inactivation currents induced by BMK-I (toxin I from the scorpion Buthus martensi Karsch), a scorpion a-like toxin.The results indicate that hainantoxin-III and hainantoxin-IV are novel spider toxins and affect the mammal neural Na+ channels through a mechanism quite different from other spider toxins targeting the neural receptor site 3, such as y-aractoxins and A-agatoxins.
Spider toxin, Dorsal ganglion neuron, Na+, current, Patch-clamp,, whole-cell
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梁宋平, Dongling Li a, Yucheng Xiao b, Weijun Hu b, Jinyun Xie b, Frank Bosmans c, Jan Tytgat c, Songping Liang b, *
FEBS Letters 555(2003)616-622,-0001,():
-1年11月30日
Hainantoxin-I is a novel peptide toxin, purified from the venom of the Chinese bird spider Selenocosmia hainana(=Ornithoctonus hainana). It includes 33 amino acid residues with a disulfide linkage of I-IV, II-V and III-VI, assigned by partial reduction and sequence analysis. Under two-electrode voltage-clamp conditions, hainantoxin-I can block rNav1.2/B1 and the insect sodium channel para/tipE expressed in Xenopus laevis oocytes with IC50 values of 68
Hainantoxin-i, Neurotoxin, Sodium channel, Solution structure, ICK motif
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梁宋平, Yu-Cheng Xiao, Song-Ping Liang*
Toxicon 41(2003)643-650,-0001,():
-1年11月30日
A neurotoxic peptide, named Hainantoxin-V (HNTX-V), was isolated from the venom of the Chinese bird spider Selenocosmia hainana. The complete amino acid sequence of HNTX-V has been determined by Edman degradation and found to contain 35 amino acid residues with three disulfide bonds. Under whole-cell patch-clamp mode, HNTX-V was proved to inhibit the tetrodotoxin-sensitive (TTX-S) sodium currents while it had no any effects on tetrodotoxin-resistant (TTX-R) sodium currents on adult rat dorsal root ganglion neurons. The inhibition of TTX-S sodium currents by HNTX-V was tested to be concentrate-dependent with the IC50 value of 42.3nM. It did not affect the activation and inactivation kinetics of currents and did not have the effect on the active threshold of sodium channels and the voltage of peak inward currents. However,100nM HNTX-V caused a 7.7mV hyperpolarizing shift in the voltage midpoint of steady-state sodium channel inactivation.The results indicated that HNTX-V inhibited mammalian voltage-gated sodium channels through a novel mechanism distinct from other spider toxins such as d-ACTXs, m-agatoxins I-VI which bind to receptor site three to slow the inactivation kinetics of sodium currents.
Spider, Sodium current, Whole-cell recording, Dorsal root ganglion
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梁宋平, Peng-Fei Zhang, Ping Chen, Wei-Jun Hu, Song-Ping Liang*
Toxicon 42(2003)15-20,-0001,():
-1年11月30日
two toxins exhibits sequence identity with other spider toxins such as ProTx-I (64%), SGTx (57%), SNX-482 (55%), and Hanatoxin (54%). HWTX-V can reversibly paralyze locusts and cockroaches for several hours with a ED50 value as 16±5mg/g to locusts, and a larger dose of the toxin can cause death. However, mHWTX-V shows no significant effect on locusts and cockroaches. The structure–activity relationship indicates that the residues Phe34 and Ser35 in the C-terminus of HWTX-V are the key residues of the biological activity.c 2003 Elsevier Science Ltd. All rights reserved.
Huwentoxin-V, The mutant of Huwentoxin-V, Key amino acid residues, Insecticidal toxin
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【期刊论文】Comparative proteomics analysis of human lung squamous carcinoma☆
梁宋平, Cui Li, a, b Zhuchu Chen, b, * Zhiqiang Xiao, a Xiaoying Wu, b Xianquan Zhan, b Xiaopeng Zhang, b Maoyu Li, b JianLing Li, a Xueping Feng, a Songping Liang, c Ping Chen, c and Jing-yun Xiec
Biochemical and Biophysical Research Communications 309(2003)253-260,-0001,():
-1年11月30日
Two-dimensional polyacrylamide gel electrophoresis (2-DE) profiles of human lung squamous carcinoma tissue and paired surrounding normal bronchial epithelial tissue were compared. Selected differential protein-spots were identified with peptide mass fingerprinting based on matrix-assisted laser desorption/ionization time-of-flight mass spectrometry (MALDI-TOF-MS) and database searching. Well-resolved and reproducible 2-DE patterns of both the tumor and the normal tissues were acquired. The average deviations of spot position were 0.873 0.125mm in IEF direction and 1.025 0.213mm in SDS–PAGE direction, respectively. For the tumor tissues, a total of 1349 67 spots were detected and 1235 48 spots were matched with an average matching rate of 91.5%. For the corresponding normal tissues, a total of 1297 73 spots were detected and 1183 56 spots were matched with an average matching rate of 91.2%. A total of 1069 45 spots were matched between the tumor and the normal tissues. Forty differential proteins between tumor and normal tissues were characterized. Some proteins were the products of oncogenes and others were involved in the regulation of cell cycle and signal transduction. These data are valuable for mass identification of differentially expressed proteins involved in lung carcinogenesis, establishing human lung cancer proteome databaseand screening molecular marker to further study human lung squamous carcinoma.2003 Published by Elsevier Inc.
Human lung squamous carcinoma tissue, Normal bronchial epithelial tissue, 2-DE PAGE, MALDI-TOF-MS, Proteome, Differential expression protein
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