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  1. Article: Cloning and Sequence Analysis of cDNAs Encoding Two Acidic PLA(2) from venom of Ophiophagus hannah(King Cobra), Guangxi Species.

    Wang, Qiu-Yan / Shu, Yu-Yan / Zhuang, Mao-Xing / Lin, Zheng-Jiong

    Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

    2001  Volume 33, Issue 3, Page(s) 340–344

    Abstract: Total RNA was extracted from venom glands of Ophiophagus hannah, Guangxi species. The cDNAs encoding PLA(2) were amplified by RT-PCR and cloned into the PUCm-T vector. The positive clones encoding two acidic PLA(2) (APLA(2)-1 and APLA(2)-2) were selected ...

    Abstract Total RNA was extracted from venom glands of Ophiophagus hannah, Guangxi species. The cDNAs encoding PLA(2) were amplified by RT-PCR and cloned into the PUCm-T vector. The positive clones encoding two acidic PLA(2) (APLA(2)-1 and APLA(2)-2) were selected and bidirectionally sequenced. Their complete amino acid sequences were deduced and found to be identical to the known amino acid sequences. Their isoelectric points calculated by computer agreed with the values determined with their protein. Homology analysis indicated that the mature peptide of APLA(2)-1 had high homology with PLA(2) from venoms of Ophiophagus hannah, Fujian and Taiwan species, but APLA(2)-2 had lower homology. The most striking difference between APLA(2)-2 and other PLA(2) from Ophiophagus hannah venoms is the missing of a extra "pancreatic loop" at residues 62--66 in APLA(2)-2, and it may be related to their species evolution and biological activity.
    Language English
    Publishing date 2001
    Publishing country China
    Document type Journal Article
    ZDB-ID 2175256-4
    ISSN 1745-7270 ; 0582-9879 ; 1672-9145
    ISSN (online) 1745-7270
    ISSN 0582-9879 ; 1672-9145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  2. Article ; Online: Structural and functional insights into lipid-bound nerve growth factors.

    Tong, Qiong / Wang, Feng / Zhou, Hong-Zhe / Sun, Han-Li / Song, Hui / Shu, Yu-Yan / Gong, Yong / Zhang, Wen-Ting / Cai, Tan-Xi / Yang, Fu-Quan / Tang, Jie / Jiang, Tao

    FASEB journal : official publication of the Federation of American Societies for Experimental Biology

    2012  Volume 26, Issue 9, Page(s) 3811–3821

    Abstract: Nerve growth factor (NGF) is a dimeric molecule that modulates the survival, proliferation, and differentiation of nervous cells and is also known to act on cells of the immune system and endocrine system. NGFs extracted from mouse submaxillary gland and ...

    Abstract Nerve growth factor (NGF) is a dimeric molecule that modulates the survival, proliferation, and differentiation of nervous cells and is also known to act on cells of the immune system and endocrine system. NGFs extracted from mouse submaxillary gland and cobra venom have different immunological behaviors, yet the underlying mechanism remains unclear. Here we report the crystal structure of the NGF purified from Chinese cobra Naja naja atra (cNGF), which unexpectedly reveals a 2-tailed lipid molecule that is embedded between the two protomers of the NGF homodimer. In addition, crystallographic analysis indicated that the purified mouse NGF(mNGF) is free from lipid but can bind lysophosphatidylserine (lyso-PS) in the same pocket as cNGF. Bioassays indicated that the binding of lipid molecules to cNGF and mNGF are essential for their mast cell activation activity and abates their p75(NTR) binding capacity. Taken together, these results suggest a new mechanism for the regulation of the function of NGF.
    MeSH term(s) Amino Acid Sequence ; Animals ; Crystallography, X-Ray ; Elapidae ; Histamine Release/drug effects ; Humans ; Lipids/chemistry ; Mast Cells/drug effects ; Models, Molecular ; Molecular Sequence Data ; Nerve Growth Factors/chemistry ; Nerve Growth Factors/isolation & purification ; Nerve Growth Factors/metabolism ; Nerve Growth Factors/pharmacology ; Sequence Homology, Amino Acid ; Spectrometry, Mass, Matrix-Assisted Laser Desorption-Ionization ; Structure-Activity Relationship
    Chemical Substances Lipids ; Nerve Growth Factors
    Language English
    Publishing date 2012-09
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 639186-2
    ISSN 1530-6860 ; 0892-6638
    ISSN (online) 1530-6860
    ISSN 0892-6638
    DOI 10.1096/fj.12-207316
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  3. Article: Preliminary Crystallographic Analysis of Phospholipase A(2) from Naja naja kaouthia Lesson Venom.

    Wang, Zhi-Qing / Zhuang, Mao-Xin / Song, Shi-Ying / Lin, Zheng-Jiong / Shu, Yu-Yan

    Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

    2001  Volume 33, Issue 5, Page(s) 582–584

    Abstract: An acidic phospholipase A(2) isolated from the venom of Naja naja kaouthia Lesson in Guangxi exhibits anticoagulative and hemolytic activities. In this work, the enzyme was crystallized by the method of hanging drop vapor diffusion. Two crystal forms ... ...

    Abstract An acidic phospholipase A(2) isolated from the venom of Naja naja kaouthia Lesson in Guangxi exhibits anticoagulative and hemolytic activities. In this work, the enzyme was crystallized by the method of hanging drop vapor diffusion. Two crystal forms were obtained and characterized by X-ray diffraction. One of them belonged to space group P 4 ( 3 ) 2 ( 1 )2 or P4(1)2(1)2 with unit cell parameters a b 8.797 nm, c 10.831 nm and there were three molecules per asymmetric unit the other belonged to space group P2(1)3 with unit cell parameters a b c 6.840 nm and there was one molecule per asymmetric unit. The diffraction data were collected up to 0.28 nm for each crystal form. The crystal properties of Naja naja verom phospholipase A(2) from different geographical regions are compared.
    Language English
    Publishing date 2001
    Publishing country China
    Document type Journal Article
    ZDB-ID 2175256-4
    ISSN 1745-7270 ; 0582-9879 ; 1672-9145
    ISSN (online) 1745-7270
    ISSN 0582-9879 ; 1672-9145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  4. Article: NGF-Tf Conjugate Prevents Degeneration of Substantia Nigra Neurons in a Mouse Model of Parkinson's Disease.

    Li, Xiao-Biao / Liao, Gong-Shan / Huang, Shao-Ming / Shu, Yu-Yan / Tang, Sheng-Xi

    Sheng wu hua xue yu sheng wu wu li xue bao Acta biochimica et biophysica Sinica

    2000  Volume 32, Issue 4, Page(s) 413–416

    Abstract: Nerve growth factor(NGF) was purified from Naja naja atra snake venom and conjugated to transferrin(Tf). This conjugate was intravenously injected into a mouse model of Parkinson's disease (PD). Both immunohistochemical staining and pathological ... ...

    Abstract Nerve growth factor(NGF) was purified from Naja naja atra snake venom and conjugated to transferrin(Tf). This conjugate was intravenously injected into a mouse model of Parkinson's disease (PD). Both immunohistochemical staining and pathological detection showed that the NGF-Tf conjugate could prevent the loss of tyrosine hydroxylase-immunoreactive neurons located in substantia nigra and the cell counts of NGF group were 2 330.0+/-260.3, and those of the MPTP group and the control group were 797.0+/-121.4 and 2 381.0+/-158.0, respectively. In addition, electron microscopic examination revealed significant protection against demyelination and vacuolation in subtantia nigra neurons in contrast to the control group. The i.v. injected NGF-Tf conjugate also reversed the neurodegenerative changes such as karyopyknosis, chromatolysis and intracytoplasmic inclusion in diseased neurons.
    Language English
    Publishing date 2000
    Publishing country China
    Document type Journal Article
    ZDB-ID 2175256-4
    ISSN 1745-7270 ; 0582-9879 ; 1672-9145
    ISSN (online) 1745-7270
    ISSN 0582-9879 ; 1672-9145
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  5. Article: Structure of a cardiotoxic phospholipase A(2) from Ophiophagus hannah with the "pancreatic loop".

    Zhang, Hai-Long / Xu, Su-Juan / Wang, Qiu-Yan / Song, Shi-Ying / Shu, Yu-Yan / Lin, Zheng-Jiong

    Journal of structural biology

    2002  Volume 138, Issue 3, Page(s) 207–215

    Abstract: The crystal structure of an acidic phospholipase A(2) from Ophiophagus hannah (king cobra) has been determined by molecular replacement at 2.6-A resolution to a crystallographic R factor of 20.5% (R(free)=23.3%) with reasonable stereochemistry. The venom ...

    Abstract The crystal structure of an acidic phospholipase A(2) from Ophiophagus hannah (king cobra) has been determined by molecular replacement at 2.6-A resolution to a crystallographic R factor of 20.5% (R(free)=23.3%) with reasonable stereochemistry. The venom enzyme contains an unusual "pancreatic loop." The conformation of the loop is well defined and different from those in pancreas PLA(2), showing its structural variability. This analysis provides the first structure of a PLA(2)-type cardiotoxin. The sites related to the cardiotoxic and myotoxic activities are explored and the oligomer observed in the crystalline state is described.
    MeSH term(s) Amino Acid Sequence ; Animals ; Binding Sites ; Cobra Cardiotoxin Proteins/chemistry ; Crystallography, X-Ray ; Elapidae/metabolism ; Electrons ; Models, Molecular ; Molecular Sequence Data ; Phospholipases A/chemistry ; Protein Binding ; Protein Conformation ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid ; Structure-Activity Relationship
    Chemical Substances Cobra Cardiotoxin Proteins ; Phospholipases A (EC 3.1.1.32)
    Language English
    Publishing date 2002-09-08
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 1032718-6
    ISSN 1095-8657 ; 1047-8477
    ISSN (online) 1095-8657
    ISSN 1047-8477
    DOI 10.1016/s1047-8477(02)00022-9
    Database MEDical Literature Analysis and Retrieval System OnLINE

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  6. Article: Structural and functional analysis of natrin, a venom protein that targets various ion channels.

    Wang, Feng / Li, He / Liu, Ming-na / Song, Hui / Han, Hong-mei / Wang, Qiong-ling / Yin, Chang-chen / Zhou, Yuan-cong / Qi, Zhi / Shu, Yu-yan / Lin, Zheng-jiong / Jiang, Tao

    Biochemical and biophysical research communications

    2006  Volume 351, Issue 2, Page(s) 443–448

    Abstract: Cysteine-rich secretory proteins (CRISPs) are secreted single-chain proteins found in different sources. Natrin is a member of the CRISP family purified from the snake venom of Naja naja atra, which has been reported as a BKca channel blocker. In our ... ...

    Abstract Cysteine-rich secretory proteins (CRISPs) are secreted single-chain proteins found in different sources. Natrin is a member of the CRISP family purified from the snake venom of Naja naja atra, which has been reported as a BKca channel blocker. In our study, crystals of natrin were obtained in two different crystal forms and the structure of one of them was solved at a resolution of 1.68A. Our electrophysiological experiments indicated that natrin can block the ion channel currents of the voltage-gated potassium channel Kv1.3. Docking analyses of the interaction between natrin and Kv1.3 revealed a novel interaction pattern different from the two previously reported K(+) channel inhibition models termed "functional dyad" and "basic ring". These findings offered new insights into the function of natrin and how the specific interactions between CRISPs and different ion channels can be achieved.
    MeSH term(s) Amino Acid Sequence ; Animals ; CHO Cells ; Cricetinae ; Cricetulus ; Crystallography, X-Ray ; Elapid Venoms/chemistry ; Elapid Venoms/metabolism ; Kv1.3 Potassium Channel/metabolism ; Models, Molecular ; Molecular Sequence Data ; Patch-Clamp Techniques ; Protein Structure, Tertiary ; Sequence Homology, Amino Acid
    Chemical Substances Elapid Venoms ; Kv1.3 Potassium Channel ; natrin protein, Naja atra
    Language English
    Publishing date 2006-12-15
    Publishing country United States
    Document type Journal Article ; Research Support, Non-U.S. Gov't
    ZDB-ID 205723-2
    ISSN 0006-291X ; 0006-291X
    ISSN (online) 0006-291X
    ISSN 0006-291X
    DOI 10.1016/j.bbrc.2006.10.067
    Database MEDical Literature Analysis and Retrieval System OnLINE

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