NDLI: Comparison of the primary structures, cytotoxicities, and affinities to phospholipids of five kinds of cytotoxins from the venom of Indian cobra, Naja naja.

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Comparison of the primary structures, cytotoxicities, and affinities to phospholipids of five kinds of cytotoxins from the venom of Indian cobra, Naja naja.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Suzuki-Matsubara, Mieko Athauda, Senarath B. P. Suzuki, Yoshiyuki Matsubara, Kazumi Moriyama, Akihiko
Description	Author Affiliation: Suzuki-Matsubara M ( Graduate School of Natural Sciences, Nagoya City University, Mizuho, Nagoya 467-8501, Japan. Electronic address: m.suzuki@nsc.nagoya-cu.ac.jp.); Athauda SB ( Department of Biochemistry, Faculty of Medicine, Peradeniya University, Peradeniya, Sri Lanka.); Suzuki Y ( Graduate School of Natural Sciences, Nagoya City University, Mizuho, Nagoya 467-8501, Japan.); Matsubara K ( Graduate School of Natural Sciences, Nagoya City University, Mizuho, Nagoya 467-8501, Japan.); Moriyama A ( Graduate School of Natural Sciences, Nagoya City University, Mizuho, Nagoya 467-8501, Japan.)
Abstract	The molecular mechanism underlying the hemolytic and cytolytic processes of cobra cytotoxins (CTXs) is not yet fully elucidated. To examine this, we analyzed the amino acid sequences, hemolytic and cytotoxic activities, and affinities to phospholipids of the five major CTXs purified from the venom of Indian cobra, Naja naja. CTX2, CTX7, and CTX8 belonged to S-type, and CTX9 and CTX10 to P-type. Comparisons of CTX7 with CTX8 and CTX9 with CTX10 revealed similar primary structures and hemolytic and cytolytic activities. CTX2, whose primary structure was rather different from the others, showed several times weaker hemolytic and cytolytic biological activities than the others. The comparison of CTX2 with CTX7 suggested the importance of Lys30 in loop II for the strong hemolytic and cytolytic activities of S-type CTXs. Cloning of 12 CTX cDNAs from the Naja naja venom cDNA library revealed that 18 out of 23 substitutions found in CTX cDNAs were nonsynonymous. This clearly indicated the accelerated evolution of CTX genes. Multiple sequence alignment of 51 kinds of CTX cDNAs and calculations of nonsynonymous and synonymous substitutions indicated that the codons coding the three loops' regions, which may interact with the hydrophobic tails of phospholipids, have undergone an accelerated evolution. In contrast, the codons coding for amino acid residues considered to participate in the recognition and binding of the hydrophilic head groups of phospholipids, eight Cys residues, and those likely stabilizing ß core structure, were all conserved.
File Format	HTM / HTML
ISSN	15320456
Volume Number	179
Journal	Comparative Biochemistry and Physiology Part C: Toxicology & Pharmacology
Language	English
Publisher	Elsevier
Publisher Date	2016-01-01
Publisher Place	United States
Access Restriction	One Nation One Subscription (ONOS)
Subject Keyword	Discipline Toxicology Discipline Pharmacology Cobra Venoms Genetics Metabolism Cytotoxins Phospholipids Amino Acid Sequence Animals Base Sequence Cell Line, Tumor Chemistry Elapidae Humans Mice Molecular Sequence Data Nih 3t3 Cells Comparative Study Journal Article Research Support, Non-u.s. Gov't
Content Type	Text
Resource Type	Article
Subject	Cell Biology Physiology Health, Toxicology and Mutagenesis Medicine Aquatic Science Biochemistry Toxicology Animal Science and Zoology

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