Linked Life Data

18423794

Source:http://linkedlifedata.com/resource/pubmed/id/18423794

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
8
pubmed:dateCreated
2008-6-9
pubmed:abstractText
Sea anemones are passive predators. They use their specialized stinging cells (nematocysts) to immobilize any prey that blunders into them. A cnida fires, everting a tubule which delivers toxins that may stick to a prey. These toxins include neurotoxins, cytotoxins, cardiotoxins and haemolysins. Heteractis magnificalysins (HMgs) belong to a family of cytolysins from the sea anemone Heteractis magnifica. HMgs are 19.5kDa basic proteins of 177 amino acids with pI values ranging from 8 to 10. From 52 cloned HMg gene sequences, we showed that HMgs are encoded by a multigene family whose members are highly homologous to each other. HMg genes are intronless, and may have arisen by gene duplication, gene conversion or mutation. By modifying the extraction procedure, we purified more natural HMg proteins from H. magnifica, thus demonstrating that H. magnifica are naturally competent to produce a large number of HMg cytolysins. Native and recombinant HMg proteins differed from each other in their amino acid sequences and biological activities. In each H. magnifica, many cytolysin isoforms are produced. H. magnifica appeared to have evolved a survival mechanism whereby a large number of cytolysins of different biological properties are produced for defense and offence.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0041-0101
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
51
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1374-82
pubmed:meshHeading
pubmed-meshheading:18423794-Amino Acid Sequence, pubmed-meshheading:18423794-Animals, pubmed-meshheading:18423794-Cells, Cultured, pubmed-meshheading:18423794-Chromatography, High Pressure Liquid, pubmed-meshheading:18423794-Cloning, Molecular, pubmed-meshheading:18423794-Cnidarian Venoms, pubmed-meshheading:18423794-Cytotoxins, pubmed-meshheading:18423794-DNA, pubmed-meshheading:18423794-Erythrocytes, pubmed-meshheading:18423794-Genome, pubmed-meshheading:18423794-Hemolytic Agents, pubmed-meshheading:18423794-Molecular Sequence Data, pubmed-meshheading:18423794-Multigene Family, pubmed-meshheading:18423794-Pore Forming Cytotoxic Proteins, pubmed-meshheading:18423794-Rats, pubmed-meshheading:18423794-Reverse Transcriptase Polymerase Chain Reaction, pubmed-meshheading:18423794-Sea Anemones, pubmed-meshheading:18423794-Sequence Alignment, pubmed-meshheading:18423794-Solubility
pubmed:year
2008
pubmed:articleTitle
A multigene family of Heteractis magnificalysins (HMgs).
pubmed:affiliation
Department of Biochemistry, Faculty of Medicine, National University of Singapore, 10 Kent Ridge Crescent, Singapore, Singapore. yawen_wang@hms.harvard.edu
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't