Linked Life Data

9839951

Source:http://linkedlifedata.com/resource/pubmed/id/9839951

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1998-12-22
pubmed:databankReference
pubmed:abstractText
Previously, we identified two pro-phenol oxidase-activating factors, named PPAF-I and PPAF-II, directly involved in the activation of the purified pro-phenol oxidase (pro-PO) from the hemolymph of the coleopteran, Holotrichia diomphalia larvae [Lee, S. Y., Kwon, T. H., Hyun, J. H., Choi, J. S., Kawabata, S. I., Iwanga, S, & Lee, B. L. (1998) Eur. J. Biochem. 254, 90-97]. Here, we report molecular cloning of cDNA for PPAF-I. Based on the sequence of the cloned cDNA, the PPAF-I gene appears to encode a member of serine protease zymogen consisting of 365 amino acid residues with a molecular mass of 40193 Da. The 109 amino acid residues preceding the amino-terminus Ile residue of the mature protein seem to constitute a prepro-sequence. The mature protein is a serine protease composed of 256 amino acids with a calculated molecular mass of 28009 Da. The overall structure is highly similar to that of Drosophila easter serine protease (42.9% identity), an essential serine protease zymogen for pattern formation in normal embryonic development. The locations of disulfide linkages in the pro-segment of PPAF-I were similar to those of Tachypleus proclotting enzyme and the mammalian neutrophil-derived defensin. Furthermore, [3H]diisopropylphosphate (iPr2P)-labeled PPAF-I was specifically produced from the crude preparation of PPAF-I zymogen by incubation with lipopolysaccharide or 1,3-beta-glucan, whereas [3H]iPr2P-labeled PPAF-I was not produced under the same conditions in the absence of these microbial polysaccharides. These results indicate that the pro-PO-activation system in H. diomphalia larvae may proceed with the activation of PPAF-I zymogen by microbial polysaccharides.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-2956
pubmed:author
pubmed:issnType
Print
pubmed:day
1
pubmed:volume
257
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
615-21
pubmed:dateRevised
2007-7-23
pubmed:meshHeading
pubmed:year
1998
pubmed:articleTitle
Molecular cloning of cDNA for pro-phenol-oxidase-activating factor I, a serine protease is induced by lipopolysaccharide or 1,3-beta-glucan in coleopteran insect, Holotrichia diomphalia larvae.
pubmed:affiliation
College of Pharmacy, Pusan National University, Kumjeong Ku, Korea.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't