Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
11
pubmed:dateCreated
2005-10-5
pubmed:abstractText
There are more prophenoloxidase (proPO) genes in mosquitoes than other model insect species studied to date. The high sequence similarity among mosquito proPOs makes it extremely difficult to use histochemical methods to determine the presence of individual proPOs in different stages of mosquito development or their tissue locations. As a consequence, there always are questions when attempting to assign any observed functions to a particular proPO. By following the PO fractions of Aedes aegypti larval proteins during chromatographic separations, we were able to isolate two proPO fractions. Each displayed a single protein band on SDS-PAGE gel. The two fractions showed relative molecular weights of 75 and 60k Da. In-gel trypsin-digestion of the two protein bands and subsequent mass spectrometry of their tryptic peptides confirmed their proPO identities. The 75 kDa protein was a new Aedes aegypti proPO that has not been described in databases, whereas the 60 kDa band contained three previously described Aedes aegypti proPO sequences, with the absence of approximately 125-128 residues at their carboxyl end as compared with their deduced sequences, which suggests that some proPOs might undergo specific proteolytic processing after synthesis. Comparison between the transcriptional profiles of different proPOs and the number of isolated proPO proteins in late-stage larvae indicates that individual proPOs might be transcribed during the earlier stages of larval development, and that resulting proPO proteins persist through all larval stages. Results of this study provide a basis for developing a comprehensive understanding of structure/function relationships of individual proPOs in mosquitoes.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0965-1748
pubmed:author
pubmed:issnType
Print
pubmed:volume
35
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1269-83
pubmed:dateRevised
2007-11-14
pubmed:meshHeading
pubmed:year
2005
pubmed:articleTitle
Purification and primary structural characterization of prophenoloxidases from Aedes aegypti larvae.
pubmed:affiliation
Department of Pathobiology, University of Illinois, 2001 South Lincoln Avenue, Urbana, IL 61802, USA. jli2@uiuc.edu
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, N.I.H., Extramural