Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
3
pubmed:dateCreated
1996-1-18
pubmed:databankReference
pubmed:abstractText
Trypsin genes in Anopheles gambiae are arranged as a tightly clustered gene family consisting of seven related coding sequences, devoid of introns. The two blood meal-inducible members of this family, Antryp1 and Antryp2, were shown to play a crucial role in the breakdown of the blood meal constituents. The role of Antryp3,4,5,6, and Antryp7 in the process of blood meal digestion remains to be elucidated. We have examined the localization and the expression patterns of these trypsins as well as the functional interactions in blood meal digestion between trypsins and other gut-specific proteases. Northern blot and RT-PCR analysis indicated that the genes Antryp3,4,5,6, and Antryp7 are all constitutively expressed in unfed female mosquitoes. Soon after blood feeding the mRNA of these trypsin genes became undetectable and appeared again at the end of the gonotrophic cycle. The blood meal-inducible trypsin Antryp1 was also constitutively expressed at low level in the gut of adult female mosquitoes. This trypsin was the only member of this gene family to be expressed in the gut of male and female pupae. By using antisera that specifically recognized recombinant Antryp4 we were able to show that the corresponding protein in Anopheles is synthesized and stored in the gut epithelium of unfed females as zymogen. Secretion and activation of this trypsin was shown to occur in the midgut lumen immediately after fluid ingestion and independently of the protein content of the meal. Recombinant trypsins expressed in Escherichia coli, with the exception of Antryp5 and Antryp6, were able to activate in vitro recombinant A. gambiae chymotrypsinogen, thus suggesting that blood meal ingestion is able to trigger a cascade of events leading to the activation of several proteases.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
0014-4894
pubmed:author
pubmed:issnType
Print
pubmed:volume
81
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
371-85
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:7498434-Amino Acid Sequence, pubmed-meshheading:7498434-Animals, pubmed-meshheading:7498434-Anopheles, pubmed-meshheading:7498434-Base Sequence, pubmed-meshheading:7498434-Blood, pubmed-meshheading:7498434-Blotting, Northern, pubmed-meshheading:7498434-Blotting, Southern, pubmed-meshheading:7498434-Chymotrypsinogen, pubmed-meshheading:7498434-Conserved Sequence, pubmed-meshheading:7498434-DNA, pubmed-meshheading:7498434-DNA Primers, pubmed-meshheading:7498434-Digestion, pubmed-meshheading:7498434-Enzyme Induction, pubmed-meshheading:7498434-Female, pubmed-meshheading:7498434-Genes, Insect, pubmed-meshheading:7498434-Insect Vectors, pubmed-meshheading:7498434-Male, pubmed-meshheading:7498434-Molecular Sequence Data, pubmed-meshheading:7498434-Multigene Family, pubmed-meshheading:7498434-RNA, Messenger, pubmed-meshheading:7498434-Recombinant Proteins, pubmed-meshheading:7498434-Sequence Alignment, pubmed-meshheading:7498434-Transcription, Genetic, pubmed-meshheading:7498434-Trypsin
pubmed:year
1995
pubmed:articleTitle
Constitutive and blood meal-induced trypsin genes in Anopheles gambiae.
pubmed:affiliation
Università La Sapienza, Istituto di Parassitologia, Rome, Italy.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't