Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1987-10-20
pubmed:abstractText
Mast cell proteinases are known to be released in response to helminth infection, and are, in particular, characteristic of the immune rejection of intestinal nematode parasites. In intestinal mucosal tissue the relevant enzyme is rat mast cell proteinase II (RMCP II) and that of other tissues, including the lung, is rat mast cell proteinase I (RMCP I). The function of these enzymes is unknown, and we have examined the possibility that they directly attack the parasites. This was done by examining the cleavage patterns produced by both proteinases on 125I-labelled excretory/secretory (ES) products of two intestinal nematodes (the infective larva of Ascaris suum, and adult Nippostrongylus brasiliensis) and one which has a pulmonary migration route (the third/fourth stage larva of A. suum). It was first established that all the labelled molecules were proteinaceous, by their susceptibility to broad spectrum proteinases, and that none were host components carried over into culture, by their antigenicity to infected hosts. All the nematode ES products were found to be remarkably resistant to RMCP I and II, only one major component of the infective larva of A. suum being cleaved by both enzymes. This was not found to reflect a resistance to serine proteinases in general, since selected ES components were cleaved by chymotrypsin and trypsin. This would, therefore, argue that, if the enzymes play any direct role in the immune expulsion of nematodes, it is unlikely to be successfully directed at their secretions.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jun
pubmed:issn
0166-6851
pubmed:author
pubmed:issnType
Print
pubmed:volume
24
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
137-45
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed:year
1987
pubmed:articleTitle
Resistance of nematode secretory products to cleavage by mast cell proteinases.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't