Serine proteinase inhibitors from insect hemolymph.
Insect hemolymph, like vertebrate serum, contains several different types of polypeptides that are able to inhibit the catalytic function of proteolytic enzymes, however studies on proteins possessing this capability have been limited to a relatively few species. A comparative examination of the inhibition of trypsin, chymotrypsin, neutrophil elastase and cathepsin G and pancreatic elastase by the hemolymph of 14 insect species belonging to six orders showed great diversity in terms of both total proteinase inhibitory capacity and specificity. Most of the inhibitors examined fall into two groups: low molecular mass proteins (below 10 kDa) related to Kunitz type inhibitors, and proteins of about 45 kDa which belong to the serpin superfamily of serine proteinase inhibitors. This minireview describes the properties, characteristics and possible biological significance of selected inhibitors.
Polanowski
A
A
Institute of Biochemistry, University of Wrocław, Poland.
Wilusz
T
T
D000818:Animals; D006458:Hemolymph / Q000737:chemistry*; D007313:Insecta / Q000737:chemistry*; D015842:Serine Proteinase Inhibitors / Q000097:blood*; D013379:Substrate Specificity
D015842:Serine Proteinase Inhibitors