Identification and characterisation of the major antiproteases in equine serum and an investigation of their role in the onset of chronic obstructive pulmonary disease (COPD).
Three major antiprotease components in equine serum were identified and characterised. These were the acidic prealbumin Pr, the homologue of human alpha-1 antitrypsin and 2 protease binding proteins, the acidic prealbumin Xc and alpha-2 macroglobulin, both capable of inhibiting the proteolytic activity of trypsin, but with only limited inhibitory effect on its esterolytic activity. The possible role of these serum antiproteases in the onset of chronic obstructive pulmonary disease (COPD), analogous to the hereditary dysproteinaemia of alpha-1 antitrypsin in man, was investigated. There was no evidence of a genetically determined variation in the protease binding proteins but an increased frequency of the electrophoretically slower Pr antitrypsin alleles was present in horses affected with COPD. However, because of both the mixed breeding of the animals investigated and the lack of correlation with low serum trypsin inhibitory capacity, measured by inhibition of DL-BAPA hydrolysis, the significance of this observation could not be critically assessed.
D000483:Alleles; D000818:Animals; D004587:Electrophoresis, Agar Gel; D005787:Gene Frequency; D006734:Horse Diseases / Q000097:blood* / Q000235:genetics; D006736:Horses; D007525:Isoelectric Focusing; D008173:Lung Diseases, Obstructive / Q000097:blood / Q000235:genetics / Q000662:veterinary*; D011228:Prealbumin / Q000302:isolation & purification; D011480:Protease Inhibitors / Q000097:blood*; D000515:alpha 1-Antitrypsin / Q000302:isolation & purification; D000511:alpha-Macroglobulins / Q000302:isolation & purification
D011228:Prealbumin; D011480:Protease Inhibitors; D000515:alpha 1-Antitrypsin; D000511:alpha-Macroglobulins