Proteinase/proteinase inhibitor imbalance in sputum sol phases from patients with chronic obstructive pulmonary disease; Suggestions for a key role played by antileukoprotease

P. D. Piccioni, J. A. Kramps, A. Rudolphus, A. Bulgheroni, M. Luisetti

Research output: Contribution to journalArticle

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Abstract

In order to characterize the imbalance between proteinases and proteinase inhibitors in sputum sol phases, we studied 25 patients (mean age, 59±11 yr) with exacerbated chronic obstructive pulmonary disease (COPD). An aliquot of sputum was used for bacteriologic determinations, and the remainder was centrifuged in order to obtain gel and sol phases. On the basis of the bacteriologic data, patients were divided into colonized patients (14) and noncolonized patients (11). All of the major inhibitors were immunologically detectable in sol phases without a significant difference between colonized and noncolonized patients (α1-proteinase inhibitor [α1-PI], 2.56μM ± 0.53μM and 2.39μM ± 0.72μM; α2-macroglobulin [α2-MG], 0.21μM ± 0.07μM and 0.16μM ± 0.05μM; antileukoprotease (ALP), 1.78μM ± 0.57μM and 1.53μM ± 0.6μM, respectively [mean ± SE]). With regard to proteinase activities, both free elastase-like and free chymotrypsin-like activities were detectable in the majority of patients (15/25) (0.59μM ± 0.15μM and 0.74μM ± 0.15μM for elastase-like activity [ELA], and 0.010μM ± 0.003μM and 0.017μM ± 0.007μM for chymotrypsin-like activity [CLA], respectively [mean ± SE]). The inhibitory profile of proteinase activities, performed by means of a panel of inhibitors, allowed us to assign specific activities mainly to neutrophil elastase and cathepsin G (Cat G). Next we looked at the relationships between inhibitors and proteinase activities. We found a significant negative correlation between neutrophil elastase activity and ALP (r = -0.58; p0.50μM) and samples (10) with no detectable ELA (1-PI and α2-MG did not differ significantly between the two groups, whereas ALP values were higher in the group with no detectable ELA (3.12μM ± 0.69μM) than in the other group (0.58μM ± 0.21μM; p

Original languageEnglish
Pages (from-to)1470-1476
Number of pages7
JournalChest
Volume102
Issue number5
Publication statusPublished - 1992

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Secretory Leukocyte Peptidase Inhibitor
Polymethyl Methacrylate
Sputum
Chronic Obstructive Pulmonary Disease
Peptide Hydrolases
Pancreatic Elastase
Macroglobulins
Leukocyte Elastase
Chymotrypsin
Cathepsin G
Gels

ASJC Scopus subject areas

  • Pulmonary and Respiratory Medicine

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Proteinase/proteinase inhibitor imbalance in sputum sol phases from patients with chronic obstructive pulmonary disease; Suggestions for a key role played by antileukoprotease. / Piccioni, P. D.; Kramps, J. A.; Rudolphus, A.; Bulgheroni, A.; Luisetti, M.

In: Chest, Vol. 102, No. 5, 1992, p. 1470-1476.

Research output: Contribution to journalArticle

Piccioni, P. D. ; Kramps, J. A. ; Rudolphus, A. ; Bulgheroni, A. ; Luisetti, M. / Proteinase/proteinase inhibitor imbalance in sputum sol phases from patients with chronic obstructive pulmonary disease; Suggestions for a key role played by antileukoprotease. In: Chest. 1992 ; Vol. 102, No. 5. pp. 1470-1476.
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abstract = "In order to characterize the imbalance between proteinases and proteinase inhibitors in sputum sol phases, we studied 25 patients (mean age, 59±11 yr) with exacerbated chronic obstructive pulmonary disease (COPD). An aliquot of sputum was used for bacteriologic determinations, and the remainder was centrifuged in order to obtain gel and sol phases. On the basis of the bacteriologic data, patients were divided into colonized patients (14) and noncolonized patients (11). All of the major inhibitors were immunologically detectable in sol phases without a significant difference between colonized and noncolonized patients (α1-proteinase inhibitor [α1-PI], 2.56μM ± 0.53μM and 2.39μM ± 0.72μM; α2-macroglobulin [α2-MG], 0.21μM ± 0.07μM and 0.16μM ± 0.05μM; antileukoprotease (ALP), 1.78μM ± 0.57μM and 1.53μM ± 0.6μM, respectively [mean ± SE]). With regard to proteinase activities, both free elastase-like and free chymotrypsin-like activities were detectable in the majority of patients (15/25) (0.59μM ± 0.15μM and 0.74μM ± 0.15μM for elastase-like activity [ELA], and 0.010μM ± 0.003μM and 0.017μM ± 0.007μM for chymotrypsin-like activity [CLA], respectively [mean ± SE]). The inhibitory profile of proteinase activities, performed by means of a panel of inhibitors, allowed us to assign specific activities mainly to neutrophil elastase and cathepsin G (Cat G). Next we looked at the relationships between inhibitors and proteinase activities. We found a significant negative correlation between neutrophil elastase activity and ALP (r = -0.58; p0.50μM) and samples (10) with no detectable ELA (1-PI and α2-MG did not differ significantly between the two groups, whereas ALP values were higher in the group with no detectable ELA (3.12μM ± 0.69μM) than in the other group (0.58μM ± 0.21μM; p",
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