Interaction of secretory leukocyte protease inhibitor with proteinase-3.

N. V. Rao, Bruce Marshall, B. H. Gray, J. R. Hoidal

Research output: Contribution to journalArticle

Abstract

Secretory leukocyte protease inhibitor (SLPI) is a 12 kD nonglycosylated serine antiproteinase secreted by cells of mucosal surfaces. In human lung, SLPI is present in the respiratory epithelium. It is the major barrier to tissue destruction mediated by the polymorphonuclear leukocyte (PMN) serine proteinases, elastase and cathepsin G, within the upper respiratory tract. We have recently described a third PMN serine proteinase, proteinase-3, that like elastase causes lung matrix destruction and experimental emphysema. The current studies examine interactions between SLPI and proteinase-3. The results show that: (1) SLPI and its reactive-site variants have no or minimal inhibitory activity against proteinase-3; (2) native SLPI does not complex with proteinase-3; (3) proteinase-3 selectively degrades both native and oxidized SLPI; (4) the cleavage of SLPI by proteinase-3 occurs at the peptide bond COOH-terminal to Ala-16 in the NH2-terminal domain of SLPI.

Original languageEnglish (US)
Pages (from-to)612-616
Number of pages5
JournalAmerican Journal of Respiratory Cell and Molecular Biology
Volume8
Issue number6
StatePublished - Jun 1993
Externally publishedYes

Fingerprint

Secretory Leukocyte Peptidase Inhibitor
Myeloblastin
Pancreatic Elastase
Serine Proteases
Neutrophils
Cathepsin G
Respiratory Mucosa
Lung
Emphysema
Respiratory System
Serine
Catalytic Domain
Tissue
Peptides

ASJC Scopus subject areas

  • Medicine(all)
  • Molecular Biology
  • Pulmonary and Respiratory Medicine
  • Clinical Biochemistry
  • Cell Biology

Cite this

Interaction of secretory leukocyte protease inhibitor with proteinase-3. / Rao, N. V.; Marshall, Bruce; Gray, B. H.; Hoidal, J. R.

In: American Journal of Respiratory Cell and Molecular Biology, Vol. 8, No. 6, 06.1993, p. 612-616.

Research output: Contribution to journalArticle

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AB - Secretory leukocyte protease inhibitor (SLPI) is a 12 kD nonglycosylated serine antiproteinase secreted by cells of mucosal surfaces. In human lung, SLPI is present in the respiratory epithelium. It is the major barrier to tissue destruction mediated by the polymorphonuclear leukocyte (PMN) serine proteinases, elastase and cathepsin G, within the upper respiratory tract. We have recently described a third PMN serine proteinase, proteinase-3, that like elastase causes lung matrix destruction and experimental emphysema. The current studies examine interactions between SLPI and proteinase-3. The results show that: (1) SLPI and its reactive-site variants have no or minimal inhibitory activity against proteinase-3; (2) native SLPI does not complex with proteinase-3; (3) proteinase-3 selectively degrades both native and oxidized SLPI; (4) the cleavage of SLPI by proteinase-3 occurs at the peptide bond COOH-terminal to Ala-16 in the NH2-terminal domain of SLPI.

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