FRINK Linked Data Fragments server

Matches in SemOpenAlex for { <https://semopenalex.org/work/W2896584077> ?p ?o ?g. }

• W2896584077 endingPage "352" @default.
• W2896584077 startingPage "341" @default.
• W2896584077 abstract "It is now well established that neutrophil elastase and cathepsin-G are responsible for elastin degradation in the lung and that the major function of α1-proteinase inhibitor (α1Pi) is to control elastolytic activity. α1Pi can inactivate many serine proteinases, but kinetic studies show it to be most efficient against elastase. Complexes of α1Pi and serine proteinases are extremely stable and can only be dissociated under alkaline conditions. Dissociation results in active enzyme and inactive inhibitor, the latter being of lower molecular weight than that of the native molecule. The reactive site of α1Pi contains a methionyl-seryl peptide bond. Treatment with SucNCl chemically oxidizes two of the methionyl residues in the inhibitor to the sulfoxide form, one of which is the reactive site methionine. No other residues are modified. Two methionyl residues of α1Pi (and no other amino acids) are also oxidized by the action of the neutrophil enzyme, myeloperoxidase. Myeloperoxidase requires hydrogen peroxide and a halide ion for its action. The optimum pH for oxidation of α1Pi is at pH 6.2 with half-maximal activity at pH 5.9 and 6.5. CaCl2, Ca(NO3)2 and Ca(Ac)2 inhibit the inactivation of α1Pi and calcium lactate enhances it. On NaDodSO1-acrylamide gel electrophoresis, myeloperoxidase-treated α1Pi has the same molecular weight as native α1Pi, but cannot form a complex with porcine elastase. In fact, the molecular weight of oxidized α1Pi is reduced in the presence of elastase, indicating modification of the inhibitor. Sequence analysis demonstrated that proteolytic cleavage occurred at the P8 methionyl bond and that both the P8 and P1 methionyl residues were oxidized. Filtered cigarette smoke, bubbled through plasma, decreased elastase inhibitory activity by 3%. Even unfiltered smoke inhibited only 19%. However, the lungs have a vast surface area, perhaps rendering inhibitors present on the lining more susceptible to oxidants. In order to show that oxidized α1Pi exists in vivo, an inflamed tissue was examined for its presence. Lung lavage fluid contains α1Pi but in quantities too small for isolation and characterization. Rheumatoid synovial fluid contains only inactive α1Pi, in which amino acid analysis shows two oxidized methionyl residues. The molecular weight of this protein is identical to native α1Pi and porcine elastase reduces it to a lower molecular weight form. Many kinds of oxidants are produced by neutrophils and macrophages. Since α1Pi contains two oxidizable methionyl residues, one essential for activity, an imbalance between proteinases and proteinase inhibitors could readily occur. Eventually, such an imbalance could give rise to emphysema, even in individuals with normal levels of α1Pi." @default.
• W2896584077 created "2018-10-26" @default.
• W2896584077 creator A5003503145 @default.
• W2896584077 creator A5034424714 @default.
• W2896584077 creator A5071593971 @default.
• W2896584077 creator A5077880236 @default.
• W2896584077 date "1981-01-01" @default.
• W2896584077 modified "2023-09-27" @default.
• W2896584077 title "OXIDATION OF ALPHA1-PROTEINASE INHIBITOR AS A MAJOR, CONTRIBUTING FACTOR IN THE DEVELOPMENT OF PULMONARY EMPHYSEMA" @default.
• W2896584077 cites W1553874478 @default.
• W2896584077 cites W1563535758 @default.
• W2896584077 cites W1583152769 @default.
• W2896584077 cites W1976784572 @default.
• W2896584077 cites W1985102595 @default.
• W2896584077 cites W1992363260 @default.
• W2896584077 cites W1994517550 @default.
• W2896584077 cites W2019946790 @default.
• W2896584077 cites W2089695818 @default.
• W2896584077 doi "https://doi.org/10.1016/b978-0-08-027379-2.50035-1" @default.
• W2896584077 hasPubMedId "https://pubmed.ncbi.nlm.nih.gov/6971678" @default.
• W2896584077 hasPublicationYear "1981" @default.
• W2896584077 type Work @default.
• W2896584077 sameAs 2896584077 @default.
• W2896584077 citedByCount "4" @default.
• W2896584077 countsByYear W28965840772020 @default.
• W2896584077 crossrefType "book-chapter" @default.
• W2896584077 hasAuthorship W2896584077A5003503145 @default.
• W2896584077 hasAuthorship W2896584077A5034424714 @default.
• W2896584077 hasAuthorship W2896584077A5071593971 @default.
• W2896584077 hasAuthorship W2896584077A5077880236 @default.
• W2896584077 hasConcept C181199279 @default.
• W2896584077 hasConcept C185592680 @default.
• W2896584077 hasConcept C203014093 @default.
• W2896584077 hasConcept C203565725 @default.
• W2896584077 hasConcept C2776414213 @default.
• W2896584077 hasConcept C2776914184 @default.
• W2896584077 hasConcept C2777132095 @default.
• W2896584077 hasConcept C2779201268 @default.
• W2896584077 hasConcept C2780908991 @default.
• W2896584077 hasConcept C2781044401 @default.
• W2896584077 hasConcept C41183919 @default.
• W2896584077 hasConcept C55493867 @default.
• W2896584077 hasConcept C86803240 @default.
• W2896584077 hasConceptScore W2896584077C181199279 @default.
• W2896584077 hasConceptScore W2896584077C185592680 @default.
• W2896584077 hasConceptScore W2896584077C203014093 @default.
• W2896584077 hasConceptScore W2896584077C203565725 @default.
• W2896584077 hasConceptScore W2896584077C2776414213 @default.
• W2896584077 hasConceptScore W2896584077C2776914184 @default.
• W2896584077 hasConceptScore W2896584077C2777132095 @default.
• W2896584077 hasConceptScore W2896584077C2779201268 @default.
• W2896584077 hasConceptScore W2896584077C2780908991 @default.
• W2896584077 hasConceptScore W2896584077C2781044401 @default.
• W2896584077 hasConceptScore W2896584077C41183919 @default.
• W2896584077 hasConceptScore W2896584077C55493867 @default.
• W2896584077 hasConceptScore W2896584077C86803240 @default.
• W2896584077 hasLocation W28965840771 @default.
• W2896584077 hasLocation W28965840772 @default.
• W2896584077 hasOpenAccess W2896584077 @default.
• W2896584077 hasPrimaryLocation W28965840771 @default.
• W2896584077 hasRelatedWork W1913482601 @default.
• W2896584077 hasRelatedWork W1969765414 @default.
• W2896584077 hasRelatedWork W2046311107 @default.
• W2896584077 hasRelatedWork W2063662866 @default.
• W2896584077 hasRelatedWork W2086152655 @default.
• W2896584077 hasRelatedWork W2087781112 @default.
• W2896584077 hasRelatedWork W2139513793 @default.
• W2896584077 hasRelatedWork W2343333218 @default.
• W2896584077 hasRelatedWork W2416306772 @default.
• W2896584077 hasRelatedWork W2692078659 @default.
• W2896584077 isParatext "false" @default.
• W2896584077 isRetracted "false" @default.
• W2896584077 magId "2896584077" @default.
• W2896584077 workType "book-chapter" @default.