CoChat
Sign Up
Cited by 22Protease and Inhibitor MechanismsNeutrophil, Myeloperoxidase and Oxidative MechanismsBlood Coagulation and Thrombosis Mechanisms

The DOI matches its Crossref record; 58 of the 58 references it cites were found in a registry or an index.

Effects of Noninhibitory α-1-Antitrypsin on Primary Human Monocyte Activation in Vitro

Moraga, Fabian, Lindgren, Stefan, Janciauskiene, Sabina·2001·Archives of Biochemistry and Biophysics
DOI 10.1006/abbi.2000.2211
Open this paper in CoChat — free account

Abstract

A major function of alpha-1-antitrypsin (AAT) is the inhibition of overexpressed serine proteinases during inflammation. However, it is also known that the biological activity of AAT is affected by chemical modifications, including oxidation of the reactive-site methionine, polymerization, and cleavage by unspecific proteases, all of which will result in AAT inactivation and/or degradation. All inactive forms of AAT can be detected in tissues and fluids recovered from inflammatory sites. To test for a possible link between the inflammation-generated, noninhibitory, cleaved form of AAT and cellular processes associated with inflammation, we studied the effects of this form at varying concentrations on human monocytes in culture. We found that cleaved AAT at concentrations ranging between 1 and 10 microM in monocyte cultures over 24 h induces elevation in monocyte chemoattractant protein-1 (MCP-1) and pro-inflammatory cytokines such as TNFalpha and IL-6 and also increases production of interstitial collagenase (MMP-1) and gelatinase B (MMP-9), members of two different classes of matrix metalloproteinase. Moreover, monocytes stimulated with higher doses of cleaved AAT show an increase in cellular oxygen consumption by about 30%, while native AAT under the same experimental conditions inhibits oxygen consumption by about 50%. These results indicate that the cleaved form of AAT may play a role in monocyte recruitment and pro-inflammatory activation during inflammatory processes, and also suggest that changes in structure occurring upon AAT cleavage could alter its functional properties with potential pathological consequences.

Overview

Integrity signals

Registry

Crossref · 10.1006/abbi.2000.2211

Cites

58 of 58 references verified0 citation errors · 0 not checkable

Statistics

Recomputing p-values needs the paper’s full text.

Verification

Claims the paper makes

This paper’s full text isn’t openly available, so its claims and self-check weren’t run. The registry and citation checks still apply.

Claims other papers make about this one

Each is checked against this paper’s own text: does it say what the citing paper says it does?

  • A1AT stimulates monocytes to secrete TNF and IL-6 and hepatocytes to produce HAMP.

    “Interestingly, A1AT, an acute-phase reactant itself, stimulates monocytes to secrete TNF and IL-6 and HC to produce HAMP (Moraga et al., 2001;Nieken et al., 1995;Schaefer et al., 2015).”

    From Iron in infection and immunity (2020) · cites this paper as Moraga et al., 2001

Citations

Cites

Flagged first, then by citations

Research works printed but not linked: 3

  1. Beyeler, 2000, J. Rheumatol., 27, 15
  2. Rapala-Kozik, 1999, J. Biol. Chem., 380, 1211
  3. Janoff, 1985, Am. Rev. Respir. Dis., 132, 417

Cited by

Sorted by citations

Related

Metadata

Authors
Moraga, F., Lindgren, S., & Janciauskiene, S.
Corresponding author
Janciauskiene, Sabina
ORCID
Janciauskiene, Sabina
Venue
Archives of Biochemistry and Biophysics
Publisher
Elsevier BV
Published
2001-02
Volume
386
Issue
2
Pages
221-226
ISSN
0003-9861 (ISSN-L)
DOI
10.1006/abbi.2000.2211
OpenAlex
W2001586938
Cited by
22
References
58
Citations by year
2025: 2 · 2021: 1 · 2020: 1 · 2019: 1 · 2012: 2
FWCI
1.00
Type
journal article
Language
en
Open access
closed
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)
Locations
  • Archives of Biochemistry and Biophysics (publishedVersion)
  • PubMed (publishedVersion)
Funders
Medicinska Fakulteten, Lunds Universitet
Topics
  • Life Sciences › Biochemistry, Genetics and Molecular Biology › Cancer Research › Protease and Inhibitor Mechanisms
  • Life Sciences › Immunology and Microbiology › Immunology › Neutrophil, Myeloperoxidase and Oxidative Mechanisms
  • Health Sciences › Medicine › Hematology › Blood Coagulation and Thrombosis Mechanisms
Keywords
alpha-1-antitrypsin, monocyte activation, MCP-1, TNF-α, interleukin-6, MMP-1, MMP-9, collagenase, oxygen consumption, inflammation, protein oxidation
MeSH terms
alpha 1-Antitrypsin, Cells, Cultured, Dose-Response Relationship, Drug, Humans, Inflammation, Macrophage Activation, Mitochondria, Monocytes, Oxygen Consumption, Tumor Necrosis Factor-alpha, Interleukin-6, Chemokine CCL2, Matrix Metalloproteinase 9, Matrix Metalloproteinase 1

About these checks

Registry, retraction, Cites and statistics results are computed, not judged, with one exception: a printed reference that no index lists is read once by a model before it counts as a citation error. Claims are extracted by a model and kept only when their quote appears verbatim in the text; each cited source is then checked, with a model’s help, for whether it says what the claim relies on. Those verdicts can be wrong — read the claim’s quote and the cited source before relying on one.

Statistics and arithmetic are recomputed, not judged.

Confidence bands are shown only for fields calibrated on our annotated test set. None is calibrated yet, so no band is shown.

What counts as a claim ›How we measure confidence ›How we check this ›

Are you an author, or do you see a problem with this page? Request a review