PubMed Health⌕ Search
Home/Archive/PubMed

PubMed · 7512342

The acute phase response.

H Baumann·J Gauldie
View original source ↗Export metadata ↓

Abstract

Adult mammals respond to tissue damage by implementing the acute phase response, which comprises a series of specific physiological reactions. This review outlines the principal cellular and molecular mechanisms that control initiation of the tissue response at the site of injury, the recruitment of the systemic defense mechanisms, the acute phase response of the liver and the resolution of the acute phase response.

Explore related subjects

Acute-Phase ProteinsAcute-Phase ReactionAnimalsHumansLiverJournal ArticleReview

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

H Baumann, J Gauldie. 1994. The acute phase response.. https://doi.org/10.1016/0167-5699(94)90137-6

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

PubMed1996

Plasma lipopolysaccharide-binding protein is found associated with a particle containing apolipoprotein A-I, phospholipid, and factor H-related proteins.

Neutrophils exhibit a dramatic enhancement of integrin-mediated cell adhesion in response to lipopolysaccharide (LPS). This response requires CD14 on the neutrophil and plasma proteins in solution. We have purified the factor from plasma that facilitates the adhesive response of neutrophil to LPS by using a combination of affinity and ion-exchange chromatography. Previous work has shown that the activity is associated with apolipoprotein A-I (apoA-I), and here we show that this activity is associated with an apoA-I-bearing complex of protein and phospholipid. Native polyacrylamide gel electrophoresis (PAGE) analysis showed a ladder of bands in the Mr 200,000 region, and electron microscopy revealed round, indented particles of 11.4 +/- 0.12 nm in diameter. Characterization of these particles revealed a density of 1.219-1.264 g/ml and approximately 10 molecules of lipid phosphate per Mr 200,000 complex. SDS-PAGE showed that each of the bands seen in native PAGE was composed of several polypeptides. These were identified as apoA-I, LPS binding protein (LBP), and factor H-related proteins (FHRPs). Physical association of apoA-I, LBP, and FHRP in these particles was further confirmed using double immunodiffusion, and association of LBP and FHRP in plasma was confirmed by coimmunoprecipitation. FHRPs are the numerically dominant protein components in these particles, and all plasma FHRP-1 appears to be associated with these particles. We suggest that FHRPs may be the defining constituent of this novel "lipoprotein" particle.

Acute-Phase Proteins↗
PubMed1996

Purification and molecular cloning of an inducible gram-negative bacteria-binding protein from the silkworm, Bombyx mori.

A 50-kDa hemolymph protein, having strong affinity to the cell wall of Gram(-) bacteria, was purified from the hemolymph of the silkworm, Bombyx mori. The cDNA encoding this Gram(-) bacteria-binding protein (GNBP) was isolated from an immunized silkworm fat body cDNA library and sequenced. Comparison of the deduced amino acid sequence with known sequences revealed that GNBP contained a region displaying significant homology to the putative catalytic region of a group of bacterial beta-1,3 glucanases and beta-1,3-1,4 glucanases. Silkworm GNBP was also shown to have amino acid sequence similarity to the vertebrate lipopolysaccharide receptor CD14 and was recognized specifically by a polygonal anti-CD14 antibody. Northern blot analysis showed that GNBP was constitutively expressed in fat body, as well as in cuticular epithelial cells of naive silkworms. Intense transcription was, however, rapidly induced following a cuticular or hemoceolien bacterial challenge. An mRNA that hybridized with GNBP cDNA was also found in the l(2)mbn immunocompetent Drosophila cell line. These observations suggest that GNBP is an inducible acute phase protein implicated in the immune response of the silkworm and perhaps other insects.

Acute-Phase Proteins↗
PubMed1996

Unstimulated peripheral blood mononuclear cells from patients with the hyper-IgD syndrome produce cytokines capable of potent induction of C-reactive protein and serum amyloid A in Hep3B cells.

The hyper-IgD and periodic fever syndrome (HIDS) and familial Mediterranean fever (FMF) are both characterized by attacks of periodic fever accompanied by acute phase responses that are substantially higher in HIDS than in FMF. To determine whether this difference could be due to differences in production of acute phase protein-inducing mediators, we studied PBMC from HIDS and FMF patients in the inactive phase of disease. Unstimulated PBMC from patients with inactive HIDS released significantly more IL-1 beta, IL-6, and TNF-alpha than did PBMC from patients with FMF, but unstimulated PBMC from the latter group released significantly more IL-1 beta and IL-6 compared with controls. Conditioned medium (CM) derived from PBMC of patients with inactive HIDS induced significantly greater CRP production and significantly higher mRNAs for CRP and SAA in Hep3B cells than did CM derived from the PBMC of patients with inactive FMF. Stimulation of PBMC with LPS led to further increases in cytokine production and in acute phase protein-inducing ability in both patient groups and in controls. These findings suggest that the greater acute phase response seen in HIDS compared with FMF reflects greater production of acute phase protein-inducing cytokines in the former patients and indicates that PBMC from inactive HIDS patients are already activated in vivo. Finally, the finding of both quantitative and qualitative differences in cytokine production by unstimulated PBMC from HIDS and FMF patients supports the likelihood of different pathogeneses of these diseases.

Acute-Phase Proteins↗