Serum amyloid A isoforms in serum and synovial fluid in horses with lipopolysaccharide-induced arthritis

Jacobsen, Stine; Niewold, Theodoor; Thomsen, Maj Halling; Nanni, Simone; Olsen, E. G. J.; Lindegaard, Claus; Andersen, Pia Haubro

doi:10.1016/j.vetimm.2005.10.012

Cited by 94 publications

(134 citation statements)

References 16 publications

Supporting

Mentioning

125

Contrasting

Order By: Relevance

“…In our study, we found that the LPS challenge of cartilage and synovial membrane explants induced expression of one main protein identified as serum amyloid A3.2 protein. Our finding is in agreement with in vivo observations, as LPS injection into the radiocarpal joint of horse induced a local inflammatory response accompanied with expression of serum amyloid isoforms 48 . The functions of serum amyloid proteins in joint diseases are not elucitaded but it is supposed that they contribute to inflammation and cartilage destruction by chemoattracting properties for leukocytes and by activating angiogenesis 49 .…”

Section: Discussionsupporting

confidence: 93%

In vitroevaluation of S-(+)-ibuprofen as drug candidate for intra-articular drug delivery system

Bédouet¹,

Pascale²,

Bonneau³

et al. 2013

Drug Development and Industrial Pharmacy

View full text Add to dashboard Cite

Intra-articular drug delivery systems (DDSs) are envisaged as interesting alternative to locally release non-steroidal anti-inflammatory drugs (NSAIDs) such as ibuprofen to reduce pain in patients with osteoarthritis. The present study examines the efficacy of S-(+)-ibuprofen on cartilage degradation as drug candidate for DDS loading. Humeral cartilage and joint capsule explants were collected from healthy sheep shoulder joints and they were cultured in mono- or in co-culture for 13 days with LPS in combination with S-(+)-ibuprofen at 50 µM and 1 mM. S-(+)-ibuprofen (50 µM) blocked prostaglandins production in LPS-activated explants but did not reduce cartilage degradation. By contrast, 1 mM S-(+)-ibuprofen treatment of cartilage explants reduced nitric oxide synthesis by 51% (p = 0.0072), proteoglycans degradation by 35% (p = 0.0114) and expression of serum amyloid protein - the main protein induced upon LPS challenge - by 44% (p < 0.0001). On contrary, in presence of synovial membrane, the protective effects of S-(+)-ibuprofen on cartilage damages were significantly diminished. At 1mM, S-(+)-ibuprofen reduced the cell lysis during culture of cartilage and joint capsule either in mono- or in co-culture. This study performed on sheep explants shows that 1 mM S-(+)-ibuprofen inhibited cartilage degradation via a mechanism independent of cyclooxygenase inhibition. Reduction of prostaglandins synthesis at 50 µM in all treatment groups and reduction of cartilage degradation observed at 1 mM suggest that S-(+)-ibuprofen could be considered as a promising drug candidate for the loading of intra-articular DDS.

show abstract

Section: Discussionsupporting

confidence: 93%

In vitroevaluation of S-(+)-ibuprofen as drug candidate for intra-articular drug delivery system

Bédouet¹,

Pascale²,

Bonneau³

et al. 2013

Drug Development and Industrial Pharmacy

View full text Add to dashboard Cite

show abstract

“…However, it has been demonstrated that APPs can be produced by many other tissues and cells (Jacobsen et al 2006, Di Filippo et al 2014a, 2014b. Under normal physiological conditions, the production of amyloid A (McDonald et al 2001) and α1 acid glycoprotein (Ceciliani et al 2005) by the epithelial cells of the mammary gland of healthy bovines has been reported.…”

Section: Discussionmentioning

confidence: 99%

“…The mechanism probably plays the role of counteracting the proinflammatory effects inside the injured tissue (Ceciliani et al 2012). Measurement of the local levels of APPs, by providing information on the inflammatory/infectious status of an organ of interest, increases the diagnostic precision (Jacobsen et al 2006). In one study, an increase was noted in the concentration of transferrin (Tf) in the CSF of people suffering from restless leg syndrome (RLS).…”

Section: Discussionmentioning

confidence: 99%

“…Acute phase proteins are primarily produced in the liver (Murata et al 2004, Petersen et al 2004, Ceron et al 2005. However, extrahepatic production of APPs is also possible in most mammalian species (Jacobsen et al 2006, Di Filippo et al 2011, 2014a. Some APPs opsonize microorganisms and activate complements, while others scavenge cellular remnants and free radicals or neutralize proteolytic enzymes (Gruys et al 2005).…”

Section: Introdutionmentioning

confidence: 99%

See 1 more Smart Citation

Acute phase proteins in serum and cerebrospinal fluid in healthy cattle: possible use for assessment of neurological diseases

et al. 2018

View full text Add to dashboard Cite

Use of acute-phase proteins (APPs) for assessment of health and disease in animals has increased greatly within the last decade. The objective was to determine the normal concentration of APPs in the serum and cerebrospinal fluid (CSF) of healthy cattle by polyacrylamide gel electrophoresis. Fifty crossbred animals (350±70kg of BW and 18±1.2 months of age), 25 heifers and 25 steers were used. CSF samples were collected from atlanto-occipital (AO) site and blood samples were obtained from the jugular vein. CSF and serum protein electrophoresis were performed by means of sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Thirty-seven proteins with molecular weights ranging from 7 and 37kDa were identified in CSF of all animals. These eight were nominally identified with immunoglobulin A and G, celuloplasmin, transferrin, albumin, α1-antitripsin, acidic glycoprotein, and haptoglobin. All protein fractions in CSF did not differ between heifers and steers. In sera, 34 proteins with molecular weights between 7 and 244kDa were identified in heifers and steers. Similar proteins were nominally identified in the sera, but only the CSF presented α1-antitripsin. The serum values of acidic glycoprotein and immunoglobulin G were significantly higher in steers compared with heifers. In conclusion, measurement of CSF acute phase protein concentrations can be useful in diagnosing and monitoring the progression of bovine neurological diseases, perhaps even to guide therapeutic procedures. The CSF electrophoretic profile of healthy cattle does not change depending on gender.

show abstract

“…In all cases, disease is caused by the conformational change of the acute phase reactant, Serum Amyloid-A (SAA) (Gruys, 2004;Kim et al, 2005;Kisilevsky, 1990), a protein encoded by multiple genes highly conserved through the evolution of eutherian mammals (Jacobsen et al, 2006;Uhlar and Whitehead, 1999). SAA is a apoliprotein of high-density lipoproteins mostly synthesized in liver in response to proinflammatory cytokines such as endogenous pyrogens IL-1 and IL-6 (Gruys, 2004).…”

Section: Aa-amyloidosismentioning

confidence: 99%

Prion and prion-like diseases in animals

Aguilar‐Calvo¹,

García²,

Espinosa³

et al. 2015

Virus Research

View full text Add to dashboard Cite

Serum amyloid A isoforms in serum and synovial fluid in horses with lipopolysaccharide-induced arthritis

Cited by 94 publications

References 16 publications

In vitroevaluation of S-(+)-ibuprofen as drug candidate for intra-articular drug delivery system

In vitroevaluation of S-(+)-ibuprofen as drug candidate for intra-articular drug delivery system

Acute phase proteins in serum and cerebrospinal fluid in healthy cattle: possible use for assessment of neurological diseases

Prion and prion-like diseases in animals

Contact Info

Product

Resources

About