Mechanisms of proteinase-inhibitor proteinase system response was estimated following of cobalt chloride injection. The increase proteinase activity, which led to significant decrease of alpha-2-macroglobulin (alpha-2-MG) level was established that indicated to the removal of the proteinase in complex with alpha-2-MG from the organism. Increase of alpha-1-proteinase inhibitor (alpha-1-PI) trypsin-inhibitory activity in the kidneys testify about removal of oxidative alpha-1-PI.
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Serum α-proteinase inhibitor concentrations in dogs with exocrine pancreatic disease, chronic hepatitis or proteinuric chronic kidney disease.
Vet J
June 2018
Gastrointestinal Laboratory, Department of Small Animal Clinical Sciences, College of Veterinary Medicine and Biomedical Sciences, Texas Agricultural and Machinery (Texas A&M) University, College Station, TX 77843-4474, USA.
Serum canine α-proteinase inhibitor (cα-PI) concentrations were evaluated in dogs with pancreatitis (n=24), exocrine pancreatic insufficiency (EPI; n=29), chronic hepatitis (CH; n=11) or proteinuric chronic kidney disease (CKD-P; n=61) to determine whether systemic proteinase/proteinase-inhibitor balance is altered in these conditions. Dogs with CKD-P had significantly lower cα-PI concentrations than dogs with pancreatitis, EPI or CH; 16% of dogs with CKD-P had serum cα-PI concentrations below the reference interval. Serum and urine cα-PI concentrations were inversely correlated in dogs with CKD-P, but not in dogs with CH.
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Wound Repair Regen
October 2014
Research and Development, Systagenix Wound Management, Gargrave, United Kingdom.
Within chronic wounds, the relationship between the clinical diagnosis of infection and bacterial/immuno-inflammatory responses is imprecise. This study prospectively examined the interrelationship between clinical, microbiological, and proinflammatory biomarker levels between chronic venous leg ulcers (CVLUs) and diabetic foot ulcers (DFUs). Wound swabs and fluids were collected from CVLUs (n = 18) and DFUs (n = 15) and diagnosed clinically as noninfected or infected; and qualitative/quantitative microbiology was performed.
View Article and Find Full Text PDFSerum alpha1-proteinase inhibitor concentrations in healthy dogs--method validation and determination of reference interval and intra-individual variation.
Vet Clin Pathol
June 2013
Department of Small Animal Clinical Sciences, College of Veterinary Medicine and Biomedical Sciences, Gastrointestinal Laboratory, Texas A&M University, College Station, TX 77843-4474, USA.
Background: A chronic loss of canine α1 -proteinase inhibitor (cα1 -PI) into the gastrointestinal (GI) tract could change the systemic proteinase-proteinase inhibitor balance. Serum cα1 -PI concentrations have not been studied in dogs with well-defined GI diseases.
Objectives: To further evaluate serum cα1 -PI concentrations in dogs with GI diseases, the objectives of this study were to (1) analytically validate a previously developed fecal cα1 -PI immunoassay to determine serum concentrations, (2) determine a population-based reference interval (RI) and assess the clinical utility, (3) determine stability of serum cα1 -PI, (4) determine the intra-individual variation in healthy dogs, and (5) determine the clinically relevant magnitude of change of serum cα1 -PI.
The proteinase/proteinase-activated receptor-2/transient receptor potential vanilloid-1 cascade impacts pancreatic pain in mice.
Life Sci
November 2010
Division of Pharmacology and Pathophysiology, Kinki University School of Pharmacy, Higashi-Osaka, Japan.
Aims: Proteinase-activated receptor-2 (PAR2) and transient receptor potential vanilloid-1 (TRPV1) are co-localized in the primary afferents, and the trans-activation of TRPV1 by PAR2 activation is involved in processing of somatic pain. Given evidence for contribution of PAR2 to pancreatic pain, the present study aimed at clarifying the involvement of TRPV1 in processing of pancreatic pain by the proteinase/PAR2 pathway in mice.
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Basic and translational research on proteinase-activated receptors: implication of proteinase/proteinase-activated receptor in gastrointestinal inflammation.
J Pharmacol Sci
December 2008
Department of Gastroenterology, Japanese Red Cross Kyoto Daiichi Hospital, Japan.
Recently, the role of serine proteinases in the pathogenesis of inflammation and autoimmune diseases via interaction with the proteinase-activated receptor (PAR) has attracted attention. Activation of PAR has a pro-inflammatory effect through the overproduction of inflammatory cytokines such as interleukin (IL)-6 and IL-8. PAR(2) activation in human esophageal epithelial cells by trypsin induces NFkappaB- and AP-1-dependent IL-8 production in association with activation of p38 MAPK and ERK1/2, suggesting that esophageal inflammation may be induced by PAR(2) activation via reflux of trypsin.
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