Studies on the effects of experimental inflammation on rat serum and hepatic amino acid pools

1983 ◽  
Vol 74 (4) ◽  
pp. 813-816 ◽  
Author(s):  
B.M.R.N.J Woloski ◽  
H.A Kaplan ◽  
J.C Jamieson
Keyword(s):  
Amino Acid ◽  
Rat Serum ◽  
Experimental Inflammation

scholarly journals The α macroglobulins of rat serum

1976 ◽  
Vol 159 (3) ◽  
pp. 643-650 ◽  
Author(s):  
A H Gordon
Keyword(s):  
Amino Acids ◽  
Amino Acid ◽  
Gel Filtration ◽  
Deae Cellulose ◽  
Complex Mixture ◽  
Male Rats ◽  
Normal Male ◽  
Rat Serum ◽  
Α2 Macroglobulin ◽  
Total Amino Acids

A three-stage method for isolation of α1 macroglobulin and α2 macroglobulin from the serum of normal and injured rats is described. The methods successively used, namely gel filtration, ultracentrifugation and chromatography on DEAE-cellulose, were chosen to minimize loss of tryptic esterase-protecting activity. The two proteins differed slightly with respect to the following properties: mol.wt., α1 macroglobulin 7.46 × 10(5), α2 macroglobulin 7.16 × 10(5); isoelectric focusing, α1, macroglobulin pI 4.4, α2 macroglobulin pI4.5. Amino acid analyses were identical, except with respect to tyrosine: α1 macroglobulin 3.96 ± 0.24, α2 macroglobulin 3.16 ± 0.32 mol/100 mol of total amino acids. When isolated from the serum of uninjured rats, α1 macroglobulin retained the capacity to bind 1.05 mol of trypsin/mol. However, if isolated from serum 2 days after injury only 0.78 mol of trypsin/mol of α1 macroglobulin was bound. α2 macroglobulin isolated from this latter serum bound on average 0.97 mol of trypsin/mol. When reduced with N-acetylcysteine, both molecules formed subunits of size corresponding to that expected for quarter molecules. When α2 macroglobulin was reduced with dithiothreitol, quarter molecules were again produced. α1 macroglobulin, however, when thus treated gave a more complex mixture, containing a component having a mol.wt. of less than 6 × 10(4). Antisera raised against the two proteins permitted estimation of the concentration of each protein in the plasmas or sera of normal and injured rats. Plasma from normal male rats contained 3.76 ± 0.56 mg of α1 macroglobulin/ml (n = 33) and 0.016 ± 0.001 mg of α2 macroglobulin/ml (n=33). After injury by injection of turpentine and cortisone, the concentrations in plasma were at 3 days 5.19 ± 0.81 mg of α1 macroglobulin/ml (n = 12) and at 2 days 1.38 ± 0.35 mg of α2 macroglobulin/ml (n = 12). Antisera to the two proteins did not cross-react with one another. The quarter molecules formed by reduction of both proteins showed increased antigenicity.

scholarly journals Investigation of the idiosyncratic hepatotoxicity of Polygonum multiflorum Thunb. through metabolomics using GC-MS

2021 ◽  
Vol 21 (1) ◽  
Author(s):  
Yan Lin ◽  
Rong Xiao ◽  
Bo-hou Xia ◽  
Zhi-min Zhang ◽  
Chun Li ◽  
...  
Keyword(s):  
Amino Acid ◽  
Glucose Metabolism ◽  
Liver Injury ◽  
Gas Chromatography Mass Spectrometry ◽  
Hexadecanoic Acid ◽  
Hydroxybutyric Acid ◽  
Polygonum Multiflorum ◽  
Rat Serum ◽  
Metabolic Biomarkers ◽  
Endogenous Metabolites

Abstract Background The idiosyncratic hepatotoxicity of Polygonum multiflorum (PM) has attracted considerable interest, but the idiosyncratically hepatotoxic components and endogenous metabolite changes resulting from idiosyncratic hepatotoxicity of PM are not well understood. The aim of this study was to identify the idiosyncratically hepatotoxic components and potential endogenous metabolic biomarkers for PM-induced liver injury. Methods Serum biochemical indicators and hematoxylin and eosin (H&E) staining were evaluated to identify pathological changes. Gas chromatography/mass spectrometry (GC-MS) was performed to identify changes in metabolic biomarkers. Orthogonal projection to latent structures discriminant analysis (OPLS-DA) was applied to determine group clustering trends and differential metabolites. Results The results for the liver index, the liver function index and liver pathology showed that Polygonum multiflorum ethanol extract (PME), 50% ethanol elution fractions and tetrahydroxystilbene glucoside (TSG) from PME can induce idiosyncratic hepatotoxicity. TSG was the main idiosyncratically hepatotoxic component. Forty endogenous metabolites were identified in the rat liver. Six biomarkers, including lower levels of L-valine and higher levels of 3-hydroxybutyric acid, hexadecanoic acid, ribose, phosphoric acid and oxalic acid, were related to PM-induced liver injury. These differential biomarkers led to disruptions in amino acid, fatty acid, oxalate, energy and glucose metabolism. A total of 32 types of endogenous metabolites were identified in rat serum. Ten biomarkers were related to the liver injury induced by TSG, including lower levels of L-valine and L-proline and higher levels of urea, caproic acid, DL-malic acid, D-mannose, 3-hydroxybutyric acid, D-galactose, octadecane and hexadecanoic acid. These differential biomarkers led to disruptions in amino acid, glucose and fat metabolism. The mechanism of idiosyncratic hepatotoxicity in PM involves TSG-induced disruptions in amino acid metabolism, lipid metabolism, energy metabolism and glucose metabolism. Conclusions These findings reflect the material basis and metabolic mechanism of idiosyncratic PM hepatotoxicity.

scholarly journals Amino acid sequence homology between rat and human C-reactive protein

1984 ◽  
Vol 221 (3) ◽  
pp. 903-906 ◽  
Author(s):  
J A Taylor ◽  
C J Bruton ◽  
J K Anderson ◽  
J E Mole ◽  
F C De Beer ◽  
...  
Keyword(s):  
Amino Acid ◽  
Amino Acid Sequence ◽  
Binding Protein ◽  
C Reactive Protein ◽  
Rat Serum ◽  
Reactive Protein ◽  
Phosphoryl Choline ◽  
Serum Amyloid P Component ◽  
C Terminus ◽  
Amyloid P

The rat serum protein that undergoes Ca2+-dependent binding to pneumococcal C-polysaccharide and to phosphocholine residues, and that is evidently a member of the pentraxin family of proteins by virtue of its appearance under the electron microscope, has been variously designated as rat C-reactive protein (CRP) [de Beer, Baltz, Munn, Feinstein, Taylor, Bruton, Clamp & Pepys (1982) Immunology 45, 55-70], ‘phosphoryl choline-binding protein’ [Nagpurkar & Mookerjea (1981) J. Biol. Chem. 256, 7440-7448] and rat serum amyloid P component (SAP) [Pontet, D'Asnieres, Gache, Escaig & Engler (1981) Biochim. Biophys. Acta 671, 202-210]. The partial amino acid sequence (45 residues) towards the C-terminus of this protein was determined, and it showed 71.7% identity with the known sequence of human CRP but only 54.3% identity with human SAP. Since human CRP and SAP are themselves approximately 50% homologous, the level of identity between the rat protein and human SAP is evidence only of membership of the pentraxin family. In contrast, the much greater resemblance to human CRP confirms that the rat C-polysaccharide-binding/phosphocholine-binding protein is in fact rat CRP.

Sign in / Sign up

Export Citation Format

Share Document