Studies on Acute Phase Proteins of Rat Serum. IV. Pathway of Secretion of Albumin and α1-Acid Glycoprotein from Liver

1973 ◽  
Vol 51 (9) ◽  
pp. 1281-1291 ◽  
Author(s):  
J. C. Jamieson ◽  
F. E. Ashton
Keyword(s):  
Endoplasmic Reticulum ◽  
Acute Phase ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Acute Phase Proteins ◽  
Smooth Endoplasmic Reticulum ◽  
Rat Serum ◽  
Experimental Animals ◽  
Acid Glycoprotein ◽  
Ionic Detergent

Normal rats and those suffering from inflammation for 12 h were given pulse injections of L-leucine-3H and D-glucosamine-14C and were killed at 3–60 min thereafter. Rough and smooth microsome fractions and a Golgi-enriched fraction were prepared from liver and the fractions were extracted with the non-ionic detergent Lubrol-W. Albumin and acute phase α1-acid glycoprotein were isolated from the extracts by application of a quantitative precipitin technique employing antisera to albumin and α1-acid glycoprotein, and specific radioactivities were determined. The results indicated that the pathway of secretion of albumin and α1-acid glycoprotein was rough endoplasmic reticulum → smooth endoplasmic reticulum → Golgi complex → blood. Although there was little difference in the pathway or rate of secretion of the proteins under study in normal and experimental animals, there was an increase in specific radioactivities of labelled leucine and glucosamine associated with α1-acid glycoprotein when isolated from subcellular fractions from livers from experimental animals.

Studies on Acute Phase Proteins of Rat Serum. II. Determination of the Contents of α1-Acid Glycoprotein, α2-Macroglobulin, and Albumin in Serum from Rats Suffering from Induced Inflammation

1972 ◽  
Vol 50 (8) ◽  
pp. 871-880 ◽  
Author(s):  
J. C. Jamieson ◽  
F. E. Ashton ◽  
A. D. Friesen ◽  
B. Chou
Keyword(s):  
Acute Phase ◽  
Acute Phase Proteins ◽  
Rat Serum ◽  
Experimental Animals ◽  
Acid Glycoprotein ◽  
Inflammatory Agent ◽  
Glycoprotein Biosynthesis ◽  
Α2 Macroglobulin

A quantitative precipitin technique has been employed to determine the contents of α1-acid glycoprotein, α2-macroglobulin, and albumin in serum from control rats and rats suffering from induced inflammation for 5–96 h. There was an increase in the content of α1-acid glycoprotein and α2-macroglobulin in serum from experimental animals reaching a maximum at 48–72 h after administration of inflammatory agent indicating that both proteins are acute phase globulins. There was only a slight change in the content of albumin in serum from experimental animals when compared with controls. Studies involving incorporation of labelled precursors of glycoprotein biosynthesis into α1-acid glycoprotein and α2-macroglobulin indicated that the most likely explanation for the increase in α1-acid glycoprotein and α2-macroglobulin in serum from experimental animals was an increase in the rates of synthesis of the two proteins in question.

scholarly journals Glycosyltransferase activities in Golgi complex and endoplasmic reticulum fractions isolated from African trypanosomes.

1984 ◽  
Vol 99 (2) ◽  
pp. 569-577 ◽  
Author(s):  
D J Grab ◽  
S Ito ◽  
U A Kara ◽  
L Rovis
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Smooth Endoplasmic Reticulum ◽  
Surface Glycoprotein ◽  
Relative Distribution ◽  
African Trypanosomes ◽  
Independent Form ◽  
Variable Surface ◽  
Dependent Form

Highly enriched Golgi complex and endoplasmic reticulum fractions were isolated from total microsomes obtained from Trypanosoma brucei, Trypanosoma congolense, and Trypanosoma vivax, and tested for glycosyltransferase activity. Purity of the fractions was assessed by electron microscopy as well as by biochemical analysis. The relative distribution of all the glycosyltransferases was remarkably similar for the three species of African trypanosomes studied. The Golgi complex fraction contained most of the galactosyltransferase activity followed by the smooth and rough endoplasmic reticulum fractions. The dolichol-dependent mannosyltransferase activities were highest for the rough endoplasmic reticulum, lower for the smooth endoplasmic reticulum, and lowest for the Golgi complex. Although the dolichol-independent form of N-acetylglucosaminyltransferase was essentially similar in all the fractions, the dolichol-dependent form of this enzyme was much higher in the endoplasmic reticulum fractions than in the Golgi complex fraction. Inhibition of this latter activity in the smooth endoplasmic reticulum fraction by tunicamycin A1 suggests that core glycosylation of the variable surface glycoprotein may occur in this organelle and not in the rough endoplasmic reticulum as previously assumed.

Studies on the site of addition of sialic acid and glucosamine to rat α1-acid glycoprotein

1977 ◽  
Vol 55 (4) ◽  
pp. 408-414 ◽  
Author(s):  
J. C. Jamieson
Keyword(s):  
Endoplasmic Reticulum ◽  
Sialic Acid ◽  
Rat Liver ◽  
Golgi Complex ◽  
Smooth Endoplasmic Reticulum ◽  
Main Site ◽  
Acid Glycoprotein ◽  
Membrane Bound ◽  
Polypeptide Chains

Ultrasonic extracts of rough and smooth endoplasmic reticulum fractions and Golgi fractions from rat liver were examined by immunoelectrophoresis using antiserum to α1-acid glycoprotein. Rough endoplasmic reticulum fractions contained only sialic acid free α1-acid glycoprotein, whereas smooth endoplasmic reticulum and Golgi fractions also contained sialic acid containing α1-acid glycoprotein. Determination of the sialic acid contents of immune precipitates isolated from the extracts suggested that the Golgi complex was the main site of addition of sialic acid to α1-acid glycoprotein. Immunological studies on puromycin extracts of polyribosomes showed that polypeptide chains of α1-acid glycoprotein and albumin were assembled mainly on membrane-bound polyribosomes. Evidence is presented from incorporation studies with labelled leucine and glucosamine that initial glycosylation of α1-acid glycoprotein occurs mainly or entirely after release of nascent polypeptide from the ribosomal site.

Studies on Acute Phase Proteins of Rat Serum. III. Site of Synthesis of Albumin and α1-Acid Glycoprotein and the Contents of These Proteins in Liver Microsome Fractions from Rats Suffering from Induced Inflammation

1973 ◽  
Vol 51 (7) ◽  
pp. 1034-1045 ◽  
Author(s):  
J. C. Jamieson ◽  
F. E. Ashton
Keyword(s):  
Liver Microsome ◽  
Acute Phase Proteins ◽  
Specific Radioactivity ◽  
Rat Serum ◽  
Experimental Animals ◽  
Acid Glycoprotein ◽  
Inflammatory Agent ◽  
Microsome Fraction ◽  
Rapid Stimulation ◽  
Short Times

Following injection of L-ieucine-3H or D-glucosamine-14C to normal rats or rats suffering from inflammation for 12 h there was a delay of 10–15 min before label appeared in albumin and α1-acid glycoprotein in serum; thereafter, there were rapid increases in specific radioactivities. The specific radioactivity of L-leucine-3H in albumin in serum from normal and experimental animals was not significantly different; however, there was a more rapid increase in specific radioactivities of both labelled compounds in α1-acid glycoprotein isolated from serum from experimental animals. Immunological techniques coupled with radioautography indicated that the microsome fraction of liver was the subcellular site of synthesis of albumin and of carbohydrate and polypeptide moieties of α1-acid glycoprotein in normal and experimental animals. The contents of albumin and α1-acid glycoprotein in liver microsome fractions from normal and experimental animals were determined by application of the quantitative precipitin technique to Lubrol-W extracts of microsome material. Little change in content of albumin associated with microsome material was found as a result of inflammation; however, there was a significant increase in the content of α1-acid glycoprotein in microsome material from experimental animals, reaching a maximum at 8–12 h after inflammation. On the basis of these latter results, it is suggested (1) that there is a fairly rapid stimulation of synthesis of α1-acid glycoprotein by liver in response to inflammation and (2) that the increased content of α1-acid glycoprotein associated with microsome material at short times of exposure to inflammatory agent is responsible for the increased content of this protein found in serum at longer times of exposure to inflammatory agent.

Studies on Acute Phase Proteins of Rat Serum. V. Effect of Induced Inflammation on the Synthesis of Albumin and α1-Acid Glycoprotein by Liver Slices

1975 ◽  
Vol 53 (4) ◽  
pp. 401-414 ◽  
Author(s):  
J. C. Jamieson ◽  
K. E. Morrison ◽  
D. Molasky ◽  
B. Turchen
Keyword(s):  
Acute Phase ◽  
Polypeptide Chain ◽  
Serum Proteins ◽  
Acute Phase Proteins ◽  
Rat Serum ◽  
Acid Glycoprotein ◽  
Liver Slices ◽  
Microsome Fraction ◽  
Lower Capacity ◽  
Acute Phase Serum

Liver slices from normal rats and those suffering from inflammation for 24–48 h were incubated with L-[14C]leucine or D-[I4C]glucosamine. Immunological techniques coupled with radioautography indicated that the microsome fraction prepared from slices contained the subcellular site of synthesis of the polypeptide chain of serum albumin, and the polypeptide and carbohydrate chains of α1-acid glycoprotein; both proteins were also present in the medium in labelled forms. The contents of albumin and α1-acid glycoprotein in the medium and in extracts of liver from experiments with liver slices from control rats and 8–72 h experimental rats were determined using the quantitative precipitin technique. There was a net increase in synthesis of both proteins when slices from control and experimental animals were used, the increase showing up in medium proteins. However, slices from livers from 8–72 h experimental rats had a greater capacity for synthesis of α1-acid glycoprotein and a lower capacity for synthesis of albumin than slices from livers from control rats, the greatest changes occurring with slices from 24 h experimental rats. Changes in synthetic capacities of liver slices from experimental rats for albumin and α1-acid glycoprotein were always accompanied by large increases in specific radioactivities of total medium proteins when experiments involved incubation of slices with L-[3H]leucine and D-[14C]glucosamine. It is suggested that the increase in specific radioactivities of medium proteins following incubation of liver slices from experimental rats with labelled leucine and glucosamine is a characteristic of the response of liver to inflammation, and reflects changes in the capacity of liver for the synthesis of α1-acid glycoprotein and other acute phase serum proteins.

Studies on Acute Phase Proteins of Rat Serum. I. Isolation and Partial Characterization of an α1-Acid Glycoprotein and an α2-Macroglobulin

1972 ◽  
Vol 50 (8) ◽  
pp. 856-870 ◽  
Author(s):  
J. C. Jamieson ◽  
A. D. Friesen ◽  
F. E. Ashton ◽  
B. Chou
Keyword(s):  
Molecular Weight ◽  
Physical Properties ◽  
Acute Phase ◽  
Isoelectric Point ◽  
Acute Phase Proteins ◽  
Partial Characterization ◽  
Rat Serum ◽  
Acid Glycoprotein ◽  
Α2 Macroglobulin

An α1-acid glycoprotein and an α2-macroglobulin were isolated from serum from rats suffering from experimentally induced inflammation for 48 h. The proteins were characterized electrophoretically and immunologically and their carbohydrate compositions and some physical properties determined. The α1-acid glycoprotein contained 34.1% carbohydrate, had an isoelectric point of 2.95, and a molecular weight of 43 000. The α2-macroglobulin contained 15.9% carbohydrate, had an isoelectric point of 4.60, and a molecular weight of about 800 000. The properties of the two proteins are compared with those of similar proteins isolated from rats and other species.

scholarly journals Experimental Ehrlichia canis infection changes acute-phase proteins

2012 ◽  
Vol 21 (3) ◽  
pp. 206-212 ◽  
Author(s):  
Thiago Demarchi Munhoz ◽  
Joice Lara Maia Faria ◽  
Giovanni Vargas-Hérnandez ◽  
José Jurandir Fagliari ◽  
Áureo Evangelista Santana ◽  
...  
Keyword(s):  
Early Detection ◽  
Early Diagnosis ◽  
Acute Phase ◽  
Acute Phase Proteins ◽  
Ehrlichia Canis ◽  
Laboratory Findings ◽  
Early Detection Of Disease ◽  
Acid Glycoprotein ◽  
The Third ◽  
Canine Ehrlichiosis

Early diagnosis of canine ehrlichiosis favors prompt institution of treatment and improves the prognosis for the animal, since this disease causes mortality among dogs. Studies have shown that determining the concentration of acute-phase proteins (APPs) may contribute towards early detection of disease and aid in predicting the prognosis. This study aimed to evaluate the APP profile in dogs experimentally infected with Ehrlichia canis, at the start of the infection and after treatment. It also investigated whether any correlation between APP levels and the clinical and laboratory alterations over the course of the disease would be possible. The results obtained showed abnormal levels of all the APPs on the third day after infection (D3), with the highest levels being reached on D18, with the exception of ceruloplasmin and acid glycoprotein, which presented their peaks on D6 and D12 respectively. We concluded that assessment of APP levels could contribute towards establishing an early diagnosis of canine ehrlichiosis, particularly regarding acid glycoprotein and ceruloplasmin, since these proteins were detected at increased levels even before the onset of clinical and laboratory findings of the disease.

scholarly journals Expression of Enamel Proteins in Rough Endoplasmic Reticulum and Golgi Complex in Human Dental Germs

2017 ◽  
Vol 35 (2) ◽  
pp. 435-441
Author(s):  
Francisco Javier Gutiérrez-Cantú ◽  
Alma Lilián Guerrero-Barrera ◽  
Wulfrano Sánchez Meraz ◽  
Amaury de Jesús Pozos-Guillen ◽  
Héctor Flores-Reyes ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Rough Endoplasmic Reticulum ◽  
Golgi Complex ◽  
Enamel Proteins

scholarly journals Luminometric assays of seven acute-phase proteins in minimal volumes of serum, plasma, sputum, and bronchioalveolar lavage.

1986 ◽  
Vol 32 (5) ◽  
pp. 743-747 ◽  
Author(s):  
J Braun ◽  
T Schultek ◽  
K F Tegtmeier ◽  
A Florenz ◽  
C Rohde ◽  
...  
Keyword(s):  
Acute Phase ◽  
Acute Phase Proteins ◽  
Immunoglobulin A ◽  
C Reactive Protein ◽  
Acid Glycoprotein ◽  
Reactive Protein ◽  
Coefficients Of Variation ◽  
Alpha 1 Antitrypsin ◽  
Heel Prick ◽  
Secretory Immunoglobulin

Abstract We describe immunoluminometric assays for seven acute-phase proteins, which can be determined in minimal volumes of plasma, serum, sputum, and bronchioalveolar lavage. The theoretical volume of serum or plasma required to measure all seven analytes in duplicate is 130 nL, although in practice the smallest volume of sample was enough to fill a hematocrit tube (about 25 microL of blood), collected from neonates by the heel-prick method. The assays could be performed with 10 microL of sputum or with 100 microL of bronchioalveolar lavage. We measured alpha 1-antitrypsin, alpha 2-macroglobulin, alpha 1-acid glycoprotein, thyroxin-binding prealbumin, C-reactive protein, and total and secretory immunoglobulin A. The assays are rapid enough for all results to be returned to the ward on the same day and are suitable for monitoring neonatal sepsis. All coefficients of variation, derived from compound precision profiles, were less than 7% for clinically relevant analyte concentrations. Correlation with commercially available nephelometric assays was good.

scholarly journals Concentrations of acute-phase proteins and immunoglobulins in serum and synovial fluid in clinically healthy heifers and steers

2019 ◽  
Vol 39 (6) ◽  
pp. 388-392
Author(s):  
Paula A. Di Filippo ◽  
Saulo T. Lannes ◽  
Marcos A.D. Meireles ◽  
Andressa F.S. Nogueira ◽  
Célia R. Quirino
Keyword(s):  
Synovial Fluid ◽  
Acute Phase ◽  
Acute Phase Proteins ◽  
Immunoglobulin A ◽  
Crossbred Cattle ◽  
Acid Glycoprotein ◽  
Molecular Weights ◽  
Sds Page ◽  
Radiocarpal Joint ◽  
Statistical Program

ABSTRACT: The aim of the study was to determine the concentration pattern of intra-articular acute phase proteins (APPs) and immunoglobulins in healthy crossbred cattle. Synovial fluid (SF) samples were collected from the radiocarpal joint of 25 heifers and 25 steers. Concentrations of APPs were measured by SDS-PAGE. The results were submitted to analysis of variance using the SAS statistical program, and means were compared by the Student-Newman-Keuls test (P<0.05). Thirty-seven proteins with molecular weights ranging from 7 to 37kDa were identified in SF of all animals. Eight were nominally identified with immunoglobulin A (IgA) and G (IgG), ceruloplasmin (Cp), transferrin (Tf), albumin (Ab), α1-antitripsin (AAT), α1-acid glycoprotein (AGP), and haptoglobin (Hp). The α1-antitripsin was only identified in the Sf of the heifers. The SF values of Cp, Hp, AGP and IgA were significantly higher in heifers than in 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, however the α1-antitrypsin was identified only in SF. The serum values Tf, AGP and IgG were significantly higher in heifers compared with steers. In conclusion, the physiological acute-phase proteins concentrations in synovial fluid of healthy ruminants can be useful in the interpretation of samples from animals with joint diseases. The SF electrophoretic profile of healthy ruminants differs depending on gender. Similar proteins were nominally identified in the sera, but only the SF of α1-antitrypsin.

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