Plasma proteins as biomarkers of the aging process

1995 ◽  
Vol 268 (2) ◽  
pp. R536-R548 ◽  
Author(s):  
R. Vranckx ◽  
L. Savu ◽  
N. Lambert ◽  
G. V. de Conchard ◽  
R. Grosse ◽  
...  
Keyword(s):  
Aging Process ◽  
Serum Proteins ◽  
Enzyme Inhibitor ◽  
Binding Capacity ◽  
Protein Biosynthesis ◽  
Exclusion Criterion ◽  
Protein Patterns ◽  
Rat Serum ◽  
Crossed Immunoelectrophoresis ◽  
Age Related

This study was designed to characterize the rat serum proteins as biomarkers of the normal aging process. Crossed immunoelectrophoresis or electroimmunodiffusion quantitation of proteins was performed in rats aged 6, 12, 24, and 30 mo. Selection of healthy animals was based on confrontation of crossed immunoelectrophoresis patterns with those of experimentally inflamed young adults and with individual anatomopathological data. Convergence of inflammatory patterns and severe histological lesions was the exclusion criterion. Senescence-induced decrease was demonstrated for eight proteins [negative senescence reactants (SRs-)] and increase for six proteins [positive SRs (SRs+)]. Most SRs belonged to the class of proteins responsive to acute inflammation [acute phase reactants (APRs)]. One SR+, the thyroxine-binding globulin, a high-affinity thyroid hormone binder, emerged as a particularly reliable senescence biomarker, showing the highest aging-related variation (8-fold increase from 6 to 30 mo) and not belonging to the APR class. Chronic treatment with perindopril, an angiotensin I-converting enzyme inhibitor used in heart and renal disease therapy, significantly enhanced thyroxine-binding capacity, possibly by preventing age-related alterations of serum lipids. Serum protein patterns prove valuable both as indexes for selecting aging animals free from superimposed pathologies and as parameters of senescence-induced changes in protein biosynthesis.

THE THYROXINE-BINDING PROPERTIES OF SERUM PROTEINS. A COMPETITIVE BINDING TECHNIQUE EMPLOYING SEPHADEX G-25

1975 ◽  
Vol 65 (3) ◽  
pp. 319-332 ◽  
Author(s):  
R. L. SUTHERLAND ◽  
M. W. SIMPSON-MORGAN
Keyword(s):  
Binding Proteins ◽  
Serum Proteins ◽  
Binding Capacity ◽  
Specific Binding ◽  
Competitive Binding ◽  
Association Constants ◽  
Binding Properties ◽  
Rat Serum ◽  
Human Proteins ◽  
Dilute Blood

SUMMARY A competitive binding technique is described for the estimation of the thyroxine (T4)-binding properties of serum proteins in dilute blood serum and lymph. When used in conjunction with an assay for total T4 the following parameters can be estimated: the number of functionally different T4 binding proteins, their individual association constants and binding capacities for T4, the amount of T4 which is bound to each binding species, and the concentration of unbound (free) T4. Both human and sheep serum have three functionally different T4-binding proteins. The association constants for the three human proteins were 9·5 × 109, 1·6 × 108 and 3·1 × 105 1/mol for T4-binding globulin (TBG), T4-binding prealbumin (TBPA) and serum albumin, respectively. The corresponding sheep proteins, TBG, TBP-2 and albumin, had association constants of 8·9 × 109, 1·4 × 108 and 3·5 × 1051/mol. Human TBG had a mean binding capacity of 21·3 μg/100 ml and that of ovine TBG was 12·8 μg/100 ml. The other specific binding proteins (TBPA in man and TBP-2 in sheep) had mean binding capacities of 307 and 359 μg/100 ml respectively. Two functionally different T4-binding proteins were identified in rat serum.

Characterization of exocoelomic fluid protein from rat conceptuses cultured in rat and human sera: a measure of yolk sac activity during organogenesis

Development ◽  
1984 ◽  
Vol 84 (1) ◽  
pp. 203-215
Author(s):  
I. M. Huxham ◽  
F. Beck
Keyword(s):  
Human Serum ◽  
Serum Proteins ◽  
Polyacrylamide Gel Electrophoresis ◽  
Protein Composition ◽  
Rat Serum ◽  
Macromolecular Transport ◽  
Two Fluids ◽  
Crossed Immunoelectrophoresis ◽  
Human Sera

Fluid from the extraembryonic coelom of 11·5-day rat embryos cultured in 100% rat serum, 100% human serum and 90% human serum supplemented with 10% rat serum between days 9·5 and 11·5 postconception were compared using polyacrylamide gel electrophoresis and crossed immunoelectrophoresis. The protein composition of the exocoelomic fluids differed considerably from one another and from each of their respective culture sera. The majority of proteins in the exocoelom were derived from macromolecular transport but some contribution was made from protein synthesis by the conceptus. Eighteen proteins normally found in rat serum were found in the exocoelom of conceptuses cultured in 100% rat serum. Eighteen proteins were found in the exocoelom of rat conceptuses cultured in 100% human serum, of which ten were derived from human serum and eight were proteins normally found in rat serum. Analysis of fluid from conceptuses cultured in 90% human serum supplemented with 10% rat serum showed eleven human serum proteins and ten rat serum proteins. Differences in the composition of both human and rat proteins between the latter two fluids were also evident.

Age-Related Changes in Valproic Acid Binding to Rat Serum Proteins in Vitro*

1996 ◽  
Vol 85 (4) ◽  
pp. 373-376 ◽  
Author(s):  
Patricia W. Slattum ◽  
Allen E. Cato ◽  
Gary M. Pollack ◽  
Kim L.R. Brouwer
Keyword(s):  
Valproic Acid ◽  
Serum Proteins ◽  
Rat Serum ◽  
Age Related ◽  
Age Related Changes

FACTORS INFLUENCING TRIIODOTHYRONINE BINDING PROPERTIES OF LIVER NUCLEAR RECEPTORS

1976 ◽  
Vol 83 (2) ◽  
pp. 293-304 ◽  
Author(s):  
Leslie J. Degroot ◽  
Janine Torresani ◽  
Pierre Carrayon ◽  
Alain Tirard
Keyword(s):  
Nuclear Receptor ◽  
Liver Cell ◽  
Serum Proteins ◽  
Binding Capacity ◽  
Protein S ◽  
Receptor Protein ◽  
Cell Nuclei ◽  
Rat Serum

ABSTRACT Triiodothyronine (T3) may bind directly to receptors present in liver cell nuclei, or may be transported into nuclei by receptor protein(s) present in the cytosol. To evaluate these possibilities, T3 binding was studied in vitro using liver cell nuclei isolated from rats exposed in vivo to very low (H), normal (N), or high levels of T3 (H + T3), and using nuclei incubated in vitro with added cytosol proteins. Ka for T3 was 0.075 ± 0.05 × 1010 m−1 in N, 0.1+0.04 in H, and 0.094 + 0.04 in H + T3, and pg T3 bound/100 μg DNA were 47 ± 17, 31 ± 14, and 29 ± 8 in the three groups. The data indicate no difference in binding capacity between the groups related to prior in vivo exposure to T3, and that T3 may bind directly to empty nuclear receptor sites. Rat liver cytosol proteins added to the in vitro incubation medium always depressed T3 uptake by nuclei. Bovine serum albumin had a similar effect. Large amounts of rat serum proteins depressed uptake, but low levels augmented T3 binding through an unknown mechanism. It is probable that free T3 in serum is in equilibrium with free T3 in the cytosol and nucleus, and binds directly to nuclear receptor proteins without mediation by a cytosol receptor protein.

ZUR REGULATION DER PROTEINBIOSYNTHESE DURCH SEXUALHORMONE: DIE WIRKUNGEN VON OESTRADIOLBENZOAT UND VON TESTOSTERONPROPIONAT AUF DIE KONZENTRATION VON SERUMPROTEINEN

1970 ◽  
Vol 62 (2_Suppl) ◽  
pp. S9-S60 ◽  
Author(s):  
Alfred Oberdorfer
Keyword(s):  
Sex Hormones ◽  
Serum Protein ◽  
Laying Hens ◽  
Testosterone Propionate ◽  
Serum Proteins ◽  
Protein Biosynthesis ◽  
Total Serum Protein ◽  
Total Serum ◽  
Specific Gene ◽  
Protein Patterns

ABSTRACT Following intramuscular injections of oestradiol-17 β 3-monobenzoate and testosterone propionate in domestic fowl, typical alterations in the immunoelectrophoretic, starchgelelectrophoretic and ultracentrifugal patterns of serum proteins were observed. These effects are due to alterations in the concentrations of specific serum proteins. Both sex hormones alter the concentrations of the same proteins. The concentrations of various proteins are increased by one of the two hormones and decreased by the other. The administration of oestradiol-17β 3-monobenzoate alters the serum-protein patterns of pullets and immature cocks, nonlaying mature hens and mature cocks towards the pattern characteristic for laying hens. Testosterone propionate alters the pattern of serum proteins for laying hens towards the pattern that is characteristic for pullets and immature cocks, nonlaying mature hens and mature cocks. These alterations are reversible. Both the extent and the duration of the alterations are dependent upon the amounts of the hormones given. The results are discussed as being phenomena of hormonal effects on the biosynthesis of proteins. A comparison of the effects of the two sex hormones on the concentrations of total serum protein shows that in the case of oestradiol-17 β 3-monobenzoate the activating effects dominate. Testosterone propionate, however, seems to have more inhibitory effects than activating ones on the biosynthesis of proteins. On the basis of the theory advanced by Jacob & Monod, concerning the regulation of protein biosynthesis, and related to Karlson's hypothesis of gene activation, a model is proposed for a theoretical explanation of the results obtained here. It is assumed that both sex hormones, acting as effectors, influence the function of repressors with complementary structures and in this way activate or inactivate specific gene loci that are responsible for the biosynthesis of proteins.

EFFECT OF pH ON THE BINDING OF THYROXINE TO SERUM PROTEINS

1970 ◽  
Vol 65 (3) ◽  
pp. 409-422 ◽  
Author(s):  
Theodore Coutsoftides ◽  
Amirav Gordon
Keyword(s):  
Serum Albumin ◽  
Serum Proteins ◽  
Binding Capacity ◽  
Ph Sensitive ◽  
The Other ◽  
Rat Serum ◽  
Effect Of Ph ◽  
Thyroxine Binding Globulin ◽  
Other Hand ◽  
Maximal Binding

ABSTRACT The maximal binding capacity of human thyroxine-binding globulin (TBG) was found to decrease, and that of thyroxine-binding pre-albumin (TBPA) to increase with an increase in pH in the range of pH 7.2 to 8.2. On the other hand, the transfer of T4125I from the serum to a weak binder (Sephadex) was found to decrease with increasing pH. The same phenomena was shown to exist in mouse and rat serum, and to be blocked by DNP, a potent TBA & TBPA binding inhibitor. It is suggested that serum albumin may play a pH sensitive role in the T4 transfer to tissue.

scholarly journals Age-related change of cefazolin binding to rat serum proteins and its relation to the molar ratio of free fatty acid to serum albumin.

1986 ◽  
Vol 9 (1) ◽  
pp. 81-87 ◽  
Author(s):  
TETSUYA TERASAKI ◽  
NORISHIGE IMAEDA ◽  
KAZUNORI NISHIDE ◽  
AKIRA TSUJI
Keyword(s):  
Fatty Acid ◽  
Free Fatty Acid ◽  
Serum Albumin ◽  
Serum Proteins ◽  
Molar Ratio ◽  
Rat Serum ◽  
Age Related

scholarly journals Changes on proteomic and metabolomic profile in serum of mice induced by chronic exposure to tramadol

2021 ◽  
Vol 11 (1) ◽  
Author(s):  
Shukun Jiang ◽  
Guojie Liu ◽  
Huiya Yuan ◽  
Enyu Xu ◽  
Wei Xia ◽  
...  
Keyword(s):  
Chronic Exposure ◽  
Molecular Mechanisms ◽  
Fatty Acid Biosynthesis ◽  
Serum Proteins ◽  
Enzyme Inhibitor ◽  
Bile Secretion ◽  
Control Group ◽  
Protein Digestion ◽  
Metabolomic Profile ◽  
Apolipoprotein C

AbstractTramadol is an opioid used as an analgesic for treating moderate or severe pain. The long-term use of tramadol can induce several adverse effects. The toxicological mechanism of tramadol abuse is unclear. Limited literature available indicates the change of proteomic profile after chronic exposure to tramadol. In this study, we analyzed the proteomic and metabolomic profile by TMT-labeled quantitative proteomics and untargeted metabolomics between the tramadol and the control group. Proteomic analysis revealed 31 differential expressed serum proteins (9 increased and 22 decreased) in tramadol-treated mice (oral, 50 mg/kg, 5 weeks) as compared with the control ones. Bioinformatics analysis showed that the dysregulated proteins mainly included: enzyme inhibitor-associated proteins (i.e. apolipoprotein C-III (Apoc-III), alpha-1-antitrypsin 1–2 (Serpina 1b), apolipoprotein C-II (Apoc-II), plasma protease C1 inhibitor, inter-alpha-trypsin inhibitor heavy chain H3 (itih3)); mitochondria-related proteins (i.e. 14-3-3 protein zeta/delta (YWHAZ)); cytoskeleton proteins (i.e. tubulin alpha-4A chain (TUBA4A), vinculin (Vcl)). And we found that the differential expressed proteins mainly involved in the pathway of the protein digestion and absorption. Metabolomics analysis revealed that differential expressed metabolites mainly involved in protein ingestion and absorption, fatty acid biosynthesis, steroid hormone biosynthesis and bile secretion. Our overall findings revealed that chronic exposure to tramadol changed the proteomic and metabolomic profile of mice. Moreover, integrated proteomic and metabolomic revealed that the protein digestion and absorption is the common enrichment KEGG pathway. Thus, the combination of proteomics and metabolomics opens new avenues for the research of the molecular mechanisms of tramadol toxicity.

The interrelationship between and the regulation of hepatic growth hormone receptors and circulating GH binding protein in the pig

1992 ◽  
Vol 126 (2) ◽  
pp. 155-161 ◽  
Author(s):  
Geoffrey R Ambler ◽  
Bernhard H Breier ◽  
Andrzej Surus ◽  
Hugh T Blair ◽  
Stuart N McCutcheon ◽  
...  
Keyword(s):  
Growth Hormone ◽  
Growth Hormone Receptor ◽  
Hormone Receptors ◽  
Binding Capacity ◽  
Binding Protein ◽  
Somatic Growth ◽  
Gh Receptor ◽  
Age Related ◽  
Igf I ◽  
Serum Gh

We evaluated the interrelationship between, and regulation of, the hepatic growth hormone receptor and serum GH binding protein (GH BP) in pigs treated with recombinant porcine growth hormone (rpGH). Infant and pubertal male pigs (N = 5 per group) received either rpGH 0.15 mg/kg daily or diluent intramuscularly for 12 days. Somatic growth, serum IGF-I and GH BP and [125I]bovine GH (bGH) binding to MgCl2-treated hepatic membrane homogenates were examined. Marked age-related increases were seen in serum GH BP (p<0.001) and [125I]bGH binding to hepatic membranes (p<0.001). GH BP was increased in rpGH treated animals (p = 0.03), from 13.8±1.2 (mean±1 x sem) (controls) to 17.8±2.0% in infants, and from 35.2±2.6 (controls) to 41.8±3.4% in pubertal animals. [125I]bGH binding to hepatic membranes was also increased by rpGH treatment (p<0.05), from 7.0±1.6 (controls) to 15.4±3.6% in infants and from 53.7±7.1 (controls) to 65.1±11.8% in pubertal animals. No significant interaction between age and treatment was seen. Overall, serum GH BP correlated significantly with [125I]bGH membrane capacity (r=0.82, p<0.001), with a correlation of r= 0.83 in the infant animals but no significant correlation in the pubertal animals considered alone (r=0.13). Serum IGF-I correlated significantly with serum GH BP (r=0.93, p<0.001) and [125]bGH membrane binding capacity (r = 0.91, p< 0.001). These observations suggest that serum GH BP levels reflect major changes of hepatic GH receptor status. In addition, the present study demonstrates that the hepatic GH receptor can be induced by GH in the infant pig, despite a developmentally low GH receptor population at this age, suggesting potential efficacy of GH at earlier ages than generally considered.

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