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At least 289 records · Page 16Linked to original sources
PubMed1998

Changes in plasma protein concentrations in ponies with experimentally induced alimentary laminitis.

OBJECTIVE: To determine whether plasma protein concentrations were altered in ponies with alimentary laminitis. ANIMALS: 12 adult ponies. PROCEDURE: Acute laminitis was induced in 6 ponies by oral administration of carbohydrate (85% corn starch, 15% wood flour); the other 6 ponies were used as controls. A physical examination was performed and blood samples were collected immediately before and 4, 8, 12, 24, and 28 hours after administration of carbohydrate. Plasma protein concentrations were determined by means of sodium dodecyl sulphate-polyacrylamide gel electrophoresis. RESULTS: 19 plasma proteins ranging from a molecular weight of 24,000 to a molecular weight of 350,000 were identified in all 12 ponies. Plasma concentrations of proteins with molecular weights of 350,000 (fibrinogen), 130,000 (ceruloplasmin), 118,000 (c-reactive protein), 67,000 (alpha1-antitrypsin I), 65,000 (alpha1-antitrypsin II), 50,000 (haptoglobulin), and 45,000 (acid glycoprotein) were significantly increased in ponies with laminitis, compared with concentrations in control ponies. CONCLUSION: Changes in plasma protein concentrations are detectable within 4 hours after the onset of alimentary laminitis in ponies. Clinical Relevance-Measurement of plasma protein concentrations may be useful in monitoring the progression of laminitis in ponies.

Animals↗
PubMed1990

Blood plasma proteins on polyurethane and alkylsiloxane plasma-treated polyurethane surfaces. Dynamic approach by stimulus-response technique. Part 2. Evaluation of adsorption data by moment technique.

In this study, interactions of blood proteins (i.e. albumin and fibrinogen) with polyurethane biomaterial surfaces were investigated in an in vitro bead column test circuit using a stimulus-response technique. The dynamic sorption process of radiolabelled proteins on the surfaces was followed by detecting the radioactivity at the exit stream of the column, which was the response of a pulse stimulus at the inlet. The mathematical model was described and solved using 'parameter estimation by cybernetic moment technique', and the adsorption rate constants of plasma proteins on different biomaterial surfaces were calculated. By evaluation of the response curves with standard and cybernetic moment techniques, the following results were obtained. Albumin and fibrinogen adsorption is competitive, and the competition is strongly dependent upon the surface characteristics of the biomaterial. Preadsorption or preferential adsorption of albumin decreases the fibrinogen adsorption, and therefore increases the biocompatibility of material surface. Adsorption of blood plasma proteins are irreversible. The moment technique can also be used for the evaluation of stimulus-response data of biological systems, to determine the process parameters.

Adsorption↗
PubMedDate not supplied

Some components of the kinin system in Cohn's unheated human plasma proteins.

The presence of a kininase and a kininogenase was demonstrated in unheated human plasma proteins. The kininase was found to inactivate synthetic bradykinin and a kinin-like substance released from a kininogen-like material in unheated plasma proteins by human urinary kallikrein. It was heat-labile and inhibited by EDTA, HgCl2 and 1,10-phenanthroline. This enzyme was estimated to be kininase I from its inhibition pattern. Inactivation of the kininase revealed the presence of a kininogenase. Five per cent heat-treated human plasma protein solution has been demonstrated to have no kininase activity but to contain the kinin-like substance. A mechanism for the formation of the kinin-like substance in 5 per cent heat-treated plasma protein solution was discussed in terms of these kinin forming components present in the unheated plasma proteins.

Blood Proteins↗
PubMed2000

Possibilities of extraction and characterization of ancient plasma proteins in archaeological bones.

Due to the mineral matrix bone proteins are capable of surviving during centuries after inhumation, but cross-linking with other bone proteins as well as fragmentation and complex reactions with humic acids and microorganisms lead to considerable alterations in molecular weight and structure of these proteins. Our group concentrates on polymorphic plasma proteins which diffuse out of the capillary system into the bone matrix where they adsorb to the mineralic substrate. So far, only little is known about the degradation and alteration of these proteins in fossil bones. It has to be evaluated whether the aged proteins still contain some of the information which renders them a valuable tool for forensic questions and population genetics in recent populations. Therefore we tried by modification of already existing methods to expand plasma protein identification and subtyping into the new field of aged plasma proteins.

Adult↗
PubMed1988

Use of arabinogalactan to obtain washed murine platelets free of contaminating plasma proteins and appropriate for studies of function, morphology, and thrombopoiesis.

A simplified procedure for preparing washed murine platelets, free of contaminating plasma proteins, has been developed. Platelet-rich plasma (PRP) was prepared from diluted whole blood from C57BL/6N mice by two centrifugations at 100 x g for 12 minutes. Platelets were concentrated and then washed by centrifugation through isosmolar 10% arabinogalactan (Stractan). Platelet recovery was 85% +/- 6% (1 SD) (n = 10) from whole blood to PRP and 86% +/- 4% (1 SD) (n = 6) from PRP to Stractan-washed platelets. Overall recovery of platelets with this technique was 73% +/- 10% (1 SD). Contamination of platelets with plasma proteins could not be detected with use of unlabeled platelets that had been incubated with radiolabeled plasma proteins followed by washing with Stractan. The Stractan-washed platelets were assessed for function by using aggregometry. The response of Stractan-washed platelets to collagen and thrombin was identical to that of unwashed platelets. Stractan-washed platelets did not respond to 20 mumol/L adenosine diphosphate unless supplemented with 12% platelet-free plasma. The morphology of the Stractan-washed platelets indicated that degranulation had not occurred. With use of antibodies directed against the alpha granule membrane protein GMP-140 or fibrinogen, no evidence of secretion or plasma protein contamination was observed. The use of this method resulted in an improved assay for the rate of thrombopoiesis, based on detection of radioactive proteins in newly synthesized platelets, by eliminating contamination by radioactive plasma proteins. Our results indicate that this procedure is a convenient method for the separation of platelets from platelet-rich plasma, free of plasma proteins, which are suitable for bioassays, functional studies, and morphologic investigations.

Animals↗
PubMedDate not supplied

Changes in plasma proteins during pregnancy.

Changes in maternal plasma proteins during pregnancy are now well documented. These changes may be quantitative, as seen in the electrophoretically separated fractions of serum and in the various binding globulins; or they may be represented by the appearance of a protein which is present only in the serum of pregnant women. These include the placental isoenzyme of alkaline phosphatase, oxytocinase, human chorionic gonadotropin and the "pregnancy-associated plasma proteins." Other constituents, such as alpha-fetoprotein, salivary amylase, prolactin and the proteins of the "pregnancy zone," which are present in small quantities in non-pregnant women as well as in men, show a substantial increase in concentration in the maternal circulation during pregnancy. An important factor in the etiology of protein changes is the effect of hormones, especially estrogen, on the synthesis and degradation of these proteins. While certain quantitative changes such as those seen in hormone binding proteins may interfere with diagnostic procedures, a number of pregnancy-associated changes in protein composition of the maternal circulation may be used to follow the course of pregnancy by monitoring placental function as well as fetal maturity and well being.

Blood Proteins↗
PubMed1991

Changes in fetal and maternal plasma protein concentration and colloid osmotic pressure with gestation.

In pregnant ewes, plasma protein levels over the gestation age range of 58-141 days fell progressively (r = -0.332, P less than 0.05, n = 36) but colloid osmotic pressure (COP, mmHg) did not change significantly. In fetal sheep carried by these ewes, plasma protein levels increased with age (r = 0.85, P less than 0.00001, n = 32). COP also rose (r = 0.8, P less than 0.00001, n = 23). Since maternal COP did not change and fetal COP increased, the net transplacental COP gradient between mother and fetus decreased with increasing age (r = -0.589, P less than 0.004, n = 22). Fetal plasma protein levels can be used to calculate fetal COP while maternal plasma protein levels cannot be used to calculate maternal COP.

Animals↗
PubMed1991

Extrahepatic expression of plasma protein genes during inflammation.

The body's protective responses to infection, wounding, trauma, and malignancy include the acute-phase reaction, which is modulated by various cytokines and their cellular receptors. During the acute-phase reaction, levels of specific proteins synthesized by the liver increase in the plasma. Little information is available about the extrahepatic synthesis of plasma proteins during the acute-phase reaction. The study described here analyzes the tissue-specific expression of genes encoding the plasma proteins albumin (ALB), alpha 1-antitrypsin (AAT), transferrin (TF), haptoglobin (HP), ceruloplasmin (CP), serum amyloid A (SAA), alpha 1-acid glycoprotein (AGP) and alpha 2-HS-glycoprotein (AHSG) during the acute-phase reaction in C57B1 mice. The acute-phase reaction was induced by intraperitoneal injections of bacterial lipopolysaccharide (LPS). During the acute-phase reaction, genes encoding CP, SAA, AGP, and HP demonstrate unique extrahepatic tissue specific patterns of expression in kidney, spleen, thymus, heart, brain, lung, testis, and epididymis. Different temporal patterns of HP gene expression also were observed in lung and thymus after induction by LPS. The function of extrahepatic synthesis of plasma proteins is not yet understood; however, a local provision of specific plasma proteins in mammalian tissues may offer the host a source of functionally important proteins during periods of stress.

Acute-Phase Reaction↗
PubMed1979

[Hyperdynamic septic shock in man: concentration course of selected coagulation factors and plasma proteins].

Coagulation factors and plasma proteins are significantly decreased in patients with hyperdynamic septic shock. Besides the activation of the coagulation system, the endotoxin-induced release of granulocyte proteases is responsible for a septic disseminated intravascular coagulation. In this situation special emphasis should be placed on the levels of antithrombin III regarding application of heparin.

Antithrombin III↗
PubMed2002

Drug-plasma protein binding assay by electrokinetic chromatography-frontal analysis.

We developed a rapid, microscale and reliable analytical method for binding of drugs to plasma proteins using capillary electrophoresis (CE) with ionic cyclodextrins (CD) combined with frontal analysis. These CDs were used as pseudostationary phases of electrokinetic chromatography (EKC). The CD-modified EKC (CDEKC) approach allowed us to separate anionic drugs from plasma proteins, whereas CZE could not separate these drugs from plasma proteins because they had a similar mobility like plasma proteins. CDs uniquely interact with these drugs but not with plasma proteins. Therefore, CDEKC could be coupled with frontal analysis to measure the binding of anionic drugs to plasma proteins. The binding values obtained by CDEKC were highly consistent with those determined by the ultrafiltration method. Our CDEKC approach should expand the applicability of CE to protein binding analysis.

Blood Proteins↗
PubMed1987

Plasma protein synthesis in experimental cancer compared to paraneoplastic conditions, including monokine administration.

During tumor growth, there are characteristic alterations in the concentration and synthesis of various plasma proteins. The purpose of this study was to evaluate whether these changes are unique to a tumor-bearing state, or rather, they represent a generalized response to a paraneoplastic state mediated by the release of monokines or protein-calorie malnutrition. Plasma protein synthesis and concentrations in mice bearing a transplantable fibrosarcoma were compared to animals receiving either a terpentine abscess, Corynebacterium parvum administration, calorie-protein depletion, or administration of the recombinant-derived monokines, murine interleukin 1 alpha or human tumor necrosis factor-alpha. Tumor-bearing animals showed a significant increase in total plasma protein synthesis that was similar in magnitude to the increase seen following a terpentine abscess or after administration of interleukin 1 or tumor necrosis factor-alpha. Similarly, the pattern of protein synthesis and concentration, as determined by isoelectric focusing or sodium dodecyl sulphate-polyacrylamide gel electrophoresis, were similar, albeit not identical, among tumor-bearing animals and those receiving either a terpentine abscess, C. parvum and monokine administration. Serum amyloid P concentrations were markedly elevated in tumor-bearing animals, as they were in animals after a sterile abscess and following interleukin 1 administration, as well as to a lesser extent tumor necrosis factor-alpha administration. We can therefore conclude that the majority of changes in plasma protein concentration and synthesis seen in this tumor-bearing model are similar to those seen during an acute inflammation and can be reproduced to a large extent by the administration of the monokines, interleukin 1 alpha or tumor necrosis factor-alpha.

Abscess↗
PubMed1990

Effects of three liquid diets on nutrition-sensitive plasma proteins of tube-fed elderly men.

The effects on three nutrition-sensitive plasma proteins of isocaloric feedings with three enteral formulas were compared in 10 tube-fed male nursing home residents. The enteral products were Isocal (based on whole protein), Peptamen (based on a mixture of oligopeptides), and Vivonex T.E.N. (based on free amino acids). The nutrition-sensitive plasma proteins were albumin, transferrin, and retinol-binding protein. After observation during four weeks of feeding with Isocal, each subject was then monitored during four weeks of Peptamen and four weeks of Vivonex T.E.N. The latter two products were alternated in a crossover design. The shift of Isocal to Peptamen did not significantly (P greater than .05) influence the serum level of albumin, transferrin, or retinol-binding protein. In contrast, the shift of Isocal to Vivonex T.E.N. or of Peptamen to Vivonex caused a significant (P less than .05) decline in all three plasma proteins, the kinetics of their reductions corresponding to their known half-lives. The behavior of the three nutrition-sensitive plasma proteins suggests that in elderly nursing home men without gastrointestinal disease the nutritional value of the protein component of the three formulas follows the order Isocal = Peptamen greater than Vivonex T.E.N. However, this conclusion will require confirmation by nitrogen balance studies.

Aged↗
PubMed1996

Reversion of thermic-shock effect on ram spermatozoa by adsorption of seminal plasma proteins revealed by partition in aqueous two-phase systems.

Centrifugal counter-current distribution (CCCD) in a dextran, Ficoll, poly(ethylene glycol) two-phase system was used to study the effect of seminal plasma proteins on the partition behaviour of ram spermatozoa exposed to thermal shock. Ram spermatozoa freed from seminal plasma by a 'swim-up' procedure were submitted to thermal shock and fractionated by CCCD. Cell viability decreased from 68% to 18% after the treatment, showing a slight displacement of the cells from the right (where a higher enrichment of live cells is found) to the centre of the profile. A change of the distribution profile was shown in the presence of either ram or bull seminal plasma. Bull seminal plasma was able to move the profile to the right, whereas ram seminal plasma increased the proportion of cells with enhanced affinity for the lower dextran-rich phase. Plasma proteins isolated from both seminal plasmas moved the profile to the right. In addition, cell viability rose to 48% after the CCCD run in the presence of ram plasma proteins. This restoring effect was lost when ram plasma proteins were thermally denatured. Bovine serum albumin was not only unable to move the profile to the right but even promoted displacement of the profile to the left. This negative effect was also observed when proteins from bull seminal plasma were in the presence of protein-free ram seminal plasma. However, proteins isolated from ram seminal plasma still restored the profile in the presence of bull seminal plasma freed from proteins. The results presented here strongly suggest that seminal plasma proteins are adsorbed by a spermatozoal surface previously exposed to thermic shock. These proteins would exert a highly specific protective effect on ram spermatozoa. In addition, in the ram seminal plasma there must be some factor which avoids this adsorption.

Adsorption↗
PubMed2000

Dietary plasma protein reduces small intestinal growth and lamina propria cell density in early weaned pigs.

ABSTRACT We quantified the effects of a diet containing animal plasma protein on small intestinal growth and mucosal morphology in early weaned pigs. Ninety-six pigs [14 d old, 4 kg body weight (BW)] were assigned in groups of 32 to three dietary treatments as follows: 1) free access to control diet (C), 2) free access to plasma protein diet (P), and 3) plasma protein, pair-fed to C (PPF). Eight pigs from each group were killed at 2, 4, 8 or 16 d. Over a 16-d period, weight gain in the P group was 43% greater (P < 0.05) than that in C pigs; weight gain was similar in C and PPF groups. Protein intake in the P group was 33% higher (P < 0.05) than that in the PPF group; no significant difference was observed between the C and P groups. Dietary protein conversion efficiencies in both the P and PPF groups were approximately 18% greater (P < 0.05) than those in the C group. Intestinal masses in the three groups did not differ at 2, 4 and 8 d. By 16 d, the jejunal and ileal protein and DNA masses (mg/kg BW) in both the P and PPF groups were lower than those in the C group (P < 0.05). Dietary plasma protein did not affect crypt cell proliferation, crypt depth or villous height in either the jejunum or ileum. However, the intravillous lamina propria cell density in the jejunum was significantly lower (P < 0.05) in P and PPF pigs than in C pigs. Plasma urea concentrations were also 40 and 42% lower (P < 0.05) in the P and PPF groups, respectively, than in the C group. Our results indicate that dietary plasma protein reduces the cellularity of the lamina propria, but not epithelial cell surface of the small intestine. Feeding plasma protein also increased the efficiency of dietary protein utilization, in part, by decreasing amino acid catabolism.

Analysis of Variance↗
PubMed1996

Detection of plasma proteins in CNS neurons: conspicuous influence of tissue-processing parameters and the utilization of serum for blocking nonspecific reactions.

Despite the presence of a blood-brain barrier (BBB), plasma proteins have been detected intraneuronally in regions with axonal projections confined to the CNS. This finding raises the question of whether plasma proteins are taken up from the brain interstitium or whether the results are due to experimental artifact. We examined the effect of various protocols for tissue processing on the intraneuronal distribution of plasma proteins using immunohistochemistry. The detection level of plasma proteins decreased after prolonged fixation, irrespective of the fixative and embedding method employed. In cryostat sections, attempts to block nonspecific staining by serum protein caused considerable nonspecific staining in itself. When nonspecific staining was blocked with a serum-free buffer, specifically labeled neuronal perikarya were found in cryostat sections of brains fixed by perfusion with paraformaldehyde without postfixation. Albumin and IgG occurred predominantly in neurons having projections beyond the BBB but also sparsely in neurons having projections confined to the CNS. Transferrin was evenly distributed within neuronal somata, irrespective of the orientation of projections. The immunoreaction product of the three plasma proteins exhibited a specific intraneuronal localization in the differently projecting neurons. In circumventricular organs, plasma proteins were observed extracellularly and in projecting fibers. In conclusion, plasma proteins are present in neurons with projections confined to the CNS and are probably taken up from the brain interstitium.

Animals↗
PubMed2004

Seminal plasma proteins prolong the viability of rainbow trout (Oncorynchus mykiss) spermatozoa.

Rainbow trout (Oncorhynchus mykiss) spermatozoa were incubated in artificial sperm motility inhibiting saline solution (SMIS), in SMIS containing seminal plasma proteins or in pure seminal plasma. In SMIS containing the total seminal plasma protein fraction or the <50 kDa protein fraction or in pure seminal plasma, significantly higher motility rates and swimming velocities could be activated than in SMIS without seminal plasma proteins and in SMIS containing the >50 kDa protein fraction. These preliminary results indicated that seminal plasma proteins have physiological functions in prolongation and stabilization of sperm viability when using sperm motility as viability index.

Animals↗