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PubMed2004

Protein profiling of urine from dogs with renal disease using ProteinChip analysis.

Measurement of total urinary proteins in individuals that tested positive by urinary dipstick is a typical method for assessing the presence of potentially serious renal disorders. In the absence of such overt proteinuria, however, measurement of specific urinary proteins may be useful in the diagnosis of nephropathies and may provide greater insight into the pathogenesis. The urine of 28 dogs (16 with renal disease and 12 healthy) was evaluated to determine whether specific low-molecular-weight proteins or the pattern of protein excretion could also be used as a marker of tubular dysfunction in dogs. Specific proteins were assessed by immunological methods, whereas protein profiles were determined by surface-enhanced laser desorption/ionization time-of-flight mass spectrometry (MS). In particular, changes in the excretion of retinol-binding protein (RBP) and Tamm-Horsfall protein (THP) appear to be of clinical relevance in the diagnosis of canine kidney diseases. The pattern of urinary protein and peptides revealed specific changes in abundance in dogs with renal disease at molecular masses (kD) of 11.58, 12.41, 12.60, 14.58, 20.95 (RBP), 27.85, and 65.69 (albumin). In conclusion, comparable proteins as in humans might be used as urinary markers for proximal (RBP) and distal (THP) tubular dysfunction in dogs. Surface-enhanced laser desorption/ionization time-of-flight MS is a promising tool for the study of kidney physiology and pathophysiology and might aid in the discovery of new biomarkers of renal disease.

Animals↗

PubMed2004

Proteomic study of a model causative agent of harmful algal blooms, Prorocentrum triestinum II: the use of differentially expressed protein profiles under different growth phases and growth conditions for bloom prediction.

Simultaneous comparison of differentially expressed protein profiles of Prorocentrum triestinum grown under different growth phases and growth conditions indicated the presence of phase-specific and stress-responsive proteins, respectively. Correlation studies on these proteins in relation to cell division phasing patterns and to models of phytoplankton growth inferred the possible functions. Most notable among these proteins were groups of proteins thought to trigger or mediate cells through specific phases of division of this alga, e.g., BP1, BP2, PB1, PB2, and PB3. Other proteins (e.g., group 1 proteins) thought to be responsible for maintaining and supporting cell concentration under adverse conditions were found. Furthermore, another group of proteins (group 2 proteins) thought to be stress-responsive were also detected. Taken overall, these differentially expressed proteins provided important information for uncovering various protective and adaptive mechanisms in the dinoflagellate's life cycle. These proteins have the potential to serve as "indicator proteins" for rapid assessment of the nutritional or metabolic status of these phytoplankton cells,and monitoring the differential expression of these phase-specific proteins and stress-specific proteins could be an important biomarker for bloom prediction.

Algal Proteins↗

PubMed1991

Outer membrane protein profiles of Yersinia ruckeri.

The outer membrane protein (OMP) profiles of 135 isolates of Yersinia ruckeri, obtained from nine European countries (100 isolates), North America (23 isolates), Australia (six isolates) and South Africa (two isolates), and including four reference strains, were examined by SDS-PAGE. Outer membranes were isolated by selective solubilisation of the cytoplasmic membrane with 0.5% (w/v) sodium N-lauroyl sarcosinate (Sarkosyl). Outer membrane proteins were stable after in vitro passage and there was no variation in OMP profiles due to colony selection. With the exception of a 39.5 kDa peptidoglycan-associated protein there was also no variation at different stages of the growth cycle. The 39.5 kDa protein was not produced during logarithmic growth phase but increased in abundance as the stationary phase progressed. Interstrain variation occurred in the possession of a 36.5 or 38 kDa heat-modifiable protein and in the possession of peptidoglycan-associated proteins in the molecular weight range 36.5 to 40.5 kDa. Based on variation of these proteins five OMP-types, designated OMP-types 1-5, were identified among the 135 isolates examined. Outer membrane protein analysis was demonstrated to be useful in epidemiological studies of Y. ruckeri.

Animals↗

PubMed2003

Protein profiling in daunorubicin-induced cardiomyopathy.

The aim of this paper was to study the protein remodelling of the left ventricle following repeated administration of either daunorubicin (DNR) or DNR in combination with the cardioprotective agent dexrazoxane (DXZ). The experiment was carried out on three groups of Chinchilla male rabbits: 1. DNR (3 mg/kg i.v.), 2. DNR (3 mg/kg i.v.) + DXZ (60 mg/kg i.p.), and 3. the control group (saline 1 ml/kg i.v. in the same schedule). The drugs were given once weekly, max. 10 administrations. Protein fractions were isolated by stepwise extraction from the samples of the left ventricle. In the DNR-group, the concentrations of both, metabolic and contractile proteins were significantly reduced, while the amount of collagen was significantly higher in comparison with the control group. In the group treated with DNR and DXZ, the concentrations of individual protein fractions (except metabolic proteins) were comparable to those of the control group, which confirms a significant cardioprotective effect of DXZ. The changes of protein profiling corresponded to functional examination of both cardiac parameters (EF, dP/dt(max), PEP: LVET index) and histological examination. These data should be used in further studies dealing with evaluation of cardiotoxic and, possibly, cardioprotective effects of new drugs.

Animals↗

PubMed1992

Alterations in myofibrillar function and protein profiles after complete global ischemia in rat hearts.

We studied changes in myofibrillar function and protein profiles after complete global ischemia with anoxia in rat hearts. Hearts were exposed to global ischemia and anoxia (CGI) for 30 or 60 minutes at 37 degrees C, and myofibrils were prepared for measurement of Ca(2+)-dependent Mg(2+)-ATPase activity at pH 7.0 and 6.5. Hearts incubated in cold saline (1 +/- 1 degrees C) and nonincubated hearts served as controls. Maximum ATPase activity was unchanged at pH 7.0 and pH 6.5 in myofibrils from hearts treated with 30 or 60 minutes of CGI. At pH 7.0, the Hill coefficient, which is an index of cooperative interactions among thin-filament proteins, was unchanged after 30 minutes of CGI but was significantly increased after 60 minutes of CGI. A similar trend for increased cooperativity was observed when myofibrillar ATPase activity was measured at pH 6.5 in myofibrils from rat hearts made ischemic for 30 or 60 minutes. Both 30 and 60 minutes of CGI resulted in increased pCa50 values (half-maximally activating free [Ca2+]) at pH 7.0 and pH 6.5. Densitometric analysis of myofibrillar proteins separated with sodium dodecyl sulfate-polyacrylamide gel electrophoresis indicated that troponin I and troponin T were degraded during 60 minutes of CGI. Two new protein bands appearing in ischemia-treated myofibrils were identified as partially degraded troponin I and troponin T with Western blots. The troponin I fragment could be phosphorylated by cAMP-dependent protein kinase. In addition, we observed phosphorylation of a protein band that corresponded to myosin light chain-2 in myofibrils from CGI-treated hearts. These results suggest that degradation of thin-filament proteins may contribute to the changes in cooperativity of Ca2+ regulation of ATPase activity observed in the myofibrils from rat hearts exposed to CGI.

Animals↗

PubMedDate not supplied

Differences between atrial and ventricular protein profiling in children with congenital heart disease.

The purpose of the present study was to compare protein profiling of atria and ventricles in children operated for congenital heart disease. Tissue samples were obtained during surgery from patients with normoxemic (ventricular and atrial septal defects) and hypoxemic (tetralogy of Fallot) diseases. Protein fractions were isolated by stepwise extraction from both right ventricular and atrial musculature. The concentration of total atrial protein in the normoxemic patients exceeded the ventricular value (110 +/- 2.1 vs 99.9 +/- 4.0 mg.g-1 wet weight, respectively); in the hypoxemic group this atrio-ventricular difference disappeared. The concentration of contractile proteins in all cardiac samples was significantly higher in the ventricles as compared with atria, while the concentration of collagenous proteins was significantly higher in the atria (due to a higher amount of the insoluble collagenous fraction). The concentration of sarcoplasmic proteins (containing predominantly enzyme systems for aerobic and anaerobic substrate utilization), however did not differ between ventricles and atria. Furthermore, ventricular contractile fractions obtained from both normoxemic and hypoxemic patients were contaminated with the myosin light chain of atrial origin. Soluble collagenous fractions (containing newly synthesized collagenous proteins, predominantly collagen I and III), derived from all ventricular samples, were contaminated by low molecular weight fragments (mol. weight 29-35 kDa). The proportion of the soluble collagenous fraction was significantly higher in atrial but not in ventricular myocardium of hypoxemic children as compared with the normoxemic group. It seems, therefore, that lower oxygen saturation affects the synthesis of collagen preferentially in atrial tissue.

Actins↗

PubMed2000

Differential protein profile in the ear-punched tissue of regeneration and non-regeneration strains of mice: a novel approach to explore the candidate genes for soft-tissue regeneration.

Wound repair/regeneration is a genetically controlled, complex process. In order to identify candidate genes regulating fast wound repair/regeneration in soft-tissue, the temporal protein profile of the soft-tissue healing process was analyzed in the ear-punched tissue of regeneration strain MRL/MpJ-Fas(lpr) (MRL) mice and non-regeneration strain C57BL/6J(B6) mice using surface-enhanced laser desorption and ionization (SELDI) ProteinChip technology. Five candidate proteins were identified in which responses of MRL to the ear punch were 2-4-fold different compared to that of B6. Their corresponding genes were predicted using an antigen-antibody assay validated mass-based approach. Most of the predicted genes are known to play a role or are likely to play a role in the wound repair/regeneration. Of the five candidate proteins, the amount of the 23560 Da protein in the ear-punched tissue was significantly correlated with the rate of ear healing in six representative strains of mice, making it a good candidate for fast wound repair/regeneration. We speculate that the increased concentration of the 23560 Da protein in the wound tissue could stimulate the expression of various growth-promoting proteins and consequently speed up the wound repair/regeneration processes. Here, we have shown that examination of protein expression profile using SELDI technology, coupled with database search, is an alternative approach to search for candidate genes for wound repair/regeneration. This novel approach can be implemented in a variety of biological applications.

Animals↗

PubMed1987

Typing of Acinetobacter calcoaceticus strains isolated from hospital patients by cell envelope protein profiles.

The usefulness of sodium dodecyl sulphate-polyacrylamide gel electrophoresis patterns of cell envelope proteins for classifying strains of Acinetobacter calcoaceticus was studied using 129 isolates from 16 in-patients in a teaching hospital. In 11 patients, all of the isolates from each patient exhibited the same pattern irrespective of the body site or time of isolation. The patterns of the isolates from four other patients were indistinguishable, with the exception of one isolate per patient. In the isolates from one patient five patterns were observed. In several cases isolates from different patients exhibited the same pattern. The relative frequency of some of these patterns was low. Epidemiological data were compatible with the assumption that the concurrent presence of bacteria of these patterns in the patients was the result of cross-infection. For one pattern, which was seen in seven patients, cross-infection could not be substantiated. On the basis of analysis of electrophoretic patterns in combination with epidemiological data on a number of strains it is concluded that cell-envelope protein profiles appear to be a useful aid in studying the dissemination of Acinetobacter in the hospital environment.

Acinetobacter↗

PubMed1982

Isozyme patterns and protein profiles in neuromuscular disorders.

The isozyme patterns of six different enzymes and the polypeptide profiles of soluble proteins have been examined in muscle biopsy specimens from 74 patients with a wide variety of neuromuscular disorders. About half of the samples showed unusual features in at least one, and often several, of the enzymes and proteins tested. The extent of the biochemical abnormalities was roughly proportional to the severity of the disorders. In all cases the unusual isozymes and polypeptide profiles seemed to reflect a reversion to the fetal pattern of gene expression. However, this change appeared to occur in extant muscle and was not dependent on the appearance of new muscle fibres. Among the enzymes, phosphoglycerate mutase followed by creatine kinase appeared to be the most sensitive index of muscle disorder. The extent of the change in the muscle creatine kinase isozyme pattern was not correlated with the levels of serum creatine kinase activity.

Acid Phosphatase↗

PubMed1982

Comparison of secretory protein profiles in developing rat pancreatic rudiments and rat acinar tumor cells.

We have previously established that secretory proteins from a rat acinar cell tumor lack two forms of procarboxypeptidase B, are deficient in a major lipase species, and possess markedly reduced amounts of the basic proteins proelastase, basic chymotrypsinogen, basic trypsinogen and ribonuclease (Iwanij, V., and J.D. Jamieson, J. Cell Biol., 95:734-741). Because secretory proteins are markers for acinar cell differentiation, we sought to establish whether the secretory protein profile of the acinar cell tumor is unique to the transformed cell or whether it resembles that of a stage of normal pancreatic development. To this end, we compared the secretory protein pattern from acinar tumor cells with that of rat pancreatic rudiments at days 19-22 of gestation and through day 21 of the postnatal period. Two-dimensional IEF-SDS gel electrophoresis coupled with biosynthetic labeling and fluorography indicates a time-dependent appearance of individual secretory proteins with basic polypeptides, except for amylase, appearing in the terminal stages of differentiation. In comparison, the secretory protein pattern of the acinar tumor cells most closely resembles that of day-19 embryonic pancreatic rudiments. We propose that the cells of the acinar cell tumor may, in part, mirror a stage of normal pancreatic development.

Amylases↗

PubMed1993

Malathion disposition in dermally and orally treated rats and its impact on the blood serum acetylcholine esterase and protein profile.

14C-methoxy-malathion with either pure or 50% E.C. formulated malathion were applied orally or dermally at one tenth of their LD50 to two batches of male albino rats. More than 90% of 14C was released with urine after 24 hours. The rest of 14C was detected in the feces, blood, intestines, liver and kidney in a descending order. No significant 14C was detected in other organs. Comparing the oral pure and formulated malathion treatments, there was no significant variation in the rate of disposition or excretion of 14C-malathion. However, the dermal treatment revealed that the 14C-formulated malathion was released faster than the pure one in urine in the first 24 hours; while the 14C-pure malathion showed relatively higher levels in the feces and blood in the first 24 hours. In a third batch of male albino rats, the effect of the same level of dermal treatment by either pure or 50% E.C. formulated malathion on serum acetylcholine-esterase (A. Ch. E.) activity and serum protein profile was studied. The serum A. Ch. E. activity was found to be inhibited to 40% activity after 6 to 24 hours for both treatments. However, after 96 hours the serum of the pure malathion treated rats showed full recovery of A.Ch.E. activity, while the formulated malathion treated showed only 60% activity. The SDS-PAGE analysis showed a differentiation in the serum protein bands of the 48 hours exposed rats to formulated malathion which was confirmed by the scanned gel profile. The FPLC integrated chromatograms proved an initiation of a new protein band accompanied with rearrangement of the albumin and pre-albumin bands. Thus it can be concluded that, the impact on the blood serum protein profile and A. Ch. E. activity can be used as reliable criteria to detect acute toxicity of malathion and other choline-esterase inhibitors in exposed field workers. Further research is needed to elucidate the specificity and sensitivity of such criteria as biomarkers for human exposure.

Acetylcholinesterase↗

PubMed2005

Changes in mussel Mytilus galloprovincialis protein profile as a reaction of water pollution.

In the present report the changes in mussels Mytilus galloprovincialis protein profile, as a reaction of water pollution, is presented. The antioxidant capacity was determined by the efficacy to scavenge the derived radical in mussel samples using the Trolox Equivalent Antioxidant Capacity (TEAC) assay. The highest percentage of inhibition was estimated in protein mussels from the dirty area (DM) in comparison with the clean samples (CM). The amounts of both zinc and copper determined by atomic spectroscopy were significantly higher in the protein mussels from the dirty than from the clean areas (P<0.05). Fourier Transform Infrared (FT-IR) spectroscopy and fluorescence revealed specific qualitative changes in secondary and tertiary structures of mussel proteins from the dirty area by the shift in the amides I and II positions and fluorescence intensity. Estimated temperature and enthalpy of denaturation in the protein mussels well correlated with fluorescence and spectroscopic measurements and showed the changes influenced by water pollution.

Animals↗

PubMed2026

Protein Profiling Identifies Biomarkers for Predicting Disease Severity in Anti-NMDAR Encephalitis.

Anti-N-methyl-D-aspartate receptor (NMDAR) encephalitis is a severe autoimmune neurological disorder characterized by pathogenic antibodies against the NMDAR. A systematic protein profiling approach is warranted to identify biomarkers capable of predicting disease status. An Olink proximity extension assay (PEA) profiled 91 inflammation-related proteins from anti-NMDAR encephalitis patients. Disease severity or prognosis were assessed by CASE score or mRS score at 6-month follow-up. Patients were stratified into distinct molecular clusters using unsupervised clustering. Logistic regression models incorporating selected biomarkers were developed to predict disease severity and prognosis, followed by absolute quantification using ELISA. Patients were classified into four consensus clusters. Clusters 1 and 2 corresponded to the mild group, while Cluster 3 represented the severe group, consistent with CASE score above 6. Cluster 4 showed heterogeneous clinical features. Elevated serum levels of IL-10, IL-6, and SIRT2, as well as increased CSF levels of CXCL10, CXCL11, and MMP10, were positively associated with severe disease. Conversely, several proteins including LTA and CCL11, CCL8, TGFB1, CXCL6 were associated with severe disease or unfavorable 6-month outcomes. A logistic regression model combining serum CXCL6 and CCL11 with CSF MMP10 achieved an area under the curve (AUC) of 0.95 for predicting disease severity. Serum CCL11 alone showed predictive value for 6-month prognosis, with an AUC of 0.79. These findings delineate distinct protein signatures associated with clinical heterogeneity of anti-NMDAR encephalitis. Prediction models incorporating multiple biomarkers may provide an approach for disease severity stratification and prognosis forecast.

Humans↗

PubMed1996

Protein Profile Variation in Cultivated and Native Freshwater Microorganisms Exposed to Chemical Environmental Pollutants

Assimilation of 35S-precursors into microbial proteins was used to investigate toxicity and adaptational responses that occur in nutrient enriched and natural freshwater samples experimentally contaminated with benzene, toluene, trichloroethylene (TCE), or xylene. Experiments were conducted to analyze (1) the potential of using microbial community protein profiles for responsive identification of chemical pollutant exposure, (2) the inhibition of microbial productivity through reduction in rate of protein synthesis caused by specific chemical pollutants, and (3) whether selection of subpopulations in freshwater microbial communities challenged with chemical pollutants leads to adaptive strategies mediated by production of particular polypeptides. The results show that distinct banding patterns of polypeptides in the range of 30 to 100 kilodaltons that were obtained following collective cultivation of freshwater microorganisms differ with each chemical pollutant. Protein yield and radioisotope incorporation were reduced within ten minutes of micro-bial exposure to chemical pollutants in the following order: xylene < toluene < benzene < TCE. Adaptation of the freshwater microbial community to chemical pollutants prior to radioisotope incorporation produced differences in polypeptide profiles, in the banding patterns of radioactive polypeptides, and in the rate of radioisotope incorporation. The rate of radioisotope incorporation by freshwater microorganisms pre-adapted to chemical pollutants was lowest with xylene (88.1% reduction), followed by TCE (84.0% reduction),toluene (67.3% reduction), and benzene (43.5% reduction). In long-term radioisotope incorporation experiments, protein yield and polypeptide radioactivity was higher in the presence of chemical pollutants than in uncontaminated control samples, suggesting increased metabolic productivity attributable to the chemical pollutants.

Journal Article↗

PubMed1994

A comparison of whole cell protein profiles for sporadic human isolates of Streptococcus equisimilis and beta-haemolytic group G streptococci.

Whole cell protein profiles were resolved for Streptococcus equisimilis (group C) and large colony human biotype beta-haemolytic group G streptococci by the use of one dimensional sodium dodecyl sulphate-polyacrylamide gel electrophoresis. Strains of S. equisimilis (27 in toto) were distributed among eight patterns designated A to H. Pattern A represented 48.2% of the latter isolates. Strains of group G streptococci (59 in toto) were distributed among sixteen patterns designated 1-16, and there were no predominant patterns which represented more than 20% of all strains. Profiles were reproducible, not susceptible to strain passage, but susceptible to variation in growth media. Considerable homology was observed among bacteria in either Lancefield group.

Bacterial Proteins↗

PubMedDate not supplied

DNA binding protein profiles in Alzheimer's disease.

Eleven frozen autopsy specimens from cerebral cortex were tested for DNA-binding protein profiles. Six were Alzheimer's disease (AD) brains, 1 was Parkinson's/senile dementia of the Alzheimer's type and 4 were age-matched control brains. Proteins were extracted in a guanidine thiocyanate-containing solvent and freed of all nucleic acids by density gradient sedimentation. The proteins were separated by sodium dodecyl sulfate gel electrophoresis and transferred to nitrocellulose by electroblotting under conditions which favor renaturation of proteins containing only one type of polypeptide. The nitrocellulose was treated with partially denatured radiolabeled DNA, washed and subjected to autoradiography. An Mr = 43 000 (43 K) DNA-binding protein was detected in 5 of the 6 AD brains and was found to be absent or at least greatly reduced in any of the other 6 brains. No other DNA-binding proteins were found which could be associated with AD brains. The nature of the 43 K protein has yet to be determined.

Aged↗

PubMed1994

Differential changes in cell morphology, macromolecular composition and membrane protein profiles of neurons and astrocytes in chronic ethanol treated rats.

Cellular morphology, macromolecular composition, (DNA, RNA and Protein content) marker enzyme activities for neurons [neuron specific enolase (NSE)] and astrocytes [glutamine synthetase (GS)] and plasma membrane protein profiles in the bulk isolated neurons and astrocytes from control and ethanol treated rats were studied. One month aged Wistar rats were given ethanol as sole drinking fluid for 10 weeks. Scanning electron microscopy revealed a characteristic cell surface smoothening in astrocytes due to ethanol treatment. DNA levels were unaltered, while RNA and Protein contents were decreased in astrocytes and neurons. Further, 3H-leucine incorporation into proteins was decreased in neurons and astrocytes derived from ethanol treated rats indicating reduced protein synthesis in neurons and astrocytes. GS activity was affected severely suggesting impairment in astrocytic functions. Plasma membrane protein composition was analyzed by 2-D electrophoresis. The analysis indicated several protein defects in the plasma membranes of neurons and astrocytes, which might be involved in 'membrane disorder' during ethanol challenge. 125I-Wheat Germ agglutinin binding studies showed three prominent proteins (160, 116 and 97 kDa) in astrocyte membrane fraction suggesting the possible involvement of N-terminal glycoproteins in altered astrocyte morphology during ethanol ingestion. Impairment in the astrocyte cell functions, protein changes in plasma membrane and cellular morphology studies suggest that astrocytes may be more vulnerable than neurons for ethanol effects.

Alcoholism↗

PubMed2001

Protein profiling comes of age.

Ever since DNA microarrays were first applied to the quantitation of RNA levels, there has been considerable interest in generating a protein homolog that can be used to assay cellular protein expression. A recent paper describes the first microarray that can be used for such protein profiling.

Gene Expression Profiling↗