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PubMed2026

Functional mapping of the Trypanosoma cruzi serinome by fluorophosphonate activity-based protein profiling.

Serine hydrolases (SHs) constitute one of the largest enzyme superfamilies in eukaryotes, yet their roles in Trypanosoma cruzi, the causative agent of Chagas disease, remain largely uncharacterized. Here, we report an activity-based chemoproteomic map of the T. cruzi epimastigote serinome by combining genome-informed in silico curation with whole-cell activity-based protein profiling (ABPP) using a panel of cell-permeable fluorophosphonate (FP)-alkyne probes. Whole-cell labelling followed by label-free quantitative proteomics (LFQ-MS) identified 37 enriched SH-like proteins, including 35 with conserved or partially conserved catalytic triad/dyad features, spanning lipases, peptidases, esterases, and previously uncharacterized hydrolases. The 35 SHs represent approximately 63% of the 56 predicted SHs retained after catalytic-site curation. Domain architecture analysis revealed broad structural diversity, while orthologue-based localization data suggested association with multiple subcellular compartments, including glycosomal, mitochondrial, and endosomal localizations. Gene Ontology enrichment highlighted lipid metabolic and catabolic processes as dominant functional themes, and protein-protein interaction network analysis supported functional connectivity among the captured enzymes. Several identified SHs, including oligopeptidase B, prolyl oligopeptidase Tc80, serine carboxypeptidase CPB1, and phospholipase A1 (PLA1) have previously been characterized in trypanosomatids, with roles linked to parasite virulence or host-pathogen interactions. Together, these findings establish a fluorophosphonate-based chemoproteomic resource for the kinetoplastid community and prioritize probe-accessible active T. cruzi SHs for future functional validation and antiparasitic inhibitor discovery.

Activity-based protein profiling↗

PubMed1990

Feedback regulation and the intracellular protein profile of Streptomyces griseus in a cycloheximide fermentation.

Two-dimensional gel electrophoresis (2-D PAGE) was used to study the intracellular protein profile of Streptomyces griseus in relation to cycloheximide (CH) biosynthesis. Four proteins (CR1-CR4) were found to be significantly and specifically repressed by addition of the antibiotic (1 g/l at 72 h) to a producing fermentation. Synthesis of these proteins was specific to the idiophase, concurrent with CH production. Initial addition of CH to the production medium resulted in slightly lower synthesis rates of two of the proteins (CR1 and CR2), while significantly delaying the onset of synthesis of the other two (CR3 and CR4). Finally, neutral polymeric resin was added to the fermentation to alleviate feedback regulation of CH synthesis, giving roughly a twofold increase in the antibiotic production rate. Production of proteins CR3 and CR4 was increased approximately tenfold immediately following resin addition, but returned to the control rate of synthesis after 24 h.

Autoradiography↗

PubMed1994

Protein profiles of Brucella suis and Brucella abortus in isoelectric focusing and sodium dodecyl sulphate-polyacrylamide gel electrophoresis.

The protein profiles of five field isolates of Brucella suis and four field isolates of B. abortus were examined. Isoelectric focusing of soluble proteins from cell sonicates produced 28 bands common to both species, with a further 10 bands being unique to a species. No intraspecies variation was detected. Sodium dodecyl sulfate extracted proteins were resolved by polyacrylamide gel electrophoresis. The proteins were transferred to nitrocellulose and then stained. These techniques allowed the demonstration of 35 bands which were common to both species, with a further 15 bands which were unique to one of the two species. Again, no intraspecies variation was detected.

Animals↗

PubMed2002

The effect of temperature on midgut and brain protein profiles in Morimus funereus larvae (Coleoptera: Cerambycidae).

The 7-days shift of M. funereus larvae, from nature to a constant temperature of 23 degrees C led to changes in midgut and brain protein quality and quantity. The changes in midgut protein profiles are characterized by an intensified protein band Mr of 29 kD, the absence of protein Mr of 22 kD and less intense bands Mr of 8.5-2.5 kD. Electrophoretic patterns of brain proteins showed less intense Mr of 66-2.5 kD protein bands.

Animals↗

PubMed2005

Cell cycle protein profile of the hepatic stellate cells(HSCs)in dimethylnitrosamine-induced rat hepatic fibrosis.

Cell cycle regulating proteins are known to have close relation with the proliferation of the mammalian cells. In injured liver, the number of HSCs is increased from proliferation. However, the expression of cell cycle proteins of HSCs during proliferation remains unevaluated. Therefore, cell cycle protein profiles of HSCs were studied in dimethyl-nitrosamine (DMN)-induced rat liver fibrosis model. Sprague-Dawley rats were intraperitoneally injected of DMN and the animals were sacrificed every week up to 4 weeks. HSCs were separated and the number of the cells in S phase was counted to evaluate the cell proliferation by flow cytometry. The expression of cyclin A, cyclin B, cyclin D1, cdk2, cdk4, cdc2, proliferating cell nuclear antigen (PCNA), p21(Cip/WAF1), and p27 was examined with immunoblotting analysis. Portion of S-phase cells peaked 7days after DMN injection. At that time, cyclin A, and PCNA showed significant increase in HSCs compared to untreated HSCs (114% and 116%, respectively, P<0.001). p21(Cip/WAF1) was decreased significantly in DMN-treated HSCs compared to control cells (88%, P<0.001). The increase of cyclin A, and PCNA and the decrease of p21(Cip/WAF1) seem to play important roles in the proliferation of HSCs during the early period of DMN treatment.

Animals↗

PubMed1988

Evaluation of a computer-assisted method of analysing SDS-PAGE protein profiles in tracing a hospital outbreak of Serratia marcescens.

Sodium dodecyl sulphate-polyacrylamide gel electrophoresis (SDS-PAGE) profiles of bacterial proteins have been successfully used for taxonomical purposes. More recently this technique has been applied to epidemiological investigations in respect of various micro-organisms including Neisseria meningitidis, Staphylococcus aureus and Clostridium difficile. The main limitations of the methods so far described are lack of standardisation in extraction and separation as well as in the analysis of results. Although reproducibility in the same laboratory has been shown to be satisfactory, comparison of results among laboratories is still difficult. Moreover, assessment of differences and/or similarities among chromatograms or autoradiographs showing many bands depends upon qualitative descriptions. Interpretation of densitometric scannings is laborious and time-consuming. In this paper we present our experience of a completely standardised, fully computer-controlled procedure for SDS-PAGE (AMBIS System) in analysing 35S-methionine-labelled total proteins. The methodology proved very useful in monitoring a hospital outbreak of Serratia marcescens. It allowed us to make quantitative comparison in a shorter time as well as to handle easily a great amount of data and usefully integrate it with those obtained with other systems such as serotyping. Furthermore, when the two systems are used together, more precise information can be gained. In this epidemic, serotyping indicated the presence of two groups which would have been missed by PAGE analysis alone. Electrophoretotyping, however, focused on similarities of cellular proteins among the epidemic strains. This allowed us to distinguish them from epidemiologically unrelated strains of the same serogroup.(ABSTRACT TRUNCATED AT 250 WORDS)

Bacterial Infections↗

PubMed1992

Changes induced in serum protein profiles by ovarian stimulation during in-vitro fertilization--embryo transfer treatment: a comparison between conception and non-conception cycles.

The profiles of plasma protein concentrations during the follicular phase in unstimulated women and in women undergoing ovarian stimulation for in-vitro fertilization--embryo transfer (IVF-ET) treatment are described. Plasma protein concentrations are correlated with those of total oestradiol (protein-bound and free) and total progesterone. In addition, 10 conception cycles and 18 non-conception cycles are compared in an attempt to identify predictors of successful treatment. Ovarian stimulation caused a significant increase in follicular phase in serum concentrations of sex hormone binding globulin (SHBG), cortisol binding protein (CBP) and insulin-like growth factor binding protein 1 (IGFBP1). In contrast no increase was observed in unstimulated cycles. Serum levels of endometrial protein PP14 decreased significantly during the follicular phase in both stimulated and unstimulated cycles. Levels of pregnancy zone protein (PZP) were more than doubled at the time of oocyte aspiration compared to the unstimulated cycles. Albumin concentrations were unchanged by the stimulation. Throughout the follicular phase, levels of SHBG were significantly higher, and total oestradiol significantly lower in women who became pregnant, than in those who did not. Therefore, a low concentration of free, biologically active oestradiol seemed to favour pregnancy, as the concentration of albumin is similar in the two groups. The endometrial protein PP14 was significantly lower during the follicular phase in conception than in non-conceptional cycles. On day 2 of the treatment cycle, the PP14 concentration showed a 75% correct prediction of conception and non-conception cycles. These results suggest that levels of PP14 may predict successful IVF cycles even before hormonal treatment is commenced.

Adult↗

PubMed2005

The alteration of protein profile of Walker 256 carinosarcoma cells during the apoptotic process induced by ultrasound.

The objective of this study was to investigate the alteration of the protein profile in cells after sonication and to identify the key proteins involved in the process of cell apoptosis. Walker 256 carinosarcoma cells were exposed to focused ultrasound (US) at the intensity of 2.0, 7.0, 10.2, 14.2 and 17.0 W/cm2 (I(spta)) for 10 min in vitro and the morphologic and functional changes of the cells were detected by hematoxylin & eosin staining and flow cytometry, with double staining of fluorescein isothiocyanate (FITC)-labeled Annexin V/propidium iodide (PI). The protein compositions in the cells after sonication were detected by 2-D SDS polyacrylamide gel electrophoresis. Our results showed that apoptosis of Walker 256 carinosarcoma cells could be induced by US. The percentage of early apoptosis and secondary necrosis increased with increasing intensity of US irradiation. Comparing with the protein patterns of cells before sonication, it was found that around 420 new protein spots were present in the gel after sonication. Among them, Hsp60 and Bcl-2 like protein 13 were found to be involved in the process of cell apoptosis and US-induced apoptosis of the cells was probably performed through the pathway of promoting the activation of caspase-3.

Animals↗

PubMed1997

[Comparison of outer membrane protein profiles of Vibrio sp].

The outer membrane protein (OMP) profiles of 32 Vibrio type strains have been compared. The major OMP profiles of different Vibrio species had a considerable heterogenecity. Most of the strains had 3-7 major OMPs, with molecular masses ranging between 91,000 and 14,000. Many strains had common major OMPs such as 54,000, 43,000 and 27,000. However, no common major OMPs in all Vibrio type strains had been found.

Bacterial Outer Membrane Proteins↗

PubMed2006

Protein profiling of sickle cell versus control RBC core membrane skeletons by ICAT technology and tandem mass spectrometry.

A proteomic approach using a cleavable ICAT reagent and nano-LC ESI tandem mass spectrometry was used to perform protein profiling of core RBC membrane skeleton proteins between sickle cell patients (SS) and controls (AA), and determine the efficacy of this technology. The data was validated through Peptide/Protein Prophet and protein ratios were calculated through ASAPratio. Through an ANOVA test, it was determined that there is no significant difference in the mean ratios from control populations (AA1/AA2) and sickle cell versus control populations (AA/SS). The mean ratios were not significantly different from 1.0 in either comparison for the core skeleton proteins (alpha spectrin, beta spectrin, band 4.1 and actin). On the natural-log scale, the variation (standard deviation) of the method was determined to be 14.1% and the variation contributed by the samples was 13.8% which together give a total variation of 19.7% in the ratios.

Anemia, Sickle Cell↗

PubMed2006

Comparison of the protein profile of established and regressed hypertension-induced left ventricular hypertrophy.

Established left ventricular hypertrophy (LVH) showed a significant alteration in the cardiac protein profile compared with normal heart. The main finding of this work was to identify proteins differently expressed in hypertension-induced LVH and the fact that after regression of LVH (histologically determined), the proteome still maintains a number of expressed proteins characteristic of the hypertrophied heart. These unrecovered proteins play an essential role in the energy production pathway, in cellular stress defense and also in hypertrophy regulation.

Amino Acid Sequence↗

PubMed1985

Pattern of protein profiles of reproductive organs after induced bilateral cryptorchidism in albino rats.

Bilateral cryptorchidism was induced surgically in albino rats and pattern of protein profiles was studied in reproductive organs. Cryptorchidism activated tissue proteolysis leading to overall degradation in soluble and structural protein fractions and in amino acids leading to prevalence of negative nitrogen balance in the reproductive organs. The testicular hypoalbuminic and hypoglobulinic conditions seem to be responsible for oligo-astheno-spermia associated with cryptorchidism.

Amino Acids↗

PubMed2026

Characteristics of Protein Profiling and Biomarkers in Aortic Regurgitation With Heart Failure.

BACKGROUND: Valvular heart disease, particularly aortic valve disease including stenosis and regurgitation, is a common heart disease. This study aimed to explore the protein profiling and the biomarkers in severe aortic valve disease and to provide new insights into the therapeutic strategy. METHODS: Blood samples from 80 subjects were collected and analyzed by data independent acquisition technique in 3 comparisons (mild/moderate-control, severe-control, and severe-mild/moderate) and validated by ELISA. The diagnostic value of differentially expressed proteins associated with severe valvular heart disease was also evaluated by the receiver operating characteristic curve. RESULTS: A total of 9976 peptides and 451 proteins were identified through liquid chromatography-tandem mass spectrometry analysis. From these, 64 in mild/moderate-control, 50 in severe-control, and 50 in severe-mild/moderate comparisons were identified as differentially expressed proteins. IGFBP7 (insulin-like growth factor-binding protein 7; 5581.0±697.0 ng/mL), DSG1 (desmoglein-1; 21.0±2.0 pg/mL), ADIPOQ (adiponectin; 26 686.0±3730 ng/mL), and JUP (junction plakoglobin; 10.2±0.6 ng/mL) levels in the severe group were significantly higher than that in the mild/moderate (P<0.05) group. Additionally, ADIPOQ and JUP levels in the severe group were also higher than that in control (P<0.001). Receiver operating characteristic curve analysis showed that IGFBP7, DSG1, JUP, and ADIPOQ had strong potential value to be associated with severe aortic valve disease. CONCLUSIONS: By constructing proteomics profile to identify the protein characteristics this study found that increased IGFBP7, DSG1, JUP, and ADIPOQ are the characteristics of proteins in patients with severe valvular heart disease. These findings provide new insight into the diagnosis and pathogenesis of valvular heart disease, particularly aortic valve disease.

Humans↗

PubMed2006

CyDye immunoblotting for proteomics: co-detection of specific immunoreactive and total protein profiles.

The development of ECL-Plex CyDye-conjugated secondary antibodies allows the advancement of conventional Western blotting, opening up possibilities for highly sensitive and quantitative protein confirmation and identification. We report a novel proteomic method to simultaneously visualise the total protein profile as well as the specific immunodetection of an individual protein species by combining cyanine CyDye pre-labelled proteins and antibody immunoblotting. This technique proposes to revolutionise both 2-D immunoprobing and protein confirmation following MS analysis.

Amino Acid Sequence↗

PubMed2005

Protein profile of pepsin-digested carious and sound human dentine.

The purpose of this study was to describe the protein profile of pepsin-digested carious and sound dentine using sodium dodecyl sulfate polyacrylamide gel electrophoresis (SDS-PAGE). Carious and sound dentine powder was decalcified using 10% EDTA at pH 7.4 for 48 h. The decalcified pellet was digested using pepsin at pH 2 under sequenced conditions: at 4 degrees C for 24 h, a further 24 h at 23 degrees C, and finally for 24 h at 37 degrees C. After every step, the soluble fraction was separated by centrifugation and analyzed in 15% SDS-PAGE. Two bands at 56 and 62 kDa could be observed in carious dentine digests and were considered specific carious bands. Similar bands could be observed in sound dentine samples, but only after pepsin digestion at higher temperatures (23 degrees C and 37 degrees C). Pepsin digests non-helical collagen and the triple helix structure of collagen is lost when the temperature rises. The bands at 56 and 62 kDa in sound dentine specimens thus represent pepsin-cleaved collagen. There is a possibility that the specific carious bands in carious dentine represent collagen decomposed in a manner similar to the way pepsin digests native dentine collagen at 23 degrees C and 37 degrees C.

Collagen↗

PubMed1999

Characterization of protein profiles and cross-reactivity of Blastocystis antigens by sodium dodecyl sulfate-polyacrylamide gel electrophoresis and immunoblot analysis.

The protein profiles of Blastocystis hominis, B. lapemi, and B. ratti were analyzed by sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) and species could be differentiated by this means as well as by Western-blot analysis with polyclonal antibodies. No intraspecies difference could be distinguished between the two B. hominis isolates or the three B. ratti isolates. Western-blot analysis showed extensive cross-reactivity of B. lapemi and B. hominis antigens with anti-B. ratti serum. Some of the cross-reactive antigens were glycoproteins as determined on the basis of their sensitivity to periodate treatment.

Animals↗

PubMed2002

[Value of the protein profile in the diagnosis of infectious endocarditis when hemolysis is present].

PURPOSE: Haptoglobin (H) and orosomucoid (O) are acute phase proteins that increase in a parallel manner. When hemolysis and inflammation are both present, study of the O-H couple on the protein profile may reveal an unknown hemolysis. METHODS: To determine if hemolysis is more frequent during infectious endocarditis than during septicemia without valvulopathy or during valvulopathy without septicemia. Study of three groups of patients: 26 patients with infectious endocarditis, 13 patients with septicemia and 36 patients with valvulopathy without septicemia. Studied parameters were the O-H couple, hemoglobin and rate of O. RESULTS: Hemolysis is clear in patients with endocarditis. The difference O-H is significantly more important during endocarditis than during septicemia without valvulopathy (P < 0.001) and during valvulopathy without sepsis (P < 0.001). CONCLUSION: Study of the O-H couple may be useful for the diagnosis of endocarditis showing a difficult-to-diagnose hemolysis.

Biomarkers↗

PubMedDate not supplied

A chemometric approach to the detection of milk adulteration based on protein profiles determined by capillary electrophoresis.

The general objective of this study was to utilize chemometrics in the interpretation of capillary electrophoresis milk protein profiles, for the detection of pasteurized milk adulteration with rehydrated milk powder or a rehydrated dairy-based milk substitute. The specific objectives were 1) to collect quantitative data on major casein and whey proteins in authentic and adulterated milks in a single CE analysis; and 2) to apply a pattern recognition procedure, Soft Independent Modeling of Class Analogies (SIMCA), on collected CE protein data, for the development of a statistical model useful in the detection of pasteurized milk adulteration. Authentic samples were fresh milk collected from various farms over a period of six months. Adulterated samples were authentic fresh milk partially or totally substituted with rehydrated milk powder or a rehydrated commercial milk substitute at different levels. Quantitative protein data obtained by capillary free zone electrophoresis for beta-lactoglobulin, alpha-lactalbumin, beta-casein, and alpha-casein of 86 samples, authentic and adulterated samples, were used as a training set to build a SIMCA multivariate statistical model. The detection of sample outliers was useful for the elimination of unusual samples and optimization of the multivariate model. From the 35 commercial pasteurized milks tested, which were treated as unknowns, a total of 14 samples (40%) were not assigned to the authentic or fresh milk group, meaning that these samples had some type of adulteration at the levels included in the training set (> 15%). Decision-making on detecting adulteration of unknown commercial pasteurized milk samples was eased since predictions were based on statistical probabilities.

Animals↗