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BACKGROUND: The treatment of large pelvic masses in postmenopausal women is a challenge in clinical practice. Although ultrasound or magnetic resonance imaging can be used to determine the size and location of the mass, it is still difficult to achieve a preoperative diagnosis. The majority of cellular leiomyomas are diagnosed by histopathology after surgery. We report the differential diagnosis and surgical management of a rare case of cellular leiomyoma in the broad ligament of the uterus. CASE SUMMARY: A 52-year-old Chinese woman without sexual history was admitted to the First Affiliated Hospital of Guangzhou University of Chinese Medicine for the first time. The patient had a 1-year history of progressive abdominal enlargement as well as a 2-year history of menopause, and complained of frequent abdominal pain and low-grade fever. Computed tomography of the abdomen showed a solid cystic mass (29.4 cm × 18.8 cm × 37.7 cm) in the pelvis and abdomen. Moreover, routine blood test results indicated a baseline cancer antigen 125 (CA-125) level of 187.7 U/mL and C-reactive protein of 109.58 mg/L. Subsequently, retrograde hysterectomy and bilateral adnexectomy were performed in this patient. On histopathologic examination of the surgical specimen, a rare cellular leiomyoma in the broad ligament was diagnosed. CONCLUSION: Clinicians need to constantly improve diagnosis and treatment for the challenges posed during clinical assessment, differential diagnosis, and surgical management.
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The iron oxide nanoparticles (Fe3O4) were prepared by organic molecule-assisted method in aqueous solution. The facile synthetic process of Fe3O4 nanoparticles was conducted only by mixing FeCl2 and 2-methylimidazole (2-MIM) without any additives. A possible growth mechanism of the Fe3O4 nanocrystals was proposed for this mild reaction. Then, the Fe3O4 nanoparticles were anchored onto graphene oxide (GO) sheets in water by ultrasound-assisted method, forming an affinity probe with strong biocompatibility. Due to the hydroxy and carboxylic groups of GO sheets, Fe3O4/GO probe exhibits excellent performance for enriching low-abundance hydrophilic peptides, while the Fe3O4 nanoparticles endure the probe with specific affinity to phosphopeptides. The analytical protocol was developed for sequential enrichment of low-abundance peptides and phosphopeptides by the affinity probe. It exhibited the sequence coverage of 26% for capture of 17 low-abundance peptides from bovine serum albumin (BSA), as well as the selectivity of 1:1:100 for phosphopeptides from α-/ß-casein/BSA, and low detectable concentration of 2.5â¯fmol and probe reusability of 5 times for capture of phosphopeptides from α-/ß-casein. Consequently, the prepared Fe3O4/GO material possesses excellent feature as multifunctional affinity probe for low-abundance peptides including phosphopeptides from complex biological matrices detected by matrix-assisted laser desorption ionization time-of-flight mass spectrometry.
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Caseínas/química , Grafito/química , Nanopartículas de Magnetita/química , Nanocompuestos/química , Péptidos/química , Fosfopéptidos/química , Albúmina Sérica Bovina/química , Interacciones Hidrofóbicas e Hidrofílicas , Espectrometría de Masa por Láser de Matriz Asistida de Ionización DesorciónRESUMEN
A facile solvothermal method for the synthesis of multifunctional magnetic CuFeMnO4 nanospheres affinity probe (NSAP) with controllable morphology and size was developed for the first time. The CuFeMnO4 nanospheres combine the brilliant features of Cu2+, Fe3+, and Mn2+ ions, so their multifunction performances are embodied by strong coordination to carboxyl and amine groups of peptides (Cu2+ and Fe3+), special affinity to phosphate groups of phosphopeptides (Fe3+ and Mn2+), and high magnetic responsiveness in a magnetic field. Their potential as an affinity probe was evaluated for highly effective enrichment, rapid magnetic separation of low-abundance peptides (neutral condition), and effective selective capture of phosphopeptides (acid condition) from various complex biosamples. Notably, CuFeMnO4 NSAP was explored for highly selective capture and isolation of phosphopeptides from A549 cells after exposure to ZnO nanoparticles for different times. Consequently, we put forward a new nanospinel ferrite-based protocol here to analyze and identify the phosphoproteins/phosphopeptides involved in cellular signaling pathways in response to exogenous stimulation.
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Compuestos de Manganeso/química , Nanosferas/química , Péptidos/química , Fosfopéptidos/química , Células A549 , Adsorción , Animales , Humanos , Magnetismo , Nanopartículas del Metal/química , Leche/metabolismo , Péptidos/análisis , Péptidos/sangre , Fosfopéptidos/análisis , Fosfopéptidos/sangre , Saliva/metabolismo , Espectrometría de Masa por Láser de Matriz Asistida de Ionización Desorción , Óxido de Zinc/químicaRESUMEN
This work presents a sequential enrichment protocol, based on two self-designed cerium-based nanocomposite affinity probes, which not only can effectively separate phosphopeptides from non-phosphopeptides but can also selectively differentiate mono- and multi-phosphopeptides for direct matrix-assisted laser desorption/ionization time-of-flight mass spectrometric (MALDI-TOF MS) analysis.
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The spinel-type magnetic manganese ferrite (MnFe2O4) microspheres synthesized by simple solvothermal method were used as a novel adsorbent for selective enrichment and effective isolation of phosphopeptides. The uniform MnFe2O4 magnetic affinity microspheres (MAMSs) had a narrow particle size distribution between 250 and 260nm, and displayed superparamagnetism with a saturation magnetization value of 67.0emu/g. Comprehensively, the possible formation mechanism of MnFe2O4 microspheres with ferric and manganous sources as dual precursors was elucidated by comparison with those of Fe3O4 nanoparticles and MnOOH nanosheets respectively with either ferric or manganous source as single precursor. It was suggested that the spherical or sheet nanostructures could be achieved via secondary recrystallization or Ostwald ripening. The MnFe2O4 MAMSs probe exhibited excellent dispersibility in aqueous solution, and rapid magnetic separation within 15s, as well as good reusability. More importantly, MnFe2O4 was highly selective for phosphopeptides because of the strong coordination interaction between metal ions (Fe3+ and Mn2+) and phosphate groups of phosphopeptdies. This high specificity was demonstrated by effectively enriching phosphopeptides from digest mixture of ß-casein and bovine serum albumin (BSA) with high content of non-phosphopeptides, and embodied further in phosphopeptides enrichment from non-fat milk digests and human serum. Consequently, the prepared MnFe2O4 affinity materials are expected to possess great potential in phosphoproteome research.
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Compuestos Férricos/química , Compuestos de Manganeso/química , Microesferas , Fosfopéptidos/química , Animales , Caseínas/química , Caseínas/metabolismo , Bovinos , Modelos Moleculares , Fosfopéptidos/metabolismo , Proteolisis , Tripsina/metabolismoRESUMEN
Polydopamine-coated Fe3 O4 magnetic nanoparticles synthesized through a facile solvothermal reaction and the self-polymerization of dopamine have been employed as a magnetic solid-phase extraction sorbent to enrich four phenolic compounds, bisphenol A, tetrabromobisphenol A, (S)-1,1'-bi-2-naphthol and 2,4,6-tribromophenol, from environmental waters followed by high-performance liquid chromatographic detection. Various parameters of the extraction were optimized, including the pH of the sample matrix, the amount of polydopamine-coated Fe3 O4 sorbent, the adsorption time, the enrichment factor of analytes, the elution solvent, and the reusability of the nanoparticles sorbent. The recoveries of these phenols in spiked water samples were 62.0-112.0% with relative standard deviations of 0.8-7.7%, indicating the good reliability of the magnetic solid-phase extraction with high-performance liquid chromatography method. In addition, the extraction characteristics of the magnetic polydopamine-coated Fe3 O4 nanoparticles were elucidated comprehensively. It is found that there are hydrophobic, π-π stacking and hydrogen bonding interactions between phenols and more dispersible polydopamine-coated Fe3 O4 in water, among which hydrophobic interaction dominates the magnetic solid-phase extraction performance.
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Lichee-like core-shell structured magnetic lutetium phosphate (Fe3O4@LuPO4) affinity microspheres were successfully synthesized and well characterized. Based on the properties of great specificity and rapid separation, magnetic LuPO4 microspheres were applied to selectively enrich phosphopeptides for MALDI-TOF MS analysis. The enrichment performance of the prepared microspheres was demonstrated by tryptic digests of standard protein (ß-casein), complex samples (tryptic digest mixture of ß-casein and bovine serum albumin at different molar ratios of 1 : 10 to 1 : 50), and real biological samples (fresh pure milk and human serum), respectively. The enrichment ability of magnetic LuPO4 microspheres for phosphopeptides was very satisfying and the captured phosphopeptides with a sharp enhancement in MS signals were reliably identified based on the appearance of metastable ion peaks with poor resolution of the corresponding dephosphorylated peptides in the mass spectra. Enrichment of phosphopeptides by the Fe3O4@LuPO4 affinity microspheres provides a powerful approach for large scale phosphoproteome analysis.
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A novel, sensitive and rapid CL method coupled with high-performance liquid chromatography separation for the determination of carbamazepine is described. The method was based on the fact that carbamazepine could significantly enhance the chemiluminescence of the reaction of cerium sulfate and tris(2,2-bipyridyl) ruthenium(II) in the presence of acid. The chromatographic separation was performed on a Kromasil® (Sigma-Aldrich) TM RP-C18 column (id: 150 mm × 4.6 mm, particle size: 5 µm, pore size: 100 Å) with a mobile phase consisting of methanol-water-glacial acetic acid (70:29:1, v/v/v) at a flowrate of 1.0 mL/min, the total analysis time was within 650 s. Under optimal conditions, CL intensity was linear for carbamazepine in the range 2.0 × 10(-8) ~ 4.0 × 10(-5) g/mL, with a detection limit of 6.0 × 10(-9) g/mL (S/N = 3) and the relative standard detection was 2.5% for 2.0 × 10(-6) g/mL (n = 11). This method was successfully applied to the analysis of carbamazepine in human urine and serum samples. The possible mechanism of the CL reaction is also discussed briefly.