Von meyenburg complex: Report of a case and review of literature

Von Meyenburg complex (VMC) (biliary hamartoma) is found incidentally in 0.6%–2.8% of adult autopsies or during histological examination and is rarely found in children. They are small, multiple and occur anywhere in the liver. VMC typically causes no symptoms or disturbances in liver functions and in most instances are diagnosed incidentally. They may represent a diagnostic dilemma when liver metastasis is suspected. Given the diagnostic uncertainty over imaging in VMC, liver biopsy is often recommended for a definitive diagnosis. The malignant potential of this finding which is currently considered and frequently ignored raises the necessity of follow-up

Selective enrichment and sensitive detection of peptide and protein biomarkers in human serum using polymeric reverse micelles and MALDI-MS

Reverse-micelle forming amphiphilic homopolymers with carboxylic acid and quaternary amine substituents are used to selectively enrich biomarker peptides and protein fragments from human serum prior to matrix assisted laser desorption/ionization mass spectrometry (MALDI-MS) analysis. After depletion of human serum albumin (HSA) and immunoglobulin G (IgG), low abundance peptide biomarkers can be selectively enriched and detected by MALDI-MS at clinically relevant concentrations by using the appropriate homopolymer(s) and extraction pH value(s). Three breast cancer peptide biomarkers, bradykinin, C4a, and ITIH4, were chosen to test this new approach, and detection limits of 0.5 ng mL-1, 0.08 ng mL-1, and 0.2 ng mL-1, respectively, were obtained. In addition, the amphiphilic homopolymers were used to detect prostate specific antigen (PSA) at concentrations as low as 0.5 ng mL-1 by targeting a surrogate peptide fragment of this protein biomarker. Selective enrichment and sensitive MS detection of low abundance peptide/protein biomarkers by these polymeric reverse micelles should be a sensitive and straightforward approach for biomarker screening in human serum

Selective Enrichment and Sensitive Detection of Peptide and Protein Biomarkers in Human Serum using Polymeric Reverse Micelles and MALDI-MS

Reverse-micelle forming amphiphilic homopolymers with carboxylic acid and quaternary amine substituents are used to selectively enrich biomarker peptides and protein fragments from human serum prior to matrix assisted laser desorption/ionization mass spectrometry (MALDI-MS) analysis. After depletion of human serum albumin (HSA) and immunoglobulin G (IgG), low abundance peptide biomarkers can be selectively enriched and detected by MALDI-MS at clinically relevant concentrations by using the appropriate homopolymer(s) and extraction pH value(s). Three breast cancer peptide biomarkers, bradykinin, C4a, and ITIH4, were chosen to test this new approach, and detection limits of 0.5 ng mL-1, 0.08 ng mL-1, and 0.2 ng mL-1, respectively, were obtained. In addition, the amphiphilic homopolymers were used to detect prostate specific antigen (PSA) at concentrations as low as 0.5 ng mL-1 by targeting a surrogate peptide fragment of this protein biomarker. Selective enrichment and sensitive MS detection of low abundance peptide/protein biomarkers by these polymeric reverse micelles should be a sensitive and straightforward approach for biomarker screening in human serum