Apolipoprotein M (apoM) is predominantly associated with HDL. In this study, it was investigated whether apoM's uncleaved signal peptide is necessary for the protein's ability to associate with lipoproteins. ApoM with a cleavable signal peptide, Q22A, was expressed, together with wild-type apoM, in HEK293 cells. On size-exclusion chromatography, the elution profile of wild-type apoM was similar to that of human HDL-associated plasma apoM. In contrast, the size of the Q22A mutant corresponded to free, unassociated apoM. This strongly indicates that the signal peptide is indeed necessary for apoM's ability to associate with lipid.
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http://dx.doi.org/10.1016/j.febslet.2008.02.007 | DOI Listing |
Rev Cardiovasc Med
January 2025
Department of Cardiology, Gazi University Faculty of Medicine, 06560 Ankara, Turkey.
Background: Hypertension-mediated organ damage (HMOD) is a critical complication of hypertension that can present with cardiac, retinal, and renal manifestations and affect patient outcomes. Serum signal peptide, CUB (complement C1r/C1s, Uegf, and Bmp1) domain, and epidermal growth factor-like domain-containing protein 1 (SCUBE-1), a novel biomarker implicated in vascular pathology, shows promise for detecting HMOD. This study aims to explore the relation between SCUBE-1 levels and HMOD in hypertensive patients.
View Article and Find Full Text PDFAnal Chem
January 2025
Shanghai Key Laboratory of Functional Materials Chemistry, School of Chemistry and Molecular Engineering, East China University of Science and Technology, Meilong Road, Shanghai 200237, P. R. China.
Protein methylation has attracted increasing attention due to its significant regulatory roles in various biological processes. However, the diversity of methylation forms, subtle differences between methylated and nonmodified sites, and their ultralow abundances pose substantial challenges for capturing and isolating methylated peptides from biological samples. Herein, we develop a chromatographic method that utilizes 4-sulfonylcalix[4]arene (SC4A) as a mobile phase additive and Click-Maltose as the stationary phase to separate methylated/nonmethylated peptides through the adsorption of the SC4A-(Me3) complex.
View Article and Find Full Text PDFAnal Chem
January 2025
Department of Laboratory Medicine, Clinical Laboratory Medicine Research Center of West China Hospital, Med+X Center for Manufacturing, Department of Rheumatology & Immunology, National Clinical Research Center for Geriatrics, Department of Gynecology of West China Tianfu Hospital, West China Hospital, Sichuan University, Chengdu, Sichuan 610041, China.
Homogeneous analysis techniques offer several advantages as alternatives to heterogeneous immunoassays, such as simplicity and rapidity. In this study, a visual homogeneous immunoassay without a labeling process was developed based on target-induced steric hindrance to regulate competitive recognition mechanism. Specifically, as the analyte concentration varies, the change of microenvironment based on steric hindrance could affect the recognition of Cu by signal probes.
View Article and Find Full Text PDFJ Biol Chem
January 2025
Department of Biochemistry and Molecular Biotechnology, University of Massachusetts Chan Medical School, Worcester, MA 01605, USA. Electronic address:
Transient protein-protein interactions play key roles in controlling dynamic cellular responses. Many examples involve globular protein domains that bind to peptide sequences known as Short Linear Motifs (SLiMs), which are enriched in intrinsically disordered regions of proteins. Here we describe a novel functional assay for measuring SLiM binding, called Systematic Intracellular Motif Binding Analysis (SIMBA).
View Article and Find Full Text PDFBiosens Bioelectron
January 2025
Department of Chemistry, Kansas State University, Manhattan, KS, 66502, USA. Electronic address:
Proteases are overexpressed at various stages of conditions such as cancers and thus can serve as biomarkers for disease diagnosis. Electrochemical techniques to detect the activity of extracellular proteases have gained attraction due to their multiplexing capability. Here we employ an electrochemical approach based on a 3 × 3 gold (Au) microelectrode array (MEA) functionalized with (2-aminoethyl)ferrocene (AEF) tagged specific peptide substrates to monitor cathepsin B (CB) protease activity.
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