The detection of ANCA (anti-neutrophil cytoplasmic antibodies) is of importance in the diagnosis of Wegener's granulomatosis (WG) and solid-phase assays for the detection of c-ANCA have been set up by various groups, using purified proteinase-3 (PR-3) in an ELISA or RIA. For the isolation of PR-3 large numbers of PMNs are needed. We therefore examined the possibility of isolating PR-3 from the purulent sputum of patients with chronic bronchitis or cystic fibrosis, since large numbers of PMNs and their degranulation products are present in such material. By a three-step chromatographic procedure (4-phenylbutylamine affinity chromatography, Biorex 70 cation exchange chromatography and monoclonal antibody anti-PR-3 affinity chromatography) we isolated a 53 kDa protein that was recognized on immunoblot by MoAbs directed against PR-3 and alpha 1-antitrypsin (alpha 1AT). We show that the 53 kDa protein is a complex of PR-3 and alpha 1AT. This complex is reactive with a selected set of c-ANCA positive sera from patients with Wegener's granulomatosis.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/0022-1759(93)90142-t | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Targeting Ribosome Biogenesis for Cancer Therapy with Oral Platinum Complexes.
JACS Au
January 2025
School of Chemistry and Chemical Engineering, Chemistry and Biomedicine Innovation Center (ChemBIC), State Key Laboratory of Coordination Chemistry, Najing University, Nanjing 210023, PR China.
Cancer cells often upregulate ribosome biogenesis to meet increased protein synthesis demands for rapid proliferation; therefore, targeting ribosome biogenesis has emerged as a promising cancer therapeutic strategy. Herein, we introduce two Pt complexes, ataluren monosubstituted platinum(IV) (SPA, formula: c,c,t,-[Pt(NH)Cl(OH)(CHFNO)], where CHFNO = ataluren) and ataluren bisubstituted platinum(IV) complex (DPA, formula: c,c,t,-[Pt(NH)Cl(CHFNO)], where CHFNO = ataluren), which effectively suppress ribosome biogenesis by inhibiting 47s pre-RNA expression. Furthermore, SPA and DPA induce nucleolar stress by dispersing nucleolar protein NPM1, ultimately inhibiting protein generation in tumor cells.
View Article and Find Full Text PDFSMAP3-ID for Identification of Endogenous Protein-Protein Interactions Reveals Regulation of Mitochondrial Activity by Lamins.
JACS Au
January 2025
Program in Chemical Biology, Department of Chemical Physiology and Biochemistry, Proteomics Shared Resources, Knight Cancer Institute, Department of Neurology, Oregon Health & Science University, 3181 SW Sam Jackson Park Rd, Portland, Oregon 97239, United States.
Proteins regulate biological functions through the formation of distinct protein complexes. Identification and characterization of these protein-protein interactions are critical to deciphering their mechanism of action. Different antibody-based or cross-linking-based methods have been developed to identify the protein-protein interactions.
View Article and Find Full Text PDFSingle-Virus Microscopy of Biochemical Events in Viral Entry.
JACS Au
January 2025
Department of Biomedical Engineering, University of Virginia, Box 800759, Charlottesville, Virginia 22908, United States.
Cell entry by enveloped viruses involves a set of multistep, multivalent interactions between viral and host proteins as well as manipulation of nanoscale membrane mechanics by these interacting partners. A mechanistic understanding of these events has been challenging due to the complex nature of the interactions and the event-to-event heterogeneity involved. Single-virus microscopy has emerged as a powerful technique to probe viral binding and fusion kinetics.
View Article and Find Full Text PDFNative Mass Spectrometry Captures the Conformational Plasticity of Proteins with Low-Complexity Domains.
JACS Au
January 2025
Department of Cell and Molecular Biology, Uppsala University, 751 24 Uppsala, Sweden.
Disordered regions are an important functional feature of many multidomain proteins. A prime example is proteins in membraneless organelles, which contain folded domains that engage in specific interactions and disordered low-complexity (LC) domains that mediate liquid-liquid phase separation. Studying these complex architectures remains challenging due to their conformational variability.
View Article and Find Full Text PDFMolecular Basis for Short-Chain Thioester Hydrolysis by Acyl Hydrolases in -Acyltransferase Polyketide Synthases.
JACS Au
January 2025
Department of Chemistry, University of Warwick, Coventry CV4 7AL, U.K.
Polyketide synthases (PKSs) are multidomain enzymatic assembly lines that biosynthesize a wide selection of bioactive natural products from simple building blocks. In contrast to their -acyltransferase (AT) counterparts, -AT PKSs rely on stand-alone ATs to load extender units onto acyl carrier protein (ACP) domains embedded in the core PKS machinery. -AT PKS gene clusters also encode stand-alone acyl hydrolases (AHs), which are predicted to share the overall fold of ATs but function like type II thioesterases (TEs), hydrolyzing aberrant acyl chains from ACP domains to promote biosynthetic efficiency.
View Article and Find Full Text PDFWant AI Summaries of new PubMed Abstracts delivered to your In-box?
Enter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!