We assessed the effects of intracrystalline urinary proteins on the ability of Type II Madin-Darby canine kidney (MDCK-II) cells to bind and degrade calcium oxalate monohydrate (COM) crystals. Binding of [14C]-labelled inorganic crystals (iCOM), and COM crystals precipitated from centrifuged and filtered (CF) or ultrafiltered (UF) human urine was quantified by radioactive analysis. SDS-PAGE confirmed the presence of intracrystalline proteins > 10 kDa in CF crystals and their absence from UF crystals. Morphological effects were assessed qualitatively by field emission scanning electron microscopy. iCOM crystals bound rapidly and extensively and were resistant to degradation. Binding of CF crystals was weaker than UF crystals, and both had markedly less affinity than iCOM. CF and UF crystals were extensively degraded within 90 min, the effect being more pronounced with CF. These results support our hypothesis that intracrystalline proteins protect against urolithiasis by facilitating intracellular proteolytic digestion and destruction of crystals phagocytosed by urothelial cells.
Download full-text PDF |
Source |
|---|---|
| http://dx.doi.org/10.1016/j.jsb.2005.04.005 | DOI Listing |
Publication Analysis
Top Keywords
Similar Publications
Implications of intracrystalline OC17 on the protection of lattice incorporated proteins.
Soft Matter
June 2024
University of Cambridge, Cambridge Institute for Medical Research, Department of Haematology, The Keith Peters Building, Hills Road, CB2 0XY Cambridge, UK.
Biogenic CaCO formation is regulated by crystallization proteins during crystal growth. Interactions of proteins with nascent mineral surfaces trigger proteins to be incorporated into the crystal lattice. As a result of incorporation, these intracrystalline proteins are protected in the lattice, an example of which is ancient eggshell proteins that have persisted in CaCO for thousands of years even under harsh environmental conditions.
View Article and Find Full Text PDFLifeSoaks: a tool for analyzing solvent channels in protein crystals and obstacles for soaking experiments.
Acta Crystallogr D Struct Biol
September 2023
Center for Bioinformatics, Universität Hamburg, Bundesstrasse 43, 20146 Hamburg, Germany.
Due to the structural complexity of proteins, their corresponding crystal arrangements generally contain a significant amount of solvent-occupied space. These areas allow a certain degree of intracrystalline protein flexibility and mobility of solutes. Therefore, knowledge of the geometry of solvent-filled channels and cavities is essential whenever the dynamics inside a crystal are of interest.
View Article and Find Full Text PDFDiffusion Coefficient of Intracrystalline Water in Intrinsic Hen Egg-White Lysozyme Crystals Determined by Confocal Raman Spectroscopy.
J Phys Chem B
November 2022
Graduate School of Nanobioscience, Yokohama City University, 22-2 Seto, Kanazawa-ku, Yokohama236-0027, Japan.
Protein crystals composed of protein molecules are expected as a novel porous material. They have high porosity, and the knowledge of the diffusion of intracrystalline water is important. In this study, the diffusion coefficient of intracrystalline water in intrinsic hen egg-white lysozyme (HEWL) crystals was determined by a method that combines confocal Raman spectroscopy and air convection with controlled relative humidity.
View Article and Find Full Text PDFDipeptidyl peptidase 9 triggers BRCA2 degradation and promotes DNA damage repair.
EMBO Rep
October 2022
Institute of Molecular Medicine and Cell Research, Medical Faculty, University of Freiburg, Freiburg, Germany.
N-terminal sequences are important sites for post-translational modifications that alter protein localization, activity, and stability. Dipeptidyl peptidase 9 (DPP9) is a serine aminopeptidase with the rare ability to cleave off N-terminal dipeptides with imino acid proline in the second position. Here, we identify the tumor-suppressor BRCA2 as a DPP9 substrate and show this interaction to be induced by DNA damage.
View Article and Find Full Text PDFBiogeochemical fingerprinting of magnetotactic bacterial magnetite.
Proc Natl Acad Sci U S A
August 2022
School of Life Sciences, University of Nevada at Las Vegas, Las Vegas, NV 89154-4004.
Biominerals are important archives of the presence of life and environmental processes in the geological record. However, ascribing a clear biogenic nature to minerals with nanometer-sized dimensions has proven challenging. Identifying hallmark features of biologically controlled mineralization is particularly important for the case of magnetite crystals, resembling those produced by magnetotactic bacteria (MTB), which have been used as evidence of early prokaryotic life on Earth and in meteorites.
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!