Related Experiment Video
Updated: Jun 12, 2026

07:45
Estimation of Urinary Nanocrystals in Humans using Calcium Fluorophore Labeling and Nanoparticle Tracking Analysis
Published on: February 9, 2021
Proteome changes in human monocytes upon interaction with calcium oxalate monohydrate crystals
Nilubon Singhto1, Kitisak Sintiprungrat, Supachok Sinchaikul
1Medical Proteomics Unit, Office for Research and Development, Faculty of Medicine Siriraj Hospital, Mahidol University, Bangkok, Thailand.
Journal of Proteome Research
|June 10, 2010
Summary
Calcium oxalate crystals alter monocyte proteomes, affecting cell cycle and metabolism. This interaction may drive kidney stone disease inflammation via oxidative stress pathways.
Area of Science:
- Nephrology
- Immunology
- Proteomics
Background:
- Monocytes infiltrate kidneys around calcium oxalate (CaOx) deposits.
- Monocytes are thought to clear these crystals, but their response to CaOx is unknown.
Purpose of the Study:
- Investigate the proteomic changes in human monocytes upon interaction with calcium oxalate monohydrate (COM) crystals.
Main Methods:
- U937 human monocyte cells were cultured with or without COM crystals.
- Proteomic analysis was performed using 2D-gel electrophoresis (2-DE) and mass spectrometry (Q-TOF MS/MS).
- Differential protein expression was confirmed by Western blot.
Main Results:
- 22 differentially expressed proteins were identified (9 up-regulated, 13 down-regulated).
- Affected proteins are involved in cell cycle, cellular structure, metabolism, and protein processing.
- Confirmed changes include up-regulation of Alix and EF-2, and down-regulation of beta-actin.
Conclusions:
- COM crystal interaction significantly alters the monocyte proteome.
- These alterations may contribute to kidney stone disease pathogenesis through inflammatory pathways and oxidative stress.
Related Concept Videos
Calmodulin-dependent Signaling
Calmodulin (CaM) is a calcium-binding protein in eukaryotes that controls various calcium-regulated cellular processes. It has four calcium-binding sites that bind calcium to form the calcium-calmodulin ( Ca2+-CaM) complex. GPCR stimulation increases the calcium levels in the cells that bind to CaM and induces a conformational change.
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
The Ca2+-CaM complex does not have enzymatic activity by itself. Instead, the complex binds downstream target proteins, including membrane proteins or enzymes,...
Feedback Regulation of Calcium Concentration
Calcium is an essential signaling molecule required for various cellular functions. Calcium pumps and ion channels on cell and organellar membranes, such as those on the endoplasmic reticulum (ER), regulate calcium concentrations inside the cell. They remain closed, keeping the cytosolic calcium levels low at a resting state.
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Various transmembrane receptors, such as G protein-coupled receptors (GPCRs), elicit a response to extracellular signals by increasing cytosolic calcium. Activated GPCRs...
Skeleton and Calcium Homeostasis
Calcium is not only the most abundant mineral in bone but also the most abundant mineral in the human body. Calcium ions are needed for bone mineralization, tooth health, heart rate regulation and strength of contraction, blood coagulation, the contraction of smooth and skeletal muscle cells, and the regulation of nerve impulse conduction. The average calcium level in the blood is about 10 mg/dL. When the body cannot maintain this level, a person will experience hypo or hypercalcemia.

