Protein-mineral interaction is known to regulate biomineral stability and morphology. We hypothesise that fluid phases produce highly dynamic protein-mineral complexes involved in physiology and pathology of biomineralisation. Here, we specifically focus on calciprotein particles, complexes of vertebrate mineral-binding proteins and calcium phosphate present in the systemic circulation and abundant in extracellular fluids - hence the designation of the ensuing protein-mineral complexes as "mud in the blood". These complexes exist amongst other extracellular particles that we collectively refer to as "the particle zoo".
Download full-text PDF |
Source |
---|---|
http://dx.doi.org/10.1016/j.jsb.2020.107577 | DOI Listing |
Food Res Int
June 2024
Department of Food Technology and Nutrition, Lovely Professional University, Phagwara, Punjab 144411, India. Electronic address:
The research aimed to evaluate the effect of ultrasonication and succinylation on the functional, iron binding, physiochemical, and cellular mineral uptake efficacy of chickpea protein concentrate. Succinylation resulted in significant improvements in the water-holding capacity (WHC) (25.47 %), oil-holding capacity (OHC) (31.
View Article and Find Full Text PDFFoods
October 2023
CARAH ASBL, Rue Pal Pastur 11, 7800 Ath, Belgium.
Minerals play an important role in maintaining human health as the deficiency of these minerals can lead to serious health issues. To address these deficiencies, current research efforts are actively investigating the utilization of protein-mineral complexes as eco-friendly, non-hazardous, suitable mineral fortifiers, characterized by minimal toxicity, for incorporation into food products. Thus, we reviewed the current challenges in incorporating the cereal-legume protein-inorganic minerals complexes' structure, binding properties, and toxicity during fortification on human health.
View Article and Find Full Text PDFKidney Int
April 2023
Department of Physiology and Pathophysiology, Johannes Kepler University Linz, Linz, Austria; Department of Nephrology, Lindenhofspital, Bern, Switzerland. Electronic address:
Protein mineral complexes, or calciprotein particles, are formed by calcium, phosphate, and the plasma protein fetuin-A. Crystalline calciprotein particles cause soft tissue calcification, oxidative stress, and inflammation, all well-known complications in chronic kidney disease. The T50 calcification propensity test measures how long it takes for amorphous calciprotein particles to crystallize.
View Article and Find Full Text PDFJ Struct Biol
December 2021
Texas A&M College of Dentistry Center for Craniofacial Research and Diagnosis, United States. Electronic address:
During enamel formation, the organic enamel protein matrix interacts with calcium phosphate minerals to form elongated, parallel, and bundled enamel apatite crystals of extraordinary hardness and biomechanical resilience. The enamel protein matrix consists of unique enamel proteins such as amelogenin, ameloblastin, and enamelin, which are secreted by highly specialized cells called ameloblasts. The ameloblasts also facilitate calcium and phosphate ion transport toward the enamel layer.
View Article and Find Full Text PDFJ Struct Biol
October 2020
Department of Nephrology, The Royal Melbourne Hospital, Melbourne, Australia; Department of Medicine, University of Melbourne, Parkville, Australia.
Protein-mineral interaction is known to regulate biomineral stability and morphology. We hypothesise that fluid phases produce highly dynamic protein-mineral complexes involved in physiology and pathology of biomineralisation. Here, we specifically focus on calciprotein particles, complexes of vertebrate mineral-binding proteins and calcium phosphate present in the systemic circulation and abundant in extracellular fluids - hence the designation of the ensuing protein-mineral complexes as "mud in the blood".
View Article and Find Full Text PDFEnter search terms and have AI summaries delivered each week - change queries or unsubscribe any time!