scholarly journals Front Cover: KFP‐1, a Novel Calcium‐Binding Peptide Isolated from Kefir, Promotes Calcium Influx Through TRPV6 Channels

2021 ◽  
Vol 65 (22) ◽  
pp. 2170058
Author(s):  
Gary Ro‐Lin Chang ◽  
Min‐Yu Tu ◽  
Yu‐Hsuan Chen ◽  
Ku‐Yi Chang ◽  
Chien‐Fu Chen ◽  
...  
2021 ◽  
pp. 2100182
Author(s):  
Gary Ro‐Lin Chang ◽  
Min‐Yu Tu ◽  
Yu‐Hsuan Chen ◽  
Ku‐Yi Chang ◽  
Chien‐Fu Chen ◽  
...  

2010 ◽  
Vol 15 (4) ◽  
pp. 282-286 ◽  
Author(s):  
So-Jeong Jeon ◽  
Ji-Hye Lee ◽  
Kyung-Bin Song

1999 ◽  
Vol 82 (6) ◽  
pp. 2936-2946 ◽  
Author(s):  
Mario B. Lips ◽  
Bernhard U. Keller

A quantitative analysis of activity-related calcium dynamics was performed in motoneurons of the nucleus hypoglossus in the brain stem slice preparation from mouse by simultaneous patch-clamp and microfluorometric calcium measurements. Motoneurons were analyzed under in vitro conditions that kept them in a functionally intact state represented by rhythmic, inspiratory-related bursts of excitatory postsynaptic currents and associated action potential discharges. Bursts of electrical activity were paralleled by somatic calcium transients resulting from calcium influx through voltage-activated calcium channels, where each action potential accounted for a calcium-mediated charge influx around 2 pC into the somatic compartment. Under in vivo conditions, rhythmic-respiratory activity in young mice occurred at frequencies up to 5 Hz, demonstrating the necessity for rapid calcium elevation and recovery in respiratory-related neurons. The quantitative analysis of hypoglossal calcium homeostasis identified an average extrusion rate, but an exceptionally low endogenous calcium binding capacity as cellular parameters accounting for rapid calcium signaling. Our results suggest that dynamics of somatic calcium transients 1) define an upper limit for the maximum frequency of respiratory-related burst discharges and 2) represent a potentially dangerous determinant of intracellular calcium profiles during pathophysiological and/or excitotoxic conditions.


ChemCatChem ◽  
2018 ◽  
Vol 10 (3) ◽  
pp. 484-484
Author(s):  
Sarah Zernia ◽  
Ronny Frank ◽  
Renato H.-J. Weiße ◽  
Heinz-Georg Jahnke ◽  
Kathrin Bellmann-Sickert ◽  
...  

2013 ◽  
Vol 14 (7) ◽  
pp. 2347-2353 ◽  
Author(s):  
Wafa Hassouneh ◽  
Michelle L. Nunalee ◽  
M. Coleman Shelton ◽  
Ashutosh Chilkoti

2015 ◽  
Vol 82 (1) ◽  
pp. 29-35 ◽  
Author(s):  
Shun-Li Huang ◽  
Li-Na Zhao ◽  
Xixi Cai ◽  
Shao-Yun Wang ◽  
Yi-Fan Huang ◽  
...  

The bioavailability of dietary ionised calcium is affected by intestinal basic environment. Calcium-binding peptides can form complexes with calcium to improve its absorption and bioavailability. The aim of this study was focused on isolation and characterisation of a calcium-binding peptide from whey protein hydrolysates. Whey protein was hydrolysed using Flavourzyme and Protamex with substrate to enzyme ratio of 25 : 1 (w/w) at 49 °C for 7 h. The calcium-binding peptide was isolated by DEAE anion-exchange chromatography, Sephadex G-25 gel filtration and reversed phase high-performance liquid chromatography (RP-HPLC). A purified peptide of molecular mass 204 Da with strong calcium binding ability was identified on chromatography/electrospray ionisation (LC/ESI) tandem mass spectrum to be Glu-Gly (EG) after analysis and alignment in database. The calcium binding capacity of EG reached 67·81 μg/mg, and the amount increased by 95% compared with whey protein hydrolysate complex. The UV and infrared spectrometer analysis demonstrated that the principal sites of calcium-binding corresponded to the carboxyl groups and carbonyl groups of glutamic acid. In addition, the amino group and peptide amino are also the related groups in the interaction between EG and calcium ion. Meanwhile, the sequestered calcium percentage experiment has proved that EG-Ca is significantly more stable than CaCl2 in human gastrointestinal tract in vitro. The findings suggest that the purified dipeptide has the potential to be used as ion-binding ingredient in dietary supplements.


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