Formation of calcium phosphate nanoparticles mediated by animal protein hydrolysates enhances calcium absorption by murine small intestine ex vivo

2019 ◽  
Vol 10 (10) ◽  
pp. 6666-6674 ◽  
Author(s):  
Yisheng Yang ◽  
Suqin Zhu ◽  
Wei Guo ◽  
Yinong Feng ◽  
Tengjiao Guo ◽  
...  

Animal protein intake appears to deliver available nanosized calcium to intestine.

2016 ◽  
Vol 474 (1) ◽  
pp. 161-167 ◽  
Author(s):  
Takeshi Tsuruta ◽  
Shinichi Saito ◽  
Yosuke Osaki ◽  
Akihiro Hamada ◽  
Ayako Aoki-Yoshida ◽  
...  

2001 ◽  
Vol 281 (3) ◽  
pp. G697-G704 ◽  
Author(s):  
David A. Groneberg ◽  
Frank Döring ◽  
Paul R. Eynott ◽  
Axel Fischer ◽  
Hannelore Daniel

The nature of protein breakdown products and peptidomimetic drugs such as β-lactams is crucial for their transmembrane transport across apical enterocyte membranes, which is accomplished by the pH-dependent high-capacity oligopeptide transporter PEPT1. To visualize oligopeptide transporter-mediated uptake of oligopeptides, an ex vivo assay using the fluorophore-conjugated dipeptide derivatived-Ala-Lys- N ε-7-amino-4-methylcoumarin-3-acetic acid (d-Ala-Lys-AMCA) was established in the murine small intestine and compared with immunohistochemistry for PEPT1 in murine and human small intestine. d-Ala-Lys-AMCA was accumulated by enterocytes throughout all segments of the murine small intestine, with decreasing intensity from the top to the base of the villi. Goblet cells did not show specific uptake. Inhibition studies revealed competitive inhibition by the β-lactam cefadroxil, the angiotensin-converting enzyme inhibitor captopril, and the dipeptide glycyl-glutamine. Controls were performed using either the inhibitor diethylpyrocarbonate or an incubation temperature of 4°C to exclude unspecific uptake. Immunohistochemistry for PEPT1 localized immunoreactivity to the enterocytes, with the highest intensity at the apical membrane. This is the first study that visualizes dipeptide transport across the mammalian intestine and indicates that uptake assays using d-Ala-Lys-AMCA might be useful for characterizing PEPT1-specific substrates or inhibitors.


2001 ◽  
Vol 120 (5) ◽  
pp. A660-A660
Author(s):  
D MCMICHAEL ◽  
A DAVIES ◽  
E MARSHMAN ◽  
P OTTEWELL ◽  
J JENKINS ◽  
...  

2017 ◽  
Author(s):  
J Houriet ◽  
YE Arnold ◽  
C Petit ◽  
YN Kalia ◽  
JL Wolfender

2014 ◽  
Vol 70 (a1) ◽  
pp. C67-C67
Author(s):  
Babak Mostaghaci ◽  
Brigitta Loretz ◽  
Robert Haberkorn ◽  
Guido Kickelbick ◽  
Claus-Michael Lehr

Calcium phosphate has been the point of interest for in vitro gene delivery for many years because of its biocompatibility and straight forward application. However, there are some limitations regarding in vivo administration of these particles mostly because of vast agglomeration of the particles and lack of strong bond between the particles and pDNA. We introduced a simple single step method to functionalize calcium phosphate nanoparticles with Aminosilanes having a different number of amine groups. The nanoparticles were characterized chemically and structurally and their toxicity and interaction with pDNA were studied as well. Results revealed that different crystalline phase of calcium phosphate nanoparticles (Brushite and Hydroxyapatite) with a size below 150 nm were prepared, depending on conditions of synthesis and phase, each with a narrow size distribution. The aminosilane agents caused oriented nucleation and growth of crystallites and can decrease the pH for producing hydroxyapatite phase. The phenomenon could be revealed with the presence of anisotropy in the structure of synthesized hydroxyapatite. The number of amine groups in the Aminosilane agent could change the phase transition pH. Brushite particles revealed to have stronger interaction with pDNA mostly because of their higher positive surface charge. Both particles showed blood compatibility and negligible toxicity. Transfection experiment revealed the capability of both brushite and hydroxyapatite particles to transfect A549 and HEK293 cells. The new modified nanoparticles can be stored in a dried state and re-dispersed easily at the time of administration. Moreover, the transfection efficiency is higher in comparison with conventional calcium phosphate. This study showed the impact of presence and type of the modifying agent on the crystal structure and the amount of surface functionalization of nanoparticles, which in consequence influenced their interaction with cells.


2004 ◽  
Vol 14 (14) ◽  
pp. 2213 ◽  
Author(s):  
T. Welzel ◽  
I. Radtke ◽  
W. Meyer-Zaika ◽  
R. Heumann ◽  
M. Epple

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