Phosphorylation and subcellular localization of Na+/H+ exchanger isoform 3 (NHE3) are associated with altered gallbladder absorptive function after formation of cholesterol gallstones

2016 ◽  
Vol 73 (1) ◽  
pp. 133-139 ◽  
Author(s):  
Yongsheng Chen ◽  
Shuodong Wu ◽  
Yu Tian ◽  
Jing Kong
Author(s):  
T. Kanetaka ◽  
M. Cho ◽  
S. Kawamura ◽  
T. Sado ◽  
K. Hara

The authors have investigated the dissolution process of human cholesterol gallstones using a scanning electron microscope(SEM). This study was carried out by comparing control gallstones incubated in beagle bile with gallstones obtained from patients who were treated with chenodeoxycholic acid(CDCA).The cholesterol gallstones for this study were obtained from 14 patients. Three control patients were treated without CDCA and eleven patients were treated with CDCA 300-600 mg/day for periods ranging from four to twenty five months. It was confirmed through chemical analysis that these gallstones contained more than 80% cholesterol in both the outer surface and the core.The specimen were obtained from the outer surface and the core of the gallstones. Each specimen was attached to alminum sheet and coated with carbon to 100Å thickness. The SEM observation was made by Hitachi S-550 with 20 kV acceleration voltage and with 60-20, 000X magnification.


Author(s):  
Howard S. Kaufman ◽  
Keith D. Lillemoe ◽  
John T. Mastovich ◽  
Henry A. Pitt

Gallstones contain precipitated cholesterol, calcium salts, and proteins. Calcium (Ca) bilirubinate, palmitate, phosphate, and carbonate occurring in gallstones have variable morphologies but characteristic windowless energy dispersive x-ray (EDX) spectra. Previous studies of gallstone microstructure and composition using scanning electron microscopy (SEM) with EDX have been limited to dehydrated samples. In this state, Ca bilirubinates appear as either glassy masses, which predominate in black pigment stones, or as clusters, which are found mostly in cholesterol gallstones. The three polymorphs of Ca carbonate, calcite, vaterite, and aragonite, have been identified in gallstones by x-ray diffraction, however; the morphologies of these crystals vary in the literature. The purpose of this experiment was to study fresh gallstones by environmental SEM (ESEM) to determine if dehydration affects gallstone Ca salt morphology.Gallstones and bile were obtained fresh at cholecystectomy from 6 patients. To prevent dehydration, stones were stored in bile at 37°C. All samples were studied within 4 days of procurement.


2019 ◽  
Vol 476 (21) ◽  
pp. 3281-3293 ◽  
Author(s):  
Elodie Lebredonchel ◽  
Marine Houdou ◽  
Hans-Heinrich Hoffmann ◽  
Kateryna Kondratska ◽  
Marie-Ange Krzewinski ◽  
...  

TMEM165 was highlighted in 2012 as the first member of the Uncharacterized Protein Family 0016 (UPF0016) related to human glycosylation diseases. Defects in TMEM165 are associated with strong Golgi glycosylation abnormalities. Our previous work has shown that TMEM165 rapidly degrades with supraphysiological manganese supplementation. In this paper, we establish a functional link between TMEM165 and SPCA1, the Golgi Ca2+/Mn2+ P-type ATPase pump. A nearly complete loss of TMEM165 was observed in SPCA1-deficient Hap1 cells. We demonstrate that TMEM165 was constitutively degraded in lysosomes in the absence of SPCA1. Complementation studies showed that TMEM165 abundance was directly dependent on SPCA1's function and more specifically its capacity to pump Mn2+ from the cytosol into the Golgi lumen. Among SPCA1 mutants that differentially impair Mn2+ and Ca2+ transport, only the Q747A mutant that favors Mn2+ pumping rescues the abundance and Golgi subcellular localization of TMEM165. Interestingly, the overexpression of SERCA2b also rescues the expression of TMEM165. Finally, this paper highlights that TMEM165 expression is linked to the function of SPCA1.


2001 ◽  
Vol 120 (5) ◽  
pp. A550-A550
Author(s):  
H HYOGO ◽  
N RANGINANI ◽  
B PAIGEN ◽  
D COHEN

Diabetes ◽  
1992 ◽  
Vol 41 (2) ◽  
pp. 215-221 ◽  
Author(s):  
A. Bornemann ◽  
T. Ploug ◽  
H. Schmalbruch

2019 ◽  
Author(s):  
Zacharias Thiel ◽  
Pablo Rivera-Fuentes

Many biomacromolecules are known to cluster in microdomains with specific subcellular localization. In the case of enzymes, this clustering greatly defines their biological functions. Nitroreductases are enzymes capable of reducing nitro groups to amines and play a role in detoxification and pro-drug activation. Although nitroreductase activity has been detected in mammalian cells, the subcellular localization of this activity remains incompletely characterized. Here, we report a fluorescent probe that enables super-resolved imaging of pools of nitroreductase activity within mitochondria. This probe is activated sequentially by nitroreductases and light to give a photo-crosslinked adduct of active enzymes. In combination with a general photoactivatable marker of mitochondria, we performed two-color, threedimensional, single-molecule localization microscopy. These experiments allowed us to image the sub-mitochondrial organization of microdomains of nitroreductase activity.<br>


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