scholarly journals Time-Dependent ATR-FTIR Spectroscopic Studies on Fatty Acid Diffusion and the Formation of Metal Soaps in Oil Paint Model Systems

2018 ◽  
Vol 57 (25) ◽  
pp. 7351-7354 ◽  
Author(s):  
Lambert Baij ◽  
Joen J. Hermans ◽  
Katrien Keune ◽  
Piet Iedema
2018 ◽  
Vol 130 (25) ◽  
pp. 7473-7476 ◽  
Author(s):  
Lambert Baij ◽  
Joen J. Hermans ◽  
Katrien Keune ◽  
Piet Iedema

2018 ◽  
Vol 51 (18) ◽  
pp. 7419-7419
Author(s):  
Lambert Baij ◽  
Joen J. Hermans ◽  
Katrien Keune ◽  
Piet D. Iedema

2018 ◽  
Vol 51 (18) ◽  
pp. 7134-7144 ◽  
Author(s):  
Lambert Baij ◽  
Joen J. Hermans ◽  
Katrien Keune ◽  
Piet D. Iedema

1997 ◽  
Vol 38 (2) ◽  
pp. 361-372
Author(s):  
M Fernández-García ◽  
M V García ◽  
M I Redondo ◽  
J A Cheda ◽  
M Fernández-García ◽  
...  

1978 ◽  
Vol 17 (1) ◽  
pp. 455-470 ◽  
Author(s):  
Kyozi Kawasaki ◽  
Mehmet C. Yalabik ◽  
J. D. Gunton

2017 ◽  
Vol 113 ◽  
pp. 198-212 ◽  
Author(s):  
Priscila M. Florido ◽  
Deborah P.S. Lobo ◽  
Camila N. Pinto ◽  
Christianne E.C. Rodrigues ◽  
Cintia B. Gonçalves

Cells ◽  
2021 ◽  
Vol 10 (9) ◽  
pp. 2248
Author(s):  
Marija Aleksic ◽  
Igor Golic ◽  
Andjelika Kalezic ◽  
Aleksandra Jankovic ◽  
Bato Korac ◽  
...  

Despite peroxisomes being important partners of mitochondria by carrying out fatty acid oxidation in brown adipocytes, no clear evidence concerning peroxisome origin and way(s) of biogenesis exists. Herein we used methimazole-induced hypothyroidism for 7, 15, and 21 days to study peroxisomal remodeling and origin in rat brown adipocytes. We found that peroxisomes originated via both canonic, and de novo pathways. Each pathway operates in euthyroid control and over the course of hypothyroidism, in a time-dependent manner. Hypothyroidism increased the peroxisomal number by 1.8-, 3.6- and 5.8-fold on days 7, 15, and 21. Peroxisomal presence, their distribution, and their degree of maturation were heterogeneous in brown adipocytes in a Harlequin-like manner, reflecting differences in their origin. The canonic pathway, through numerous dumbbell-like and “pearls on strings” structures, supported by high levels of Pex11β and Drp1, prevailed on day 7. The de novo pathway of peroxisomal biogenesis started on day 15 and became dominant by day 21. The transition of peroxisomal biogenesis from canonic to the de novo pathway was driven by increased levels of Pex19, PMP70, Pex5S, and Pex26 and characterized by numerous tubular structures. Furthermore, specific peroxisomal origin from mitochondria, regardless of thyroid status, indicates their mutual regulation in rat brown adipocytes.


1987 ◽  
Vol 243 (2) ◽  
pp. 405-412 ◽  
Author(s):  
T W Stephens ◽  
R A Harris

The sensitivity of carnitine palmitoyltransferase I to inhibition by 4-hydroxyphenylglyoxylate was decreased markedly in liver mitochondria isolated from either 48 h-starved or streptozotocin-diabetic rats. These treatments of the rat also decreased the sensitivity of fatty acid oxidation by isolated hepatocytes to inhibition by this compound. Furthermore, incubation of hepatocytes prepared from fed rats with N6O2′-dibutyryl cyclic AMP also decreased the sensitivity, whereas incubation of hepatocytes prepared from starved rats with lactate plus pyruvate had the opposite effect on 4-hydroxyphenylglyoxylate inhibition of fatty acid oxidation. The sensitivity of carnitine palmitoyltransferase I of mitochondria to 4-hydroxyphenylglyoxylate increased in a time-dependent manner, as previously reported for malonyl-CoA. Likewise, oleoyl-CoA activated carnitine palmitoyltransferase I in a time-dependent manner and prevented the sensitization by 4-hydroxyphenylglyoxylate. Increased exogenous carnitine caused a moderate increase in fatty acid oxidation by hepatocytes under some conditions and a decreased 4-hydroxyphenylglyoxylate inhibition of fatty acid oxidation at low oleate concentration, without decreasing the difference in 4-hydroxyphenylglyoxylate inhibition between fed- and starved-rat hepatocytes. Time-dependent changes in the conformation of carnitine palmitoyltransferase I or the membrane environment may be involved in differences among nutritional states in 4-hydroxyphenylglyoxylate-sensitivity of carnitine palmitoyltransferase I.


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