scholarly journals Studies of dihydroxyacetone phosphate acyltransferase in rat small intestine. Subcellular localization and effect of partially hydrogenated fish oil and clofibrate

1992 ◽  
Vol 282 (2) ◽  
pp. 565-570 ◽  
Author(s):  
B Ruyter ◽  
J S Lund ◽  
M S Thomassen ◽  
E N Christiansen

The subcellular localization of dihydroxyacetone phosphate acyltransferase (DHAPAT) activity in rat small intestine was investigated by Nycodenz-gradient centrifugation. We found that DHAPAT had a predominant peroxisomal distribution, with a separate enzyme activity located in the microsomal fraction, the same distribution as found in rat liver. The effect of feeding rats on a diet with 20% (w/w) partially hydrogenated fish oil (PHFO) or 0.3% clofibrate on the activity of DHAPAT in rat small intestine and liver was studied. Both 20% PHFO and 0.3% clofibrate gave a 1.8-fold stimulation of the specific activities of DHAPAT in peroxisomes of the small intestine, whereas in the liver 20% PHFO gave a 1.4-fold stimulation and 0.3% clofibrate a 1.6-fold stimulation of the total DHAPAT activities in the postnuclear supernatant. The specific activities of DHAPAT in liver were not affected.

1990 ◽  
Vol 34 (1) ◽  
pp. 13-20 ◽  
Author(s):  
Magny S. Thomassen ◽  
Torill Rørtveit ◽  
Astrid Nilsson ◽  
Kristian Prydz ◽  
Erling N. Christiansen

1982 ◽  
Vol 71 (1) ◽  
pp. 103-107 ◽  
Author(s):  
F. C. PATRA ◽  
D. MAHALANABIS ◽  
K. N. JALAN

1994 ◽  
Vol 267 (4) ◽  
pp. G584-G594 ◽  
Author(s):  
S. D. Krasinski ◽  
G. Estrada ◽  
K. Y. Yeh ◽  
M. Yeh ◽  
P. G. Traber ◽  
...  

Lactase-phlorizin hydrolase (LPH) and sucrase-isomaltase (SI) are intestine-specific microvillus membrane hydrolases whose specific activities demonstrate reciprocal regulation during development but whose mechanisms of regulation have not been fully defined. To investigate transcriptional control of these two proteins, the rat LPH and SI genes were cloned, and antisense probes for preprocessed mRNAs (pre-mRNAs) were developed from intron sequence. LPH mRNA, as measured by quantitative ribonuclease (RNase) protection assays, was abundant before weaning and decreased two- to fourfold during weaning, whereas SI mRNA was first detected 14 days after birth and increased rapidly to abundant levels by age 28 days. LPH and SI pre-mRNA levels paralleled those of their respective mRNAs. LPH transcriptional rate declined during weaning, whereas that of SI increased during this time as determined by RNase protection assays of pre-mRNAs and nuclear run-on assays. In the adult rat, LPH mRNA was restricted to the jejunum and proximal ileum, whereas SI mRNA was detected throughout the small intestine, a pattern regulated by transcriptional rate as confirmed by nuclear run-on assays. Lactase and sucrase specific activities correlated well with their respective protein and mRNA concentrations in all experiments. We conclude that gene transcription plays a major role in the developmental and horizontal regulation of LPH and SI biosynthesis and that these two genes are regulated differently in rat small intestine.


Endocrinology ◽  
1985 ◽  
Vol 116 (3) ◽  
pp. 1133-1138 ◽  
Author(s):  
C. F. FERRIS ◽  
M. J. ARMSTRONG ◽  
J. K. GEORGE ◽  
C. A. STEVENS ◽  
R. E. CARRAWAY ◽  
...  

2001 ◽  
Vol 120 (5) ◽  
pp. A226-A226
Author(s):  
R FRASER ◽  
C FRISBY ◽  
M SCHIRMER ◽  
A BLACKSHAW ◽  
E YEOH

2001 ◽  
Vol 120 (5) ◽  
pp. A226
Author(s):  
Robert Fraser ◽  
Claudine Frisby ◽  
Murray Schirmer ◽  
Ashley Blackshaw ◽  
Eric K. Yeoh

1987 ◽  
Vol 244 (2) ◽  
pp. 443-448 ◽  
Author(s):  
B N Patel ◽  
M I Mackness ◽  
M J Connock

1. The subcellular localization of dihydroxyacetone-phosphate acyltransferase (DHAPAT) (assayed in the presence of pyrophosphate) and glucose-6-phosphate dehydrogenase (NADP+-dependent) activity in mouse kidney was investigated by density-gradient centrifugation. 2. DHAPAT has a predominantly peroxisomal distribution, and the activity in purified peroxisomes is stimulated by various organic and inorganic phosphate-containing compounds. The pH optimum is acid. 3. Approx. 10% of the cellular NADP+-dependent glucose-6-phosphate dehydrogenase activity is associated with peroxisomal fractions and may provide a source of NADPH for the peroxisomal reduction of acyl-dihydroxyacetone phosphate formed by DHAPAT activity.


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