Induction of rat alkaline phosphatase isozymes bearing a glycan-phosphatidylinositol anchor modified by in vivo treatment with a benzimidazole derivative linked to ethylbenzene

2000 ◽  
Vol 127 (2) ◽  
pp. 193-202 ◽  
Author(s):  
Tsuyoshi Harada ◽  
Iwao Koyama ◽  
Kousuke Sato ◽  
Tsugikazu Komoda
Keyword(s):  
Alkaline Phosphatase ◽  
Benzimidazole Derivative ◽  
In Vivo Treatment

Antigenic changes of a murine lymphoma by in vivo treatment with triazene derivatives

1981 ◽  
Vol 11 (4) ◽  
Author(s):  
M.C. Fioretti ◽  
B. Nardelli ◽  
R. Bianchi ◽  
C. Nisi ◽  
G. Sava
Keyword(s):  
Murine Lymphoma ◽  
In Vivo Treatment

The two isozymes of rat intestinal alkaline phosphatase are products of two distinct genes

2000 ◽  
Vol 3 (1) ◽  
pp. 1-8 ◽  
Author(s):  
Q. XIE ◽  
D. H. ALPERS
Keyword(s):  
Alkaline Phosphatase ◽  
Transcriptional Start Site ◽  
In Vivo Studies ◽  
Peroxisome Proliferator ◽  
Start Site ◽  
Intestinal Alkaline Phosphatase ◽  
Promoter Regions ◽  
Flanking Regions

Xie, Q., and D. H. Alpers. The two isozymes of rat intestinal alkaline phosphatase are products of two distinct genes. Physiol Genomics 3: 1–8, 2000.—Rat intestinal alkaline phosphatases (IAP-I and -II) differ in primary structure, substrate specificity, tissue localization, and response to fat feeding. This study identifies two distinct genes (∼5–6 kb) corresponding to each isozyme and containing 11 exons of nearly identical size. The exon-intron junctions are identical with those found in IAP genes from other species. The 1.7 and 1.2 bp of 5′ flanking regions isolated from each gene, respectively, contain Sp1 and gut-enriched Kruppel-like factor (GKLF) binding sites, but otherwise show little identity. There is a potential CAAT-box 14 bp 5′ to the transcriptional start site, 36 bp upstream from IAP-I, and a TATA-box 31 bp 5′ to the transcriptional start site, 55 bp upstream from IAP-II. Transfection of these promoter regions (linked to luciferase as a reporter gene) into a kidney cell line, COS-7, produced the differential response to oleic acid expected from in vivo studies, i.e., threefold increase using the 5′ flanking region of IAP-II, but not IAP-I. This response was not reproduced by 5,8,11,14-eicosatetraynoic acid (ETYA) or clofibrate, suggesting that peroxisome proliferator response elements are not involved. Isolation of the IAP-II gene will allow determination of the sequences responsible for dietary fat response in the enterocyte.

In vivo treatment with nitazoxanide induces anaerobic metabolism in experimental intraperitoneal cysticercosis

2017 ◽  
Vol 116 (11) ◽  
pp. 3037-3041 ◽  
Author(s):  
Joelma M. Nasareth ◽  
Carolina M. Fraga ◽  
Nayana F. Lima ◽  
Guaraciara A. Picanço ◽  
Tatiane L. Costa ◽  
...  
Keyword(s):  
Anaerobic Metabolism ◽  
In Vivo Treatment
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