scholarly journals Enhancement of Intestinal Alkaline Phosphatase Expression by 1,25(OH)2D3 in the Human Intestinal Epithelial-like Cell Line Caco-2

2018 ◽  
Vol 71 (1) ◽  
pp. 21-29
Author(s):  
Seiko Noda ◽  
Asako Yamada ◽  
Kanae Nakaoka ◽  
Masae Goseki-Sone
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Line ◽  
Intestinal Epithelial ◽  
Intestinal Alkaline Phosphatase ◽  
Alkaline Phosphatase Expression

scholarly journals Characterization of human foetal intestinal alkaline phosphatase. Comparison with the isoenzymes from the adult intestine and human tumour cell lines

1983 ◽  
Vol 211 (3) ◽  
pp. 553-558 ◽  
Author(s):  
C M Behrens ◽  
C A Enns ◽  
H H Sussman
Keyword(s):  
Alkaline Phosphatase ◽  
Cell Line ◽  
Tumour Cell ◽  
Tumour Cell Line ◽  
Subunit Structure ◽  
Human Tumour ◽  
Intestinal Alkaline Phosphatase ◽  
Alkaline Phosphatases ◽  
Inhibition Studies

The molecular structure of human foetal intestinal alkaline phosphatase was defined by high-resolution two-dimensional polyacrylamide-gel electrophoresis and amino acid inhibition studies. Comparison was made with the adult form of intestinal alkaline phosphatase, as well as with alkaline phosphatases isolated from cultured foetal amnion cells (FL) and a human tumour cell line (KB). Two non-identical subunits were isolated from the foetal intestinal isoenzyme, one having same molecular weight and isoelectric point as placental alkaline phosphatase, and the other corresponding to a glycosylated subunit of the adult intestinal enzyme. The FL-cell and KB-cell alkaline phosphatases were also found to contain two subunits similar to those of the foetal intestinal isoenzyme. Characterization of neuraminidase digests of the non-placental subunit showed it to be indistinguishable from the subunits of the adult intestinal isoenzyme. This implies that no new phosphatase structural gene is involved in the transition from the expression of foetal to adult intestinal alkaline phosphatase, but that the molecular changes involve suppression of the placental subunit and loss of neuraminic acid from the non-placental subunit. Enzyme-inhibition studies demonstrated an intermediate response to the inhibitors tested for the foetal intestinal, FL-cell and KB-cell isoenzymes when compared with the placental, adult intestinal and liver forms. This result is consistent with the mixed-subunit structure observed for the former set of isoenzymes. In summary, this study has defined the molecular subunit structure of the foetal intestinal form of alkaline phosphatase and has demonstrated its expression in a human tumour cell line.

Differentiation-dependent activation of the human intestinal alkaline phosphatase promoter by HNF-4 in intestinal cells

2005 ◽  
Vol 289 (2) ◽  
pp. G220-G226 ◽  
Author(s):  
Line Olsen ◽  
Simon Bressendorff ◽  
Jesper T. Troelsen ◽  
Jorgen Olsen
Keyword(s):  
Alkaline Phosphatase ◽  
Binding Site ◽  
Promoter Sequence ◽  
Computer Assisted ◽  
Intestinal Epithelial ◽  
Intestinal Alkaline Phosphatase ◽  
Cis Element ◽  
Nuclear Extracts ◽  
Brush Border Enzyme ◽  
Translational Start

The intestinal alkaline phosphatase gene ( ALPI) encodes a digestive brush-border enzyme, which is highly upregulated during small intestinal epithelial cell differentiation. To identify new putative promoter motifs responsible for the regulation of ALPI expression during differentiation of the enterocytes, we have conducted a computer-assisted cis-element search of the proximal human ALPI promoter sequence. A putative recognition site for the transcription factor hepatocyte nuclear factor (HNF)-4 was predicted at the positions from −94 to −82 in relation to the translational start site. The ability of HNF-4α to stimulate the expression from the ALPI promoter was investigated in the nonintestinal Hela cell line. Cotransfection with an HNF-4α expression vector demonstrated a direct activation of the ALPI promoter through this −94 to −82 element. EMSA showed that HNF-4α from nuclear extracts of differentiated intestinal epithelial cells (Caco-2) bound with high affinity to the predicted HNF-4 binding site. A 521 bp promoter fragment containing the HNF-4 binding site demonstrated a differentiation-dependent increase in promoter activity in Caco-2 cells. The presence of the HNF-4 binding site was necessary for this increase to occur.

scholarly journals Early Weaning Reduces Small Intestinal Alkaline Phosphatase Expression in Pigs

2010 ◽  
Vol 140 (3) ◽  
pp. 461-468 ◽  
Author(s):  
Dale Lackeyram ◽  
Chengbo Yang ◽  
Tania Archbold ◽  
Kendall C. Swanson ◽  
Ming Z. Fan
Keyword(s):  
Alkaline Phosphatase ◽  
Early Weaning ◽  
Intestinal Alkaline Phosphatase ◽  
Small Intestinal ◽  
Alkaline Phosphatase Expression

The effect of intestinal alkaline phosphatase on intestinal epithelial cells, macrophages and chronic colitis in mice

Life Sciences ◽  
2014 ◽  
Vol 100 (2) ◽  
pp. 118-124 ◽  
Author(s):  
Changhyun Lee ◽  
Jaeyoung Chun ◽  
Sung Wook Hwang ◽  
Seung Joo Kang ◽  
Jong Pil Im ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Epithelial Cells ◽  
Intestinal Epithelial Cells ◽  
Intestinal Epithelial ◽  
Chronic Colitis ◽  
Intestinal Alkaline Phosphatase

Goblet cells and intestinal Alkaline phosphatase expression (IAP) during the development of the rat small intestine

2017 ◽  
Vol 119 (1) ◽  
pp. 71-77 ◽  
Author(s):  
José Rosa Gomes ◽  
Laís Costa Ayub ◽  
Camila Audrey dos Reis ◽  
Miriam Joice Machado ◽  
Jéssica da Silva ◽  
...  
Keyword(s):  
Alkaline Phosphatase ◽  
Small Intestine ◽  
Goblet Cells ◽  
Rat Small Intestine ◽  
Intestinal Alkaline Phosphatase ◽  
Alkaline Phosphatase Expression
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