TYROSINE KINASE INHIBITORS REVERSE BUTYRATE STIMULATION OF HUMAN CACO-2 INTESTINAL EPITHELIAL CELL ALKALINE PHOSPHATASE BUT NOT BUTYRATE PROMOTION OF DIPEPTIDYL DIPEPTIDASE

1998 ◽  
Vol 22 (5) ◽  
pp. 339-344 ◽  
Author(s):  
M BASSON
2015 ◽  
Vol 195 (10) ◽  
pp. 5011-5024 ◽  
Author(s):  
Eva Hainzl ◽  
Silvia Stockinger ◽  
Isabella Rauch ◽  
Susanne Heider ◽  
David Berry ◽  
...  

1999 ◽  
Vol 77 (2) ◽  
pp. 138-142 ◽  
Author(s):  
Tamas Zakar ◽  
Jane E Mijovic ◽  
Damyanti Bhardwaj ◽  
David M Olson

Human amnion cells in primary culture respond to glucocorticoids in a characteristic fashion by the increased expression of the inducible prostaglandin endoperoxide H synthase isoenzyme, PGHS-2. Since PGHS-2 induction by agonists generally involves tyrosine kinases, we examined the possibility that the glucocorticoid stimulation of PGHS-2 in the amnion cells is tyrosine kinase dependent. PGHS-2 expression was stimulated in confluent, serum-starved amnion cells with dexamethasone, and the effect of the tyrosine kinase inhibitors herbimycin A and tyrphostins AG126, AG1288, and A1 on enzyme activity induction was determined. All four inhibitors blocked the increase of PGHS activity in a concentration-dependent manner with IC50 values of 0.077 ± 0.05, 15.38 ± 5.14, 20.91 ± 3.1, and 29.77 ± 8.21 µM, respectively (mean ± SE, n = 4). Dexamethasone increased (approximately twofold) the tyrosine phosphorylation of 120-, 110-, and 77-kDa proteins in cell extracts, and herbimycin A selectively blocked the phosphorylation of the 110-kDa phosphoprotein. The stimulation of the steady-state level of PGHS-2 mRNA by dexamethasone was also inhibited by herbimycin A. These results suggest that glucocorticoids induce PGHS-2 expression in amnion cells with the involvement of tyrosine kinase(s). The role of tyrosine kinase dependent mechanisms in the control of amnion cell responsiveness to corticosteroids remains to be established.Key words: amnion, glucocorticoid, tyrosine kinase, prostaglandin H synthase.


FEBS Letters ◽  
1999 ◽  
Vol 444 (2-3) ◽  
pp. 173-176 ◽  
Author(s):  
Takaki Hiwasa ◽  
Yoshiko Arase ◽  
Zheng Chen ◽  
Kazuko Kita ◽  
Kazuo Umezawa ◽  
...  

1999 ◽  
Vol 276 (6) ◽  
pp. C1245-C1258 ◽  
Author(s):  
Jean Q. Tian ◽  
Andrea Quaroni

Using the conditionally immortalized human cell line tsFHI, we have investigated the role of cyclin-dependent kinase inhibitors (CKIs) in intestinal epithelial cell differentiation. Expression of cyclins, cyclin-dependent kinases (Cdk), and CKIs was examined under conditions promoting growth, growth arrest, or expression of differentiated traits. Formation of complexes among cell cycle regulatory proteins and their kinase activities were also investigated. The tsFHI cells express three CKIs: p16, p21, and p27. With differentiation, p21 and p27 were strongly induced, but with different kinetics: the p21 increase was rapid but transient and the p27 increase was delayed but sustained. Our results suggest that the function of p16 is primarily to inhibit cyclin D-associated kinases, making tsFHI cells dependent on cyclin E-Cdk2 for pRb phosphorylation and G1/S progression. Furthermore, they indicate that p21 is the main CKI involved in irreversible growth arrest during the early stages of cell differentiation in association with D-type cyclins, cyclin E, and Cdk2, whereas p27 may induce or stabilize expression of differentiated traits acting independently of cyclin-Cdk function.


2019 ◽  
Vol 7 (9) ◽  
pp. e14086
Author(s):  
Balasubramanian Palaniappan ◽  
Palanikumar Manoharan ◽  
Subha Arthur ◽  
Soudamani Singh ◽  
Usha Murughiyan ◽  
...  

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