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Target Concepts:
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Query: UNIPROT:P01350 (
gastrin
)
9,683
document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)
We examined the potential role of protein kinase C in signal transduction induced by
gastrin
's stimulation of rat colonic epithelium. Protein synthesis ([35S]methionine incorporation into protein) and enzyme activity (decrease in the cytosolic activity) were measured following epithelial stimulation with
gastrin
.
Gastrin
(10 nM) increased [35S]methionine incorporation into protein to 265% above maintenance level. The effect of
gastrin
was comparable to the stimulation induced by phorbol 12-myristate, 13-acetate (PMA), a strong activator of protein kinase C. The increase in protein synthesis induced by
gastrin
was totally abolished by 1-(5-isoquinolinyl)-
2-methylpiperazine
, an inhibitor of protein kinase C activity.
Gastrin
also decreased the cytosolic activity of the enzyme, an index of its activation and subsequent translocation to other cellular compartments. Therefore, we conclude that
gastrin
may be acting through a protein kinase C mechanism.
...
PMID:Possible involvement of protein kinase C in mediating gastrin-induced response in rat colonic epithelium. 180 Sep 56
We studied the role of
gastrin
in regulating cholangiocyte proliferation induced by bile duct ligation (BDL). In purified cholangiocytes, we evaluated (1) for the presence of cholecystokinin-B (CCK-B)/
gastrin
receptors, (2) the effect of
gastrin
on D-myo-Inositol 1,4,5-triphosphate (IP(3)) levels, and (3) the effect of
gastrin
on DNA synthesis and adenosine 3', 5'-monophosphate (cAMP) levels in the absence or presence of CCK-A (L-364,718) and CCK-B/
gastrin
(L-365,260) receptor inhibitors, 1, 2-bis(2-aminophenoxy)-ethane-N,N,N',N'-tetraacetic acid tetrakis(acetxymethyl ester) (BAPTA/AM; an intracellular Ca(2+) chelator), and 2 protein kinase C (PKC) inhibitors, 1-(5-Isoquinolinylsulfonyl)-
2-methylpiperazine
(H7) and staurosporin. To evaluate if
gastrin
effects on cholangiocyte proliferation are mediated by the isoform PKCalpha, we evaluated (1) for the presence of PKCalpha in cholangiocytes and (2) the effect of
gastrin
on the PKCalpha protein expression in a triton-soluble (containing cytoplasm + membrane) and a triton-insoluble (containing cytoskeleton) fraction. To evaluate the effects of
gastrin
in vivo, immediately following BDL,
gastrin
or bovine serum albumin (BSA) was infused by minipumps for 7 days to rats and we measured cholangiocyte growth and cAMP levels. We found CCK-B/
gastrin
receptors on cholangiocytes.
Gastrin
increased IP(3) levels.
Gastrin
inhibited DNA synthesis and cAMP synthesis in cholangiocytes.
Gastrin
effects on cholangiocyte functions were blocked by L-365,260, BAPTA/AM, H7, and staurosporin but not by L-364,718.
Gastrin
induced translocation of PKCalpha from cholangiocyte cytoskeleton to membrane. In vivo,
gastrin
decreased cholangiocyte growth and cAMP synthesis compared with controls. We concluded that
gastrin
inhibits cholangiocyte growth in BDL rats by interacting with CCK-B/
gastrin
receptors through a signal transduction pathway involving IP(3), Ca(2+), and PKCalpha.
...
PMID:Gastrin inhibits cholangiocyte growth in bile duct-ligated rats by interaction with cholecystokinin-B/Gastrin receptors via D-myo-inositol 1,4,5-triphosphate-, Ca(2+)-, and protein kinase C alpha-dependent mechanisms. 1086 84