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Drug-Target Interaction

Drug

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PubChem ID:3032732
Structure:
Synonyms:
20763-88-6
234788_ALDRICH
30115-44-7
4-04-00-04312 (Beilstein Handbook Reference)
688-73-3
688-76-6
90915_FLUKA
AC1MHUMB
AC1Q2UP8
AG-G-66485
BRN 3587329
C011559
CHEMBL1236208
CID3032732
DB08601
EINECS 211-704-4
HSDB 6362
I14-3138
LS-146622
NCGC00164096-01
Stannane, tri-n-butyl-, hydride
Stannane, tributyl-
TBTC chloride
TBY
Tin, tri-n-butyl-, hydride
tri-n-butyl tin maleate
Tri-n-butylstannane hydride
tri-n-butyltin
TRI-N-BUTYLTIN HYDRIDE
Tributlytin
TRIBUTYL TIN
Tributylstannane
Tributylstannic hydride
Tributyltin
tributyltin acetate
tributyltin chloride
tributyltin fluoride
Tributyltin hydride
tributyltin ion (1+)
tributyltin tetrafluoroborate
TRIBUTYLTINHYDRIDE

Target

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Uniprot ID:KAPCG_HUMAN
Synonyms:
cAMP-dependent protein kinase catalytic subunit gamma
PKA C-gamma
EC-Numbers:2.7.11.11
Organism:Homo sapiens
Human
PDB IDs:-

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----

References:

12941541
Decreased adenylyl cyclase and cAMP-dependent protein kinase activities inhibit the cytotoxic function of human natural killer cells.. Amanuel K Bariagaber; Margaret M Whalen (2003) Human immunology display abstract
Natural killer (NK) cells are lymphocytes that are capable of destroying tumor cells and virally infected cells without prior sensitization. Elevation of cyclic 3', 5' adenosine monophosphate (cAMP) levels in NK cells is known to cause dramatic inhibition of NK cytolytic function. However, the effect of lowering cellular levels of cAMP on the cytolytic function of natural killer (NK) cells has not been studied. The current study investigated the effects of inhibiting adenylyl cyclase (AC) or cAMP-dependent protein kinase (PKA) activities on the ability of NK cells to lyse K562 tumor cells, and on the activation of NK-cell phospholipase C (PLC) by tumor targets. Exposure of NK cells to the AC inhibitors MDL-12,330A (MDL) or 2',5',-Dideoxyadenosine (DDA) completely blocked their ability to destroy K562 tumor cells. Further, target-induced stimulation of NK-cell PLC was inhibited by as much as 90% when NK cells were treated with the AC inhibitors. Treatment of NK cells with the PKA inhibitor, H-89, caused essentially complete inhibition of cytotoxic function while decreasing target-induced stimulation of PLC by about 50%. Additionally, exposure to the organotin compound, tributyltin (TBT), which decreases cAMP levels in NK cells (as much as 80%) caused a decrease in cytotoxic function by as much as 90%. These data suggest that decreased levels of cAMP may cause very significant loss of NK cytotoxic function and that this may be mediated by decreased PKA activity. These data coupled with previous work revealing that increased cAMP levels inhibit NK cytotoxic function, suggest that tight regulation of cAMP levels is critical to NK cell function.