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. 1999 Oct 12;96(21):11854–11859. doi: 10.1073/pnas.96.21.11854

Table 1.

Binding affinities of DAG lactones to β2-chimaerin

Compound R1 R2 Ki β2-chimaerin (nM) Ki PKCα (nM) Ratio Ki (PKCα/β2-chim)
graphic file with name pq21934460t1.jpg L3-DL-B8 CH3(CH2)2 CH2CH(i-Pr)2 8.4 ± 1.4 (3) 19.4 ± 1.5 2.3
L5-DL-B8 CH2(CH2)4 CH2CH(i-Pr)2 2.7 ± 0.5 (3) 4.4 ± 0.6 1.6
L9-DL-B8 CH3(CH2)8 CH2CH(i-Pr)2 2.1 ± 0.2 (3) 2.3 ± 0.1 1.1
B8-DL-L3 CH2CH(i-Pr)2 CH3(CH2)2 N.D. 24 ± 0.9 ND
B8-DL-L5 CH2CH(i-Pr)2 CH3(CH2)4 2.8 ± 0.3 (3) 7.3 ± 0.5 2.6
B8-DL-L9 CH2CH(i-Pr)2 CH3(CH2)8 2.2 ± 0.1 (3) 13.1 ± 0.4 6.0
B8-DL-B8 CH2CH(i-Pr)2 CH2CH(i-Pr)2 0.9 ± 0.1 (10) 2.9 ± 0.2 3.2
OAG 144 ± 26  (3) 230 ± 28 (3) 1.6
DAG lactone (R1-DL-R2) PDBu 1.5 ± 0.1 (3) 0.15 ± 0.01 (3) 0.1

A fixed concentration of [3H]PDBu (5 nM) and increasing concentrations (in triplicate) of the competing ligand were used in each binding assay. The ID50 values were determined from the competition curves and the corresponding Ki values were calculated as described in Materials and Methods. Values are expressed as the mean ± SE of the number of experiments in parentheses. ND, not determined.