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directly assess the role of activation of PPARδ in control of muscle fiber plasticity and mitochondrial biogenesis, we generated mice expressing a transgene in which the 78-amino-acid VP16 activation domain was fused to the N-terminus of full-length PPARδ, under control of the 2.2-kb human α-skeletal actin promoter. In agreement with the previous characterization of this promoter (Brennan and Hardeman 1993; Clapham et al. 2000), the VP16-PPARδ transgene was selectively expressed in skeletal muscle, with 10-fold less in the heart (Figure 1C). Among different types of muscle fibers, the levels of VP16-PPARδ expression appeared to be similar (unpublished data). As shown in Figure 1D for gastrocnemius muscle, VP16-PPARδ fusion protein was produced at a level similar to that of endogenous PPARδ in wild-type littermates. Interestingly, the level of endogenous muscle PPARδ protein in the transgenic mice was much higher than in the control littermates. The substantial increase of endogenous PPARδ may have been caused by a switch to type I fiber (see below), which intrinsically expresses higher levels of PPARδ (Figure 1A and 1B)."}

{"project":"2_test","denotations":[{"id":"15328533-7678010-84708276","span":{"begin":408,"end":412},"obj":"7678010"},{"id":"15328533-10935638-84708277","span":{"begin":429,"end":433},"obj":"10935638"},{"id":"T71983","span":{"begin":408,"end":412},"obj":"7678010"},{"id":"T59671","span":{"begin":429,"end":433},"obj":"10935638"}],"text":"To directly assess the role of activation of PPARδ in control of muscle fiber plasticity and mitochondrial biogenesis, we generated mice expressing a transgene in which the 78-amino-acid VP16 activation domain was fused to the N-terminus of full-length PPARδ, under control of the 2.2-kb human α-skeletal actin promoter. In agreement with the previous characterization of this promoter (Brennan and Hardeman 1993; Clapham et al. 2000), the VP16-PPARδ transgene was selectively expressed in skeletal muscle, with 10-fold less in the heart (Figure 1C). Among different types of muscle fibers, the levels of VP16-PPARδ expression appeared to be similar (unpublished data). As shown in Figure 1D for gastrocnemius muscle, VP16-PPARδ fusion protein was produced at a level similar to that of endogenous PPARδ in wild-type littermates. Interestingly, the level of endogenous muscle PPARδ protein in the transgenic mice was much higher than in the control littermates. The substantial increase of endogenous PPARδ may have been caused by a switch to type I fiber (see below), which intrinsically expresses higher levels of PPARδ (Figure 1A and 1B)."}

{"project":"craft-ca-core-ex-dev","denotations":[{"id":"T1137","span":{"begin":253,"end":258},"obj":"PR_EXT:000013057"},{"id":"T1138","span":{"begin":266,"end":273},"obj":"GO:0065007"},{"id":"T1139","span":{"begin":286,"end":287},"obj":"CHEBI_SO_EXT:base"},{"id":"T1140","span":{"begin":288,"end":293},"obj":"NCBITaxon:9606"},{"id":"T1141","span":{"begin":294,"end":310},"obj":"PR_EXT:000003674"},{"id":"T1142","span":{"begin":296,"end":304},"obj":"UBERON:0004288"},{"id":"T1143","span":{"begin":311,"end":319},"obj":"SO_EXT:0000167"},{"id":"T1144","span":{"begin":377,"end":385},"obj":"SO_EXT:0000167"},{"id":"T1145","span":{"begin":440,"end":444},"obj":"PR_EXT:P06492"},{"id":"T1146","span":{"begin":445,"end":450},"obj":"PR_EXT:000013057"},{"id":"T1147","span":{"begin":451,"end":460},"obj":"SO_EXT:0000902"},{"id":"T1148","span":{"begin":477,"end":486},"obj":"GO:0010467"},{"id":"T1169","span":{"begin":1043,"end":1055},"obj":"CL:0002211"},{"id":"T1170","span":{"begin":1089,"end":1098},"obj":"GO:0010467"},{"id":"T1171","span":{"begin":1116,"end":1121},"obj":"PR_EXT:000013057"},{"id":"T1123","span":{"begin":45,"end":50},"obj":"PR_EXT:000013057"},{"id":"T1124","span":{"begin":54,"end":61},"obj":"GO:0065007"},{"id":"T1125","span":{"begin":65,"end":71},"obj":"UBERON_EXT:muscle_structure_or_tissue"},{"id":"T1126","span":{"begin":65,"end":77},"obj":"CL:0000187"},{"id":"T1127","span":{"begin":93,"end":106},"obj":"GO:0005739"},{"id":"T1128","span":{"begin":107,"end":117},"obj":"GO_EXT:biogenesis_or_biosynthesis"},{"id":"T1129","span":{"begin":132,"end":136},"obj":"NCBITaxon:10088"},{"id":"T1130","span":{"begin":137,"end":147},"obj":"GO:0010467"},{"id":"T1131","span":{"begin":150,"end":159},"obj":"SO_EXT:0000902"},{"id":"T1132","span":{"begin":176,"end":186},"obj":"CHEBI_SO_EXT:amino_acid"},{"id":"T1133","span":{"begin":187,"end":191},"obj":"PR_EXT:P06492"},{"id":"T1134","span":{"begin":203,"end":209},"obj":"SO_EXT:0000417"},{"id":"T1135","span":{"begin":214,"end":219},"obj":"SO_EXT:sequence_fusion_process"},{"id":"T1136","span":{"begin":227,"end":237},"obj":"CHEBI_SO_EXT:N_terminus_or_N_terminal_region"},{"id":"T1149","span":{"begin":490,"end":505},"obj":"UBERON_EXT:skeletal_muscle_organ_or_tissue"},{"id":"T1150","span":{"begin":532,"end":537},"obj":"UBERON:0000948"},{"id":"T1151","span":{"begin":576,"end":582},"obj":"UBERON_EXT:muscle_structure_or_tissue"},{"id":"T1152","span":{"begin":576,"end":589},"obj":"CL:0000187"},{"id":"T1153","span":{"begin":605,"end":609},"obj":"PR_EXT:P06492"},{"id":"T1154","span":{"begin":610,"end":615},"obj":"PR_EXT:000013057"},{"id":"T1155","span":{"begin":616,"end":626},"obj":"GO:0010467"},{"id":"T1156","span":{"begin":696,"end":716},"obj":"UBERON:0001388"},{"id":"T1157","span":{"begin":718,"end":722},"obj":"PR_EXT:P06492"},{"id":"T1158","span":{"begin":723,"end":728},"obj":"PR_EXT:000013057"},{"id":"T1159","span":{"begin":729,"end":735},"obj":"SO_EXT:sequence_fusion_entity_or_process"},{"id":"T1160","span":{"begin":736,"end":743},"obj":"CHEBI_PR_EXT:protein"},{"id":"T1161","span":{"begin":798,"end":803},"obj":"PR_EXT:000013057"},{"id":"T1162","span":{"begin":807,"end":816},"obj":"SO_EXT:wild_type_entity_or_quality"},{"id":"T1163","span":{"begin":869,"end":875},"obj":"UBERON_EXT:muscle_structure_or_tissue"},{"id":"T1164","span":{"begin":876,"end":881},"obj":"PR_EXT:000013057"},{"id":"T1165","span":{"begin":882,"end":889},"obj":"CHEBI_PR_EXT:protein"},{"id":"T1166","span":{"begin":897,"end":907},"obj":"SO_EXT:transgenic_entity"},{"id":"T1167","span":{"begin":908,"end":912},"obj":"NCBITaxon:10088"},{"id":"T1168","span":{"begin":1001,"end":1006},"obj":"PR_EXT:000013057"}],"text":"To directly assess the role of activation of PPARδ in control of muscle fiber plasticity and mitochondrial biogenesis, we generated mice expressing a transgene in which the 78-amino-acid VP16 activation domain was fused to the N-terminus of full-length PPARδ, under control of the 2.2-kb human α-skeletal actin promoter. In agreement with the previous characterization of this promoter (Brennan and Hardeman 1993; Clapham et al. 2000), the VP16-PPARδ transgene was selectively expressed in skeletal muscle, with 10-fold less in the heart (Figure 1C). Among different types of muscle fibers, the levels of VP16-PPARδ expression appeared to be similar (unpublished data). As shown in Figure 1D for gastrocnemius muscle, VP16-PPARδ fusion protein was produced at a level similar to that of endogenous PPARδ in wild-type littermates. Interestingly, the level of endogenous muscle PPARδ protein in the transgenic mice was much higher than in the control littermates. The substantial increase of endogenous PPARδ may have been caused by a switch to type I fiber (see below), which intrinsically expresses higher levels of PPARδ (Figure 1A and 1B)."}

{"project":"craft-ca-core-dev","denotations":[{"id":"T991","span":{"begin":45,"end":50},"obj":"PR:000013057"},{"id":"T992","span":{"begin":54,"end":61},"obj":"GO:0065007"},{"id":"T993","span":{"begin":65,"end":77},"obj":"CL:0000187"},{"id":"T994","span":{"begin":93,"end":106},"obj":"GO:0005739"},{"id":"T995","span":{"begin":132,"end":136},"obj":"NCBITaxon:10088"},{"id":"T996","span":{"begin":137,"end":147},"obj":"GO:0010467"},{"id":"T997","span":{"begin":150,"end":159},"obj":"SO:0000902"},{"id":"T998","span":{"begin":187,"end":191},"obj":"PR:P06492"},{"id":"T999","span":{"begin":203,"end":209},"obj":"SO:0000417"},{"id":"T1000","span":{"begin":253,"end":258},"obj":"PR:000013057"},{"id":"T1001","span":{"begin":266,"end":273},"obj":"GO:0065007"},{"id":"T1002","span":{"begin":288,"end":293},"obj":"NCBITaxon:9606"},{"id":"T1003","span":{"begin":294,"end":310},"obj":"PR:000003674"},{"id":"T1004","span":{"begin":296,"end":304},"obj":"UBERON:0004288"},{"id":"T1005","span":{"begin":311,"end":319},"obj":"SO:0000167"},{"id":"T1006","span":{"begin":377,"end":385},"obj":"SO:0000167"},{"id":"T1007","span":{"begin":440,"end":444},"obj":"PR:P06492"},{"id":"T1008","span":{"begin":445,"end":450},"obj":"PR:000013057"},{"id":"T1009","span":{"begin":451,"end":460},"obj":"SO:0000902"},{"id":"T1010","span":{"begin":477,"end":486},"obj":"GO:0010467"},{"id":"T1011","span":{"begin":490,"end":498},"obj":"UBERON:0004288"},{"id":"T1012","span":{"begin":532,"end":537},"obj":"UBERON:0000948"},{"id":"T1013","span":{"begin":576,"end":589},"obj":"CL:0000187"},{"id":"T1014","span":{"begin":605,"end":609},"obj":"PR:P06492"},{"id":"T1015","span":{"begin":610,"end":615},"obj":"PR:000013057"},{"id":"T1016","span":{"begin":616,"end":626},"obj":"GO:0010467"},{"id":"T1017","span":{"begin":696,"end":716},"obj":"UBERON:0001388"},{"id":"T1018","span":{"begin":718,"end":722},"obj":"PR:P06492"},{"id":"T1019","span":{"begin":723,"end":728},"obj":"PR:000013057"},{"id":"T1020","span":{"begin":798,"end":803},"obj":"PR:000013057"},{"id":"T1021","span":{"begin":876,"end":881},"obj":"PR:000013057"},{"id":"T1022","span":{"begin":908,"end":912},"obj":"NCBITaxon:10088"},{"id":"T1023","span":{"begin":1001,"end":1006},"obj":"PR:000013057"},{"id":"T1024","span":{"begin":1043,"end":1055},"obj":"CL:0002211"},{"id":"T1025","span":{"begin":1089,"end":1098},"obj":"GO:0010467"},{"id":"T1026","span":{"begin":1116,"end":1121},"obj":"PR:000013057"}],"text":"To directly assess the role of activation of PPARδ in control of muscle fiber plasticity and mitochondrial biogenesis, we generated mice expressing a transgene in which the 78-amino-acid VP16 activation domain was fused to the N-terminus of full-length PPARδ, under control of the 2.2-kb human α-skeletal actin promoter. In agreement with the previous characterization of this promoter (Brennan and Hardeman 1993; Clapham et al. 2000), the VP16-PPARδ transgene was selectively expressed in skeletal muscle, with 10-fold less in the heart (Figure 1C). Among different types of muscle fibers, the levels of VP16-PPARδ expression appeared to be similar (unpublished data). As shown in Figure 1D for gastrocnemius muscle, VP16-PPARδ fusion protein was produced at a level similar to that of endogenous PPARδ in wild-type littermates. Interestingly, the level of endogenous muscle PPARδ protein in the transgenic mice was much higher than in the control littermates. The substantial increase of endogenous PPARδ may have been caused by a switch to type I fiber (see below), which intrinsically expresses higher levels of PPARδ (Figure 1A and 1B)."}