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targeting Acadm produced a mouse model for MCAD deficiency with features that mimic the clinical, biochemical, and pathologic phenotype found in human patients. MCAD-deficient patients have abnormal plasma and urine metabolites associated with the medium chain–length enzyme specificity. MCAD-deficient patients [15] often display a characteristic urinary hexanoylglycine peak, as was seen in MCAD−/− mice. Acylcarnitine analysis indicated, however, mouse MCAD is more active toward longer chain substrates than the human MCAD enzyme. This finding is similar to that seen with very long-chain acyl-CoA dehydrogenase (VLCAD) where mouse VLCAD is most active toward C16 acyl-substrates as compared to human VLCAD with the most enzymatic activity toward C14 acyl-substrates [16].\nETF reduction assays of liver homogenates were performed to characterize the MCAD−/− mice at the enzymatic level. MCAD−/− mice had a significantly reduced ability to dehydrogenate C8-CoA, as is the case in human patients where MCAD activity is reduced to near zero with C8-CoA . This was less so with palmitoyl-CoA (C16:0). Because there was clearly no MCAD antigen detected in MCAD−/− mice, the residual dehydrogenase activity measured with these two substrates must represent the activity of other chain length–specific acyl-CoA dehydrogenases.\nA high degree of neonatal mortality in MCAD−/− mice was a striking observation and appears to be analogous to the patterns of clinical episodes and mortality in MCAD-deficient patients. MCAD−/− mice exhibited significant neonatal mortality with approximately 60% of the MCAD−/− pups dying prior to weaning at 3 wk of age. Human patients present with hypoglycemia, hypoketonemia, and nonketotic organic aciduria precipitated by fasting, most frequently during the first 24 mo in life [1]. It is likely that neonatal MCAD−/− pups are manifesting sensitivity to fasting with decompensation in a short period of time if maternal milk is not ingested. In contrast, no mortality was noted in adult MCAD−/− mice unless challenged with cold stress and fasting. Under cold challenge conditions, however, MCAD−/− mice were unable to maintain body temperature. Brown fat is predominantly responsible for thermogenesis and normally expresses high levels of Acadm mRNA.\nThe microvesicular and macrovesicular hepatic steatosis seen in fasted MCAD−/− mice is consistent with the primary pathological finding seen in human MCAD patients with fasting stress. Sporadic cardiac lesions in MCAD−/− mice, however, were an interesting and unexpected finding. The diffuse cardiomyopathy with multifocal myocyte degeneration and necrosis observed in MCAD−/− mice has not been reported in human MCAD patients, however, cardiac arrhythmias and dysfunction have been reported in MCAD-deficient patients [17, 18]. Interestingly, cardiomyopathy has been observed in VLCAD deficiency [19] and other disorders of long chain fat metabolism such as severe CPT-1 and -2 deficiencies [1]. Thus it is tempting to relate the cardiac problems in the mouse to the apparent broader range of substrate utilization of mouse MCAD. The inconsistent liver and cardiac lesions in these mice is analogous with the significant inter- and intrafamilial phenotypic heterogeneity seen in MCAD deficiency in humans [1,20].\nIn comparisons with our experiences with the other mouse models for acyl-CoA dehydrogenase deficiencies, the overall phenotype of MCAD−/− mice is less severe than that found in LCAD−/− mice, yet more pronounced than the VLCAD−/− or SCAD−/− mouse models [16,21,22]. All of these mutants are cold intolerant and display varying degrees of fatty changes in liver, heart, and kidney. LCAD−/− mice show more spontaneous deaths and gestational losses than the other deficiencies [21]. The significant neonatal mortality in MCAD−/− mice is distinctive from these other mouse models suggesting a greater degree of sensitivity to fasting intolerance. The phenotypes of both the VLCAD−/− and SCAD−/− mice are relatively mild if the animals are not cold stressed [16,22]. The MCAD-deficient mouse offers new insights into the pathogenesis of mitochondrial β-oxidation deficiencies and will provide a robust tool to better understand the role of fatty acids in other relevant diseases."}

{"project":"craft-ca-core-dev","denotations":[{"id":"T4690","span":{"begin":2151,"end":2155},"obj":"NCBITaxon:10088"},{"id":"T4689","span":{"begin":2048,"end":2052},"obj":"NCBITaxon:10088"},{"id":"T4688","span":{"begin":2034,"end":2039},"obj":"UBERON:0007023"},{"id":"T4687","span":{"begin":1985,"end":1993},"obj":"GO:0007631"},{"id":"T4686","span":{"begin":1973,"end":1977},"obj":"UBERON:0001913"},{"id":"T4685","span":{"begin":1826,"end":1830},"obj":"UBERON:0000104"},{"id":"T4684","span":{"begin":1670,"end":1675},"obj":"NCBITaxon:9606"},{"id":"T4683","span":{"begin":1631,"end":1636},"obj":"GO:0016265"},{"id":"T4682","span":{"begin":1542,"end":1546},"obj":"NCBITaxon:10088"},{"id":"T4681","span":{"begin":1395,"end":1399},"obj":"NCBITaxon:10088"},{"id":"T4680","span":{"begin":1323,"end":1331},"obj":"CHEBI:17984"},{"id":"T4679","span":{"begin":1187,"end":1191},"obj":"NCBITaxon:10088"},{"id":"T4678","span":{"begin":1159,"end":1166},"obj":"CHEBI:59132"},{"id":"T4677","span":{"begin":1102,"end":1115},"obj":"CHEBI:15525"},{"id":"T4676","span":{"begin":1074,"end":1077},"obj":"CHEBI:15346"},{"id":"T4675","span":{"begin":1007,"end":1012},"obj":"NCBITaxon:9606"},{"id":"T4674","span":{"begin":984,"end":987},"obj":"CHEBI:15346"},{"id":"T4673","span":{"begin":967,"end":980},"obj":"MOP:0000590"},{"id":"T4672","span":{"begin":923,"end":927},"obj":"NCBITaxon:10088"},{"id":"T4671","span":{"begin":886,"end":890},"obj":"NCBITaxon:10088"},{"id":"T4670","span":{"begin":825,"end":830},"obj":"UBERON:0002107"},{"id":"T4669","span":{"begin":805,"end":814},"obj":"MOP:0000569"},{"id":"T4668","span":{"begin":801,"end":804},"obj":"GO:0045251"},{"id":"T4667","span":{"begin":779,"end":783},"obj":"CHEBI:22221"},{"id":"T4666","span":{"begin":723,"end":728},"obj":"NCBITaxon:9606"},{"id":"T4665","span":{"begin":692,"end":696},"obj":"CHEBI:22221"},{"id":"T4664","span":{"begin":654,"end":659},"obj":"NCBITaxon:10088"},{"id":"T4663","span":{"begin":601,"end":625},"obj":"CHEBI:61910"},{"id":"T4662","span":{"begin":540,"end":545},"obj":"NCBITaxon:9606"},{"id":"T4661","span":{"begin":474,"end":479},"obj":"NCBITaxon:10088"},{"id":"T4660","span":{"begin":431,"end":444},"obj":"CHEBI:17387"},{"id":"T4659","span":{"begin":425,"end":429},"obj":"NCBITaxon:10088"},{"id":"T4658","span":{"begin":380,"end":395},"obj":"CHEBI:64390"},{"id":"T4657","span":{"begin":372,"end":379},"obj":"UBERON:0001088"},{"id":"T4656","span":{"begin":240,"end":251},"obj":"CHEBI:25212"},{"id":"T4655","span":{"begin":234,"end":239},"obj":"UBERON:0001088"},{"id":"T4654","span":{"begin":223,"end":229},"obj":"UBERON:0001969"},{"id":"T4653","span":{"begin":169,"end":174},"obj":"NCBITaxon:9606"},{"id":"T4652","span":{"begin":51,"end":56},"obj":"NCBITaxon:10088"},{"id":"T4735","span":{"begin":4253,"end":4264},"obj":"CHEBI:35366"},{"id":"T4734","span":{"begin":4166,"end":4175},"obj":"MOP:0000568"},{"id":"T4733","span":{"begin":4150,"end":4163},"obj":"GO:0005739"},{"id":"T4732","span":{"begin":4099,"end":4104},"obj":"NCBITaxon:10088"},{"id":"T4731","span":{"begin":4041,"end":4048},"obj":"NCBITaxon:33208"},{"id":"T4730","span":{"begin":4009,"end":4013},"obj":"NCBITaxon:10088"},{"id":"T4729","span":{"begin":3881,"end":3886},"obj":"NCBITaxon:10088"},{"id":"T4728","span":{"begin":3844,"end":3848},"obj":"NCBITaxon:10088"},{"id":"T4727","span":{"begin":3745,"end":3756},"obj":"GO:0007565"},{"id":"T4726","span":{"begin":3734,"end":3740},"obj":"GO:0016265"},{"id":"T4725","span":{"begin":3707,"end":3711},"obj":"NCBITaxon:10088"},{"id":"T4724","span":{"begin":3691,"end":3697},"obj":"UBERON:0002113"},{"id":"T4723","span":{"begin":3680,"end":3685},"obj":"UBERON:0000948"},{"id":"T4722","span":{"begin":3673,"end":3678},"obj":"UBERON:0002107"},{"id":"T4721","span":{"begin":3559,"end":3564},"obj":"NCBITaxon:10088"},{"id":"T4720","span":{"begin":3504,"end":3508},"obj":"NCBITaxon:10088"},{"id":"T4719","span":{"begin":3457,"end":3461},"obj":"NCBITaxon:10088"},{"id":"T4718","span":{"begin":3387,"end":3395},"obj":"CHEBI:17984"},{"id":"T4717","span":{"begin":3370,"end":3375},"obj":"NCBITaxon:10088"},{"id":"T4716","span":{"begin":3304,"end":3310},"obj":"NCBITaxon:9606"},{"id":"T4715","span":{"begin":3188,"end":3192},"obj":"NCBITaxon:10088"},{"id":"T4714","span":{"begin":3163,"end":3170},"obj":"UBERON:0000948"},{"id":"T4713","span":{"begin":3153,"end":3158},"obj":"UBERON:0002107"},{"id":"T4712","span":{"begin":3124,"end":3129},"obj":"NCBITaxon:10088"},{"id":"T4711","span":{"begin":3060,"end":3065},"obj":"NCBITaxon:10088"},{"id":"T4710","span":{"begin":3036,"end":3043},"obj":"UBERON:0000948"},{"id":"T4709","span":{"begin":2981,"end":2983},"obj":"PR:000005838"},{"id":"T4708","span":{"begin":2971,"end":2974},"obj":"_FRAGMENT"},{"id":"T4707","span":{"begin":2971,"end":2976},"obj":"PR:000005835"},{"id":"T4706","span":{"begin":2930,"end":2955},"obj":"GO:0001676"},{"id":"T4705","span":{"begin":2930,"end":2944},"obj":"CHEBI:15904"},{"id":"T4704","span":{"begin":2742,"end":2749},"obj":"UBERON:0000948"},{"id":"T4703","span":{"begin":2712,"end":2717},"obj":"NCBITaxon:9606"},{"id":"T4702","span":{"begin":2682,"end":2686},"obj":"NCBITaxon:10088"},{"id":"T4701","span":{"begin":2628,"end":2635},"obj":"CL:0000187"},{"id":"T4700","span":{"begin":2526,"end":2530},"obj":"NCBITaxon:10088"},{"id":"T4699","span":{"begin":2499,"end":2506},"obj":"UBERON:0000948"},{"id":"T4698","span":{"begin":2449,"end":2454},"obj":"NCBITaxon:9606"},{"id":"T4697","span":{"begin":2384,"end":2388},"obj":"NCBITaxon:10088"},{"id":"T4696","span":{"begin":2343,"end":2350},"obj":"UBERON:0002107"},{"id":"T4695","span":{"begin":2333,"end":2342},"obj":"GO:0031982"},{"id":"T4694","span":{"begin":2314,"end":2323},"obj":"GO:0031982"},{"id":"T4693","span":{"begin":2268,"end":2277},"obj":"GO:0010467"},{"id":"T4692","span":{"begin":2241,"end":2254},"obj":"GO:0031649"},{"id":"T4691","span":{"begin":2198,"end":2207},"obj":"UBERON:0001348"}],"relations":[{"id":"R3110","pred":"_lexicallyChainedTo","subj":"T4709","obj":"T4708"}],"text":"Discussion\nSuccessfully targeting Acadm produced a mouse model for MCAD deficiency with features that mimic the clinical, biochemical, and pathologic phenotype found in human patients. MCAD-deficient patients have abnormal plasma and urine metabolites associated with the medium chain–length enzyme specificity. MCAD-deficient patients [15] often display a characteristic urinary hexanoylglycine peak, as was seen in MCAD−/− mice. Acylcarnitine analysis indicated, however, mouse MCAD is more active toward longer chain substrates than the human MCAD enzyme. This finding is similar to that seen with very long-chain acyl-CoA dehydrogenase (VLCAD) where mouse VLCAD is most active toward C16 acyl-substrates as compared to human VLCAD with the most enzymatic activity toward C14 acyl-substrates [16].\nETF reduction assays of liver homogenates were performed to characterize the MCAD−/− mice at the enzymatic level. MCAD−/− mice had a significantly reduced ability to dehydrogenate C8-CoA, as is the case in human patients where MCAD activity is reduced to near zero with C8-CoA . This was less so with palmitoyl-CoA (C16:0). Because there was clearly no MCAD antigen detected in MCAD−/− mice, the residual dehydrogenase activity measured with these two substrates must represent the activity of other chain length–specific acyl-CoA dehydrogenases.\nA high degree of neonatal mortality in MCAD−/− mice was a striking observation and appears to be analogous to the patterns of clinical episodes and mortality in MCAD-deficient patients. MCAD−/− mice exhibited significant neonatal mortality with approximately 60% of the MCAD−/− pups dying prior to weaning at 3 wk of age. Human patients present with hypoglycemia, hypoketonemia, and nonketotic organic aciduria precipitated by fasting, most frequently during the first 24 mo in life [1]. It is likely that neonatal MCAD−/− pups are manifesting sensitivity to fasting with decompensation in a short period of time if maternal milk is not ingested. In contrast, no mortality was noted in adult MCAD−/− mice unless challenged with cold stress and fasting. Under cold challenge conditions, however, MCAD−/− mice were unable to maintain body temperature. Brown fat is predominantly responsible for thermogenesis and normally expresses high levels of Acadm mRNA.\nThe microvesicular and macrovesicular hepatic steatosis seen in fasted MCAD−/− mice is consistent with the primary pathological finding seen in human MCAD patients with fasting stress. Sporadic cardiac lesions in MCAD−/− mice, however, were an interesting and unexpected finding. The diffuse cardiomyopathy with multifocal myocyte degeneration and necrosis observed in MCAD−/− mice has not been reported in human MCAD patients, however, cardiac arrhythmias and dysfunction have been reported in MCAD-deficient patients [17, 18]. Interestingly, cardiomyopathy has been observed in VLCAD deficiency [19] and other disorders of long chain fat metabolism such as severe CPT-1 and -2 deficiencies [1]. Thus it is tempting to relate the cardiac problems in the mouse to the apparent broader range of substrate utilization of mouse MCAD. The inconsistent liver and cardiac lesions in these mice is analogous with the significant inter- and intrafamilial phenotypic heterogeneity seen in MCAD deficiency in humans [1,20].\nIn comparisons with our experiences with the other mouse models for acyl-CoA dehydrogenase deficiencies, the overall phenotype of MCAD−/− mice is less severe than that found in LCAD−/− mice, yet more pronounced than the VLCAD−/− or SCAD−/− mouse models [16,21,22]. All of these mutants are cold intolerant and display varying degrees of fatty changes in liver, heart, and kidney. LCAD−/− mice show more spontaneous deaths and gestational losses than the other deficiencies [21]. The significant neonatal mortality in MCAD−/− mice is distinctive from these other mouse models suggesting a greater degree of sensitivity to fasting intolerance. The phenotypes of both the VLCAD−/− and SCAD−/− mice are relatively mild if the animals are not cold stressed [16,22]. The MCAD-deficient mouse offers new insights into the pathogenesis of mitochondrial β-oxidation deficiencies and will provide a robust tool to better understand the role of fatty acids in other relevant diseases."}

{"project":"2_test","denotations":[{"id":"16121256-3054550-86078329","span":{"begin":337,"end":339},"obj":"3054550"},{"id":"16121256-11590124-86078330","span":{"begin":796,"end":798},"obj":"11590124"},{"id":"16121256-11826276-86078331","span":{"begin":1832,"end":1833},"obj":"11826276"},{"id":"16121256-12897989-86078332","span":{"begin":2825,"end":2827},"obj":"12897989"},{"id":"16121256-15858970-86078333","span":{"begin":2829,"end":2831},"obj":"15858970"},{"id":"16121256-9498103-86078334","span":{"begin":2903,"end":2905},"obj":"9498103"},{"id":"16121256-11826276-86078335","span":{"begin":2998,"end":2999},"obj":"11826276"},{"id":"16121256-11826276-86078336","span":{"begin":3312,"end":3313},"obj":"11826276"},{"id":"16121256-3786030-86078337","span":{"begin":3314,"end":3316},"obj":"3786030"},{"id":"16121256-11590124-86078338","span":{"begin":3573,"end":3575},"obj":"11590124"},{"id":"16121256-9861014-86078339","span":{"begin":3576,"end":3578},"obj":"9861014"},{"id":"16121256-2919115-86078340","span":{"begin":3579,"end":3581},"obj":"2919115"},{"id":"16121256-9861014-86078341","span":{"begin":3793,"end":3795},"obj":"9861014"},{"id":"16121256-11590124-86078342","span":{"begin":4072,"end":4074},"obj":"11590124"},{"id":"16121256-2919115-86078343","span":{"begin":4075,"end":4077},"obj":"2919115"},{"id":"T51581","span":{"begin":337,"end":339},"obj":"3054550"},{"id":"T54031","span":{"begin":796,"end":798},"obj":"11590124"},{"id":"T82680","span":{"begin":1832,"end":1833},"obj":"11826276"},{"id":"T5881","span":{"begin":2825,"end":2827},"obj":"12897989"},{"id":"T84974","span":{"begin":2829,"end":2831},"obj":"15858970"},{"id":"T76819","span":{"begin":2903,"end":2905},"obj":"9498103"},{"id":"T6939","span":{"begin":2998,"end":2999},"obj":"11826276"},{"id":"T95865","span":{"begin":3312,"end":3313},"obj":"11826276"},{"id":"T70433","span":{"begin":3314,"end":3316},"obj":"3786030"},{"id":"T33523","span":{"begin":3573,"end":3575},"obj":"11590124"},{"id":"T5628","span":{"begin":3576,"end":3578},"obj":"9861014"},{"id":"T94082","span":{"begin":3579,"end":3581},"obj":"2919115"},{"id":"T78823","span":{"begin":3793,"end":3795},"obj":"9861014"},{"id":"T19746","span":{"begin":4072,"end":4074},"obj":"11590124"},{"id":"T30516","span":{"begin":4075,"end":4077},"obj":"2919115"}],"text":"Discussion\nSuccessfully targeting Acadm produced a mouse model for MCAD deficiency with features that mimic the clinical, biochemical, and pathologic phenotype found in human patients. MCAD-deficient patients have abnormal plasma and urine metabolites associated with the medium chain–length enzyme specificity. MCAD-deficient patients [15] often display a characteristic urinary hexanoylglycine peak, as was seen in MCAD−/− mice. Acylcarnitine analysis indicated, however, mouse MCAD is more active toward longer chain substrates than the human MCAD enzyme. This finding is similar to that seen with very long-chain acyl-CoA dehydrogenase (VLCAD) where mouse VLCAD is most active toward C16 acyl-substrates as compared to human VLCAD with the most enzymatic activity toward C14 acyl-substrates [16].\nETF reduction assays of liver homogenates were performed to characterize the MCAD−/− mice at the enzymatic level. MCAD−/− mice had a significantly reduced ability to dehydrogenate C8-CoA, as is the case in human patients where MCAD activity is reduced to near zero with C8-CoA . This was less so with palmitoyl-CoA (C16:0). Because there was clearly no MCAD antigen detected in MCAD−/− mice, the residual dehydrogenase activity measured with these two substrates must represent the activity of other chain length–specific acyl-CoA dehydrogenases.\nA high degree of neonatal mortality in MCAD−/− mice was a striking observation and appears to be analogous to the patterns of clinical episodes and mortality in MCAD-deficient patients. MCAD−/− mice exhibited significant neonatal mortality with approximately 60% of the MCAD−/− pups dying prior to weaning at 3 wk of age. Human patients present with hypoglycemia, hypoketonemia, and nonketotic organic aciduria precipitated by fasting, most frequently during the first 24 mo in life [1]. It is likely that neonatal MCAD−/− pups are manifesting sensitivity to fasting with decompensation in a short period of time if maternal milk is not ingested. In contrast, no mortality was noted in adult MCAD−/− mice unless challenged with cold stress and fasting. Under cold challenge conditions, however, MCAD−/− mice were unable to maintain body temperature. Brown fat is predominantly responsible for thermogenesis and normally expresses high levels of Acadm mRNA.\nThe microvesicular and macrovesicular hepatic steatosis seen in fasted MCAD−/− mice is consistent with the primary pathological finding seen in human MCAD patients with fasting stress. Sporadic cardiac lesions in MCAD−/− mice, however, were an interesting and unexpected finding. The diffuse cardiomyopathy with multifocal myocyte degeneration and necrosis observed in MCAD−/− mice has not been reported in human MCAD patients, however, cardiac arrhythmias and dysfunction have been reported in MCAD-deficient patients [17, 18]. Interestingly, cardiomyopathy has been observed in VLCAD deficiency [19] and other disorders of long chain fat metabolism such as severe CPT-1 and -2 deficiencies [1]. Thus it is tempting to relate the cardiac problems in the mouse to the apparent broader range of substrate utilization of mouse MCAD. The inconsistent liver and cardiac lesions in these mice is analogous with the significant inter- and intrafamilial phenotypic heterogeneity seen in MCAD deficiency in humans [1,20].\nIn comparisons with our experiences with the other mouse models for acyl-CoA dehydrogenase deficiencies, the overall phenotype of MCAD−/− mice is less severe than that found in LCAD−/− mice, yet more pronounced than the VLCAD−/− or SCAD−/− mouse models [16,21,22]. All of these mutants are cold intolerant and display varying degrees of fatty changes in liver, heart, and kidney. LCAD−/− mice show more spontaneous deaths and gestational losses than the other deficiencies [21]. The significant neonatal mortality in MCAD−/− mice is distinctive from these other mouse models suggesting a greater degree of sensitivity to fasting intolerance. The phenotypes of both the VLCAD−/− and SCAD−/− mice are relatively mild if the animals are not cold stressed [16,22]. The MCAD-deficient mouse offers new insights into the pathogenesis of mitochondrial β-oxidation deficiencies and will provide a robust tool to better understand the role of fatty acids in other relevant diseases."}

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"obj":"SO_EXT:sequence_nullness_or_absence"},{"id":"T4907","span":{"begin":3836,"end":3840},"obj":"GO_PR_EXT:medium_chain_acyl_CoA_dehydrogenase"},{"id":"T4906","span":{"begin":3814,"end":3822},"obj":"PATO_UBERON_EXT:neonate_or_newborn"},{"id":"T4905","span":{"begin":3745,"end":3756},"obj":"GO:0007565"},{"id":"T4904","span":{"begin":3734,"end":3740},"obj":"GO:0016265"},{"id":"T4903","span":{"begin":3707,"end":3711},"obj":"NCBITaxon:10088"},{"id":"T4902","span":{"begin":3705,"end":3706},"obj":"SO_EXT:sequence_nullness_or_absence"},{"id":"T4901","span":{"begin":3703,"end":3704},"obj":"SO_EXT:sequence_nullness_or_absence"},{"id":"T4900","span":{"begin":3699,"end":3703},"obj":"GO_PR_EXT:long_chain_acyl_CoA_dehydrogenase"},{"id":"T4899","span":{"begin":3691,"end":3697},"obj":"UBERON:0002113"},{"id":"T4898","span":{"begin":3680,"end":3685},"obj":"UBERON:0000948"}],"relations":[{"id":"R3111","pred":"_lexicallyChainedTo","subj":"T4867","obj":"T4866"}],"text":"Discussion\nSuccessfully targeting Acadm produced a mouse model for MCAD deficiency with features that mimic the clinical, biochemical, and pathologic phenotype found in human patients. MCAD-deficient patients have abnormal plasma and urine metabolites associated with the medium chain–length enzyme specificity. MCAD-deficient patients [15] often display a characteristic urinary hexanoylglycine peak, as was seen in MCAD−/− mice. Acylcarnitine analysis indicated, however, mouse MCAD is more active toward longer chain substrates than the human MCAD enzyme. This finding is similar to that seen with very long-chain acyl-CoA dehydrogenase (VLCAD) where mouse VLCAD is most active toward C16 acyl-substrates as compared to human VLCAD with the most enzymatic activity toward C14 acyl-substrates [16].\nETF reduction assays of liver homogenates were performed to characterize the MCAD−/− mice at the enzymatic level. MCAD−/− mice had a significantly reduced ability to dehydrogenate C8-CoA, as is the case in human patients where MCAD activity is reduced to near zero with C8-CoA . This was less so with palmitoyl-CoA (C16:0). Because there was clearly no MCAD antigen detected in MCAD−/− mice, the residual dehydrogenase activity measured with these two substrates must represent the activity of other chain length–specific acyl-CoA dehydrogenases.\nA high degree of neonatal mortality in MCAD−/− mice was a striking observation and appears to be analogous to the patterns of clinical episodes and mortality in MCAD-deficient patients. MCAD−/− mice exhibited significant neonatal mortality with approximately 60% of the MCAD−/− pups dying prior to weaning at 3 wk of age. Human patients present with hypoglycemia, hypoketonemia, and nonketotic organic aciduria precipitated by fasting, most frequently during the first 24 mo in life [1]. It is likely that neonatal MCAD−/− pups are manifesting sensitivity to fasting with decompensation in a short period of time if maternal milk is not ingested. In contrast, no mortality was noted in adult MCAD−/− mice unless challenged with cold stress and fasting. Under cold challenge conditions, however, MCAD−/− mice were unable to maintain body temperature. Brown fat is predominantly responsible for thermogenesis and normally expresses high levels of Acadm mRNA.\nThe microvesicular and macrovesicular hepatic steatosis seen in fasted MCAD−/− mice is consistent with the primary pathological finding seen in human MCAD patients with fasting stress. Sporadic cardiac lesions in MCAD−/− mice, however, were an interesting and unexpected finding. The diffuse cardiomyopathy with multifocal myocyte degeneration and necrosis observed in MCAD−/− mice has not been reported in human MCAD patients, however, cardiac arrhythmias and dysfunction have been reported in MCAD-deficient patients [17, 18]. Interestingly, cardiomyopathy has been observed in VLCAD deficiency [19] and other disorders of long chain fat metabolism such as severe CPT-1 and -2 deficiencies [1]. Thus it is tempting to relate the cardiac problems in the mouse to the apparent broader range of substrate utilization of mouse MCAD. The inconsistent liver and cardiac lesions in these mice is analogous with the significant inter- and intrafamilial phenotypic heterogeneity seen in MCAD deficiency in humans [1,20].\nIn comparisons with our experiences with the other mouse models for acyl-CoA dehydrogenase deficiencies, the overall phenotype of MCAD−/− mice is less severe than that found in LCAD−/− mice, yet more pronounced than the VLCAD−/− or SCAD−/− mouse models [16,21,22]. All of these mutants are cold intolerant and display varying degrees of fatty changes in liver, heart, and kidney. LCAD−/− mice show more spontaneous deaths and gestational losses than the other deficiencies [21]. The significant neonatal mortality in MCAD−/− mice is distinctive from these other mouse models suggesting a greater degree of sensitivity to fasting intolerance. The phenotypes of both the VLCAD−/− and SCAD−/− mice are relatively mild if the animals are not cold stressed [16,22]. The MCAD-deficient mouse offers new insights into the pathogenesis of mitochondrial β-oxidation deficiencies and will provide a robust tool to better understand the role of fatty acids in other relevant diseases."}