PMC:1189074 / 4340-16229 JSONTXT

{"target":"https://pubannotation.org/docs/sourcedb/PMC/sourceid/1189074","sourcedb":"PMC","sourceid":"1189074","source_url":"http://www.ncbi.nlm.nih.gov/pmc/1189074","text":"Results\n\nGene Targeting and Generation of MCAD-Deficient Mice\nMCAD insertion vector (MCAD IV2) was designed to undergo gap repair of the 1.3-kb deleted region upon homologous recombination in 129P2 (129P2/OlaHsd) ES cells E14–1. Correct targeting of the MCAD locus resulted in a duplication of exons 8, 9, and 10 and integration of flanking plasmid and Neo sequences (Figure 1A). The insertion vector was designed to duplicate exon 8, 9, and 10 at the MCAD locus. Translation of the duplicated exon 8 region results in the formation of premature stop codons resulting in truncation of the MCAD monomer. Specifically, the first premature stop codon arises after translation of only seven amino acids from the duplicated exon 8. The resulting MCAD monomer is missing the C-terminal domain α-helixes that are responsible for making intersubunit contacts to generate the functional MCAD homotetramer.\nFigure 1 Strategy for Disruption of the Mouse Acadm Gene\n(A) The MCAD IV2 insertion targeting vector with a deleted 1.3-kb region encompassing exon 10 and flanking sequences. MCAD IV2 undergoes gap repair upon homologous recombination at the endogenous Acadm locus resulting in a duplication of exons 8, 9, and 10 at the disrupted allele.\n(B) Southern blot analysis of EcoRI-digested genomic DNA from ES cells screened by PCR. Probe A, a DNA fragment consisting of a portion of exon 10 that is not present in the targeting vector, hybridizes to an endogenous 3.1-kb fragment and, upon homologous recombination, to a 13.2-kb fragment. Lane 1 represents a wild-type ES cell line, and Lane 2 and 3 represent targeted ES cell lines. ES cell clones were screened by PCR (data not shown) and confirmed by Southern blot analysis. Southern blot analysis used an exon 10 probe (probe A), not present in the targeting vector, hybridized to a 13.2-kb band in addition to the 3.1-kb endogenous band indicating targeted insertion of the vector at the Acadm locus (Figure 1B). Correctly targeted ES cell clones were microinjected into B6 (C57BL/6NTac) blastocysts to generate chimeric mice. Chimeric mice were backcrossed to both 129P2 and B6 inbred mice to produce MCAD+/− and eventually MCAD−/− mice on a B6/129 mixed background. The studies described here were conducted exclusively on the B6/129 mixed background compared with littermate controls or B6/129 control groups maintained by intercrosses as were the mutants. Perpetuating this mutation as a congenic mutant line on the 129P2 background proved impractical. The 129P2 mice were poor breeders as wild-types, and when introduced, the Acadm mutation was nearly lost on this background because of the high rate of neonatal death. Because of the molecular structure of the targeted allele, it proved virtually impossible to distinguish all three potential genotypes. We could clearly detect the presence or absence of the targeted allele, however, whether a particular mouse was MCAD−/− or MCAD+/− could not be determined by Southern blot or PCR of genomic DNA. Ultimately MCAD−/− mice were ascertained by immunoblot analysis of offspring with subsequent perpetuation of MCAD−/− and MCAD+/+ mice as separate groups.\n\nRNA Analysis\nRT-PCR amplification from exon 7 to 11 from total heart RNA amplified the expected 600-base pair (bp) fragment in MCAD+/+ and MCAD+/− mice, and a 1.5-kb fragment in MCAD−/− mice (data not shown). Sequence analysis of the 1.5-kb fragment revealed that the amplified fragment consisted of exon 7 to exon 10 with 280 bp of pGEM plasmid sequence followed by exons 8–11. Some of the plasmid sequences, along with the pPGKNEOpA sequence, were deleted from this spliced mRNA.\nNorthern blot analysis revealed Acadm was normally expressed in all tissues analyzed from MCAD+/+ mice with the most robust expression occurring in brown fat, kidney, heart, skeletal muscle, and liver with minimal expression in the brain, white fat, and testes (Figure 2). Interestingly, although RT-PCR amplified an incorrectly spliced Acadm transcript, no Acadm transcripts were detected by northern blot analysis from MCAD−/− mice. These results strongly suggest that the mutant RNA is unstable and degraded rapidly or, alternatively, undergoes nonsense mediated RNA decay.\nFigure 2 Northern Blot Analysis from MCAD−/− (n = 2) and MCAD+/+ (n = 2) Mice\nAcadm message was detected from the heart, liver, brown fat, brain, kidney, and muscle (and white fat and testes, data not shown) of only MCAD+/+ mice. Most robust expression occurred in brown fat, kidney, heart, and skeletal muscle. MCAD−/− mice had no detectable message in all tissues examined.\n\nLiver Enzyme Analyses\nImmunoblot analyses of liver homogenates with anti-MCAD antisera demonstrated that the 42 kDa MCAD monomer was present in MCAD+/+ mice, but not in MCAD−/− mice (Figure 3). As a control analysis, anti–short-chain acyl-CoA dehydrogenase (SCAD) antisera revealed no differences in levels of expression of SCAD protein between MCAD+/+ and MCAD−/− mice (Figure 3).\nFigure 3 Immunoblots of Liver Homogenates from MCAD+/+ and MCAD−/− Mice\nThese were probed with anti-MCAD antibody or anti-SCAD antibody. Homozygous MCAD−/− mice had no detectable MCAD protein. MCAD protein is only detectable under the MCAD protein–spiked (positive control) lane. As a control analysis, liver homogenates probed with anti-SCAD antibody revealed that SCAD protein was present in both MCAD+/+ and MCAD−/− mice. No MCAD positive-control protein is detected by anti-SCAD antibodies (MCAD lane). mw, molecular weight standards. Enzyme activity was analyzed in mouse liver homogenates using the electron transport flavoprotein (ETF) reduction assay with octanoyl-CoA (C8:0) and palmitoyl-CoA (C16:0) as substrates. MCAD−/− mice had a significant reduction in ability to dehydrogenate octanoyl-CoA and a modest reduction in activity toward palmitoyl-CoA compared to MCAD+/+ mice (Table 1). Specifically, the dehydrogenation of octanoyl-CoA and palmitoyl-CoA substrates were reduced by 75% and by 30%, respectively, in MCAD−/− mice as compared to MCAD+/+ controls.\nTable 1 Characteristics of MCAD-Deficient Mice\nValues given are mean ± SD.\naMCAD+/+ n = 5 and MCAD−/− n = 5.\nbMCAD+/+ n = 8 litters and MCAD−/− n = 10 litters.\ncMCAD+/+ n = 5 and MCAD−/− n = 6.\ndMCAD+/+ n = 4 and MCAD−/− n = 5.\neExpressed as a ratio relative to the internal standard.\n\nNeonatal Deaths\nSignificant neonatal mortality was noted in MCAD−/− pups. Although equal numbers of pups were born from MCAD+/+ and MCAD−/− mice, only 41% of MCAD−/− mice survived to weaning as compared to 98% of MCAD+/+ mice (Table 1). The mechanism of neonatal loss remains undetermined. The MCAD−/− pups are abandoned more frequently than MCAD+/+ pups for unknown reasons. They are likely more prone to hypothermia than MCAD+/+. Because of the difficulty of distinguishing the MCAD−/− mutants from the MCAD+/− heterozygous pups by molecular analysis due to the insertion mutation, we could only compare MCAD+/+ × MCAD+/+ matings with MCAD−/− × MCAD−/− matings. Thus, we were unable to evaluate the pedigrees from heterozygous matings.\n\nFasting and Cold Intolerance\nIn order to examine the stress effects of fasting on MCAD-deficient mice, they were fasted for 24 h prior to analysis. MCAD−/− mice displayed lower serum glucose and elevated serum free fatty acid levels although neither result was significant, as compared to MCAD+/+ mice (Table 1).\nTo determine the effects of cold stress, mice were fasted for 18 h and placed in 4 °C environment for a 3-h period. The MCAD−/− mice were significantly compromised within this short period of cold stress, some severe enough to result in fatalities. After 1 h of the cold challenge, the average rectal temperature of MCAD−/− mice (n = 5) was 23.4 °C as compared with 35 °C for MCAD+/+ mice (n = 4). Rectal temperatures declined to unrecoverable temperatures of 16.7–19.2 °C in three of the five MCAD−/− mice. By the end of the 1.5-h mark, the two surviving MCAD−/− mice averaged 22.7 °C. In contrast, all four MCAD+/+ mice survived the 3-h cold stress, ending with an average rectal temperature of 33.6 °C.\n\nOrganic Acid and Acylcarnitine Analysis\nUrine organic acid analysis revealed that MCAD−/− mice developed an organic acid profile similar to MCAD-deficient human patients. Specifically, when fasted for 18 h, MCAD−/− mice developed significantly elevated concentrations of adipic, suberic, and sebacic acids and hexanoylglycine as compared to MCAD+/+ controls, which showed trace to no detectable amounts of the same organic acids (Table 1). Adipic acid is not specific to MCAD deficiency. We also evaluated β-hydroxybutyric and acetoacetic concentrations and found no significant differences between MCAD genotypes (data not shown).\nComparison of MCAD+/+ and MCAD−/− mice revealed no significant differences in total serum carnitine concentrations between MCAD+/+ and MCAD−/− mice, but MCAD−/− mice had a 5- to 6-fold elevation of serum decenoylcarnitine evident in the acylcarnitine profile (Figure 4A). Bile acylcarnitine analysis revealed a similar acylcarnitine pattern as in serum (Figure 4B). However, the acylcarnitine profiles of the MCAD−/− mice are different from those of human MCAD-deficient patients (Figure 4C). Human patients present with elevated levels of C6, C8, and C10:1 acylcarnitines, as did the mutant mice; however, the predominant peak was C8 acylcarnitine in humans, whereas in the mouse it was C10:1 acylcarnitine.\nFigure 4 Acylcarnitine Analyses\n(A) Serum acylcarnitine analysis of MCAD+/+ (n = 4) and MCAD−/− mice (n = 4)\nThere are significant elevations in acylcarnitine species as indicated in MCAD−/− mice. Values shown are mean values ± standard deviation (SD). Asterisk indicates p \u003c 0.002 and ‡ indicates p \u003c 0.01.\n(B) There are significant elevations in bile acylcarnitines of the same mice shown in (A) as indicated. Values shown are mean values ± SD. Asterisk indicates p \u003c 0.001.\n(C) Bile acylcarnitine profile of an MCAD−/− mouse compared to a human patient with MCAD deficiency. Internal standards are indicated by an asterisk.\n\nHistopathology\nComplete histopathologic examination of one group of mutant and MCAD+/+ control mice after a 24-h fast demonstrated diffuse microvesicular and macrovesicular hepatic steatosis in 6–8-wk-old MCAD−/− mice whereas MCAD+/+ mice had no histologic changes (Figure 5A and 5B). In another group of 4-wk-old MCAD+/+ and MCAD−/− mice fasted for 24-h, there were minimal to no abnormalities in all organs evaluated. Only the older MCAD−/− mice, therefore, demonstrated hepatic steatosis. In addition, we found sporadic cardiac lesions in multiple MCAD−/− mice.\nFigure 5 Histopathology of MCAD+/+ and MCAD−/− Mice\n(A) MCAD+/+ mice had no evidence of hepatic steatosis following a 24-h fast. Liver section with Oil-Red O stain.\n(B) Hepatosteatosis in MCAD−/− mouse following a 24-h fast. Oil-Red O stained liver sections revealed severe and diffuse microvesicular and macrovesicular hepatic steatosis in MCAD−/− mice.\n(C and D) Diffuse cardiomyopathy with chronic active multifocal myocyte degeneration and necrosis in MCAD−/− mice. In one example, an MCAD−/− mouse had diffuse cardiomyopathy with chronic active multifocal myocyte degeneration and necrosis (Figure 5C and 5D). Changes in degenerating myocytes included swelling, pale staining, and, in portions of the sarcoplasm, replacement of myofibrils with finely granular eosinophilic material. Nuclei of affected myocytes were large, pale, and vesicular and had prominent nucleoli. In the most severely affected areas, there was loss of myocytes accompanied by fibrosis. In the wall of the aorta at the base of the heart there was multifocal degeneration of the elastic tissue, accompanied by multifocal collections of globular translucent yellow-brown pigment interpreted to be ceroid/lipofuscin. Similar deposits were scattered within adjacent adipose 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