Abstract:
:The effect of fatty acid binding proteins (FABPs) on two key steps of microsomal phosphatidic acid formation was examined. Rat liver microsomes were purified by size-exclusion chromatography to remove endogenous cytosolic fatty acid and fatty acyl-CoA binding proteins while recombinant FABPs were used to avoid cross-contamination with such proteins from native tissue. Neither rat liver (L-FABP) nor rat intestinal fatty acid binding protein (I-FABP) stimulated liver microsomal fatty acyl-CoA synthase. In contrast, L-FABP and I-FABP enhanced microsomal conversion of [14C]oleoyl-CoA and glycerol 3-phosphate to [14C]phosphatidic acid by 18- and 7-fold, respectively. The mechanism for this stimulation, especially by I-FABP, is not known. However, several observations presented here suggest that, like L-FABP, I-FABP may interact with fatty acyl-CoA and thereby stimulate enzyme activity. First, I-FABP decreased microsomal membrane-bound oleoyl-CoA. Second, oleoyl-CoA displaced I-FABP bound fluorescent fatty acid, cis-parinaric acid, with Ki of 5.3 microM and 1.1 sites. Third, oleoyl-CoA decreased I-FABP tryptophan fluorescence with a Kd of 4.2 microM. Fourth, oleoyl-CoA red shifted emission spectra of acrylodated I-FABP, a sensitive marker of I-FABP interactions with ligands. In summary, the results demonstrate for the first time that both L-FABP and I-FABP stimulate liver microsomal phosphatidic acid formation by enhancing synthesis of phosphatidate from fatty acyl-CoA and glycerol 3-phosphate.
journal_name
Arch Biochem Biophysjournal_title
Archives of biochemistry and biophysicsauthors
Jolly CA,Hubbell T,Behnke WD,Schroeder Fdoi
10.1006/abbi.1997.9957subject
Has Abstractpub_date
1997-05-01 00:00:00pages
112-21issue
1eissn
0003-9861issn
1096-0384pii
S0003-9861(97)99957-4journal_volume
341pub_type
杂志文章abstract::We have observed abnormally high membrane cholesterol levels and a subsequent deficiency of oxidative energy production in mitochondria from cultured Morris hepatoma cells (MH7777). Using cholesterol affinity chromatography and MALDI-TOF Mass Spectrometry, we have identified the voltage dependent anion channel (VDAC) ...
journal_title:Archives of biochemistry and biophysics
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doi:10.1006/abbi.1993.1410
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pub_type: 杂志文章
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更新日期:2012-12-01 00:00:00
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pub_type: 杂志文章
doi:10.1006/abbi.1995.1122
更新日期:1995-02-01 00:00:00
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pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
pub_type: 杂志文章
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pub_type: 杂志文章
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journal_title:Archives of biochemistry and biophysics
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更新日期:1991-12-01 00:00:00
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pub_type: 杂志文章
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