کد مقاله | کد نشریه | سال انتشار | مقاله انگلیسی | نسخه تمام متن |
---|---|---|---|---|
1950123 | 1537814 | 2007 | 15 صفحه PDF | دانلود رایگان |
عنوان انگلیسی مقاله ISI
Hydrolysis of minor glycerophospholipids of plasma lipoproteins by human group IIA, V and X secretory phospholipases A2
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کلمات کلیدی
HDLPLA2sPLA2PtdSerPtdInsGlcPtdChoIn vitro incubationLysoPtdChoCAPEXglycerophosphoserineCIDGroPChoPtdGroBSA - BSALC/ESI-MS - LC / ESI-MSPtdEtn - PtDEtnbovine serum albumin - آلبومین سرم گاوphospholipase A2 - آنزیم فسفولیپاز A2 secretory PLA2 - ترشح PLA2collision induced dissociation - تقارن ناشی از برخوردphosphatidylinositol - فسفاتیدیل اینوزیتولphosphatidylcholine - فسفاتیدیل کولینphosphatidylglycerol - فسفاتیدیل گلیسرولphosphatidylethanolamine - فسفاتیدیلتانولامینPhosphatidylserine - فسفاتیدیلسرینLysophosphatidylcholine - لیزوفسفاتیدیل کولینhigh density lipoprotein - لیپوپروتئین با چگالی بالاlow density lipoprotein - لیپوپروتئین چگالی کمLDL - لیپوپروتئین کم چگالی(کلسترول بد)Cardiolipin - کاردیولیپینhigh performance liquid chromatography - کروماتوگرافی مایع با کارایی بالاHPLC - کروماتوگرافی مایعی کاراgas–liquid chromatography - کروماتوگرافی گاز مایعglycerophosphoethanolamine - گلیسروفسفاتانولامینglycerophosphocholine - گلیسروفسفوکولینglycerophosphoglycerol - گلیسروفسفوگلیسیرین
موضوعات مرتبط
علوم زیستی و بیوفناوری
بیوشیمی، ژنتیک و زیست شناسی مولکولی
زیست شیمی
پیش نمایش صفحه اول مقاله
چکیده انگلیسی
We investigated the hydrolysis of the minor glycerophospholipids of human HDL3, total HDL and LDL using human group IIA, V and X secretory phospholipases A2 (sPLA2s). For this purpose we employed the enzyme and substrate concentrations and incubation times optimized for hydrolysis of phosphatidylcholine (PtdCho), the major glycerophospholipid of plasma lipoproteins. In contrast to PtdCho, which was readily hydrolyzed by group V and X sPLA2s, and to a lesser extent by group IIA sPLA2, the minor ethanolamine, inositol and serine glycerophospholipids exhibited marked resistance to hydrolysis by all three sPLA2s. Thus, when PtdCho was hydrolyzed about 80%, the ethanolamine and inositol glycerophospholipids reached a maximum of 40% hydrolysis. The hydrolysis of phosphatidylserine (PtdSer), which was examined to a more limited extent, showed similar resistance to group IIA, V and X sPLA2s, although the group V sPLA2 attacked it more readily than group X sPLA2 (52% versus 39% hydrolysis, respectively). Surprisingly, the group IIA sPLA2 hydrolysis remained minimal at 10-15% for all minor glycerophospholipids, and was of the order seen for the PtdCho hydrolysis by group IIA sPLA2 at the 4-h digestion time. All three enzymes attacked the oligo- and polyenoic species in proportion to their mole percentage in the lipoproteins, although there were exceptions. There was evidence of a more rapid destruction of the palmitoyl compared to the stearoyl arachidonoyl glycerophospholipids. Overall, the characteristics of hydrolysis of the molecular species of the lipoprotein-bound diradyl GroPEtn, GroPIns and GroPSer by group V and X sPLA2s differed significantly from those observed with lipoprotein-bound PtdCho. As a result, the acidic inositol and serine glycerophospholipids accumulated in the digestion residues of both LDL and HDL, and presumably increased the acidity of the residual particles. An accumulation of the ethanolamine glycerophospholipids in the sPLA2 digestion residues also had not been previously reported. These results further emphasize the diversity in the enzymatic activity of the group IIA, V and X sPLA2s. Since these sPLA2s possess comparable tissue distribution, their combined activity may exacerbate their known proinflammatory and proatherosclerotic function.
ناشر
Database: Elsevier - ScienceDirect (ساینس دایرکت)
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1771, Issue 1, January 2007, Pages 5-19
Journal: Biochimica et Biophysica Acta (BBA) - Molecular and Cell Biology of Lipids - Volume 1771, Issue 1, January 2007, Pages 5-19
نویسندگان
W. Pruzanski, G. Lambeau, M. Lazdunski, W. Cho, J. Kopilov, A. Kuksis,