Phosphorus Assay in Column Chromatography

Bartlett, Grant R.

doi:10.1016/s0021-9258(18)70226-3

Cited by 12,371 publications

(981 citation statements)

References 6 publications

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“…The serum, liver and cortical total phospholipids were estimated by the method of Barlett. 13 The protein concentration in serum or tissue homogenate was determined by the method of Lowery et al 14…”

Section: Biochemical Assaysmentioning

confidence: 99%

Effect of spironolactone on cisplatininduced nephrotoxicity in rabbits

2001

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The effects of a single interaperitoneal dose of cisplatin (6.5 mg kg day 1), oral doses of spironolactone (20.0 mg kg 1) for 5 days or the combined treatment (spironolactone+cisplatin) on the kidney function and liver function parameters, as well as the serum, liver and kidney cortical lipid contents were studied. The serum urea and creatinine concentrations (measured as kidney function parameters) were not altered by spironolactone treatment, but were significantly (P<0.001) elevated by cisplatin administration. However, animals exposed to both spironolactone+ cisplatin revealed drastic increases in the serum creatinine and urea concentrations amounting to about four and twofold those of cisplatin-alone treated animals, respectively. The histological examination of slides of kidneys from animals exposed to the combined drugs exhibited more extensive necrosis in the tubules compared to those from animals treated with cisplatin alone. Non of the drug treatments had any effects on the serum alanine transaminase (ALT) and aspartate transaminase (AST) levels (measured as liver function parameters) or liver protein content or hepatic alkaline phosphatase (ALP) activity. The histological examination also revealed apparently normal livers in all experimental groups. The cisplatin-induced nephrotoxicity was accompanied by hypercholesterolaemia and hyperphospholipidaemia, whereas spiro nolactone showed a hypocholesterolaemic effect. The concomitant treatment with both cisplatin and spiro nolactone significantly (P<0.05) raised the serum triacylglycerol (TAG) concentration compared to the cisplatin-alone-treated group. Both spironolactone and cisplatin administered separately or jointly caused accumulation of cholesterol and TAG in the kidney cortex with significant depletion of the liver cholesterol content. The present results indicated that spironolactone aggravates the cisplatin-induced nephrotoxicity in the rabbit.

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Section: Biochemical Assaysmentioning

confidence: 99%

Effect of spironolactone on cisplatininduced nephrotoxicity in rabbits

2001

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“…LDL protein was measured according to Lowry et al (27) and phospholipid by Bartlett's method (28). Total and unesterified cholesterol, as well as triglyceride, were determined by enzymatic kits: Boehringer Mannheim #236691, #310378 and #877557, respectively.…”

Section: Ldl Compositionmentioning

confidence: 99%

Small dense low density lipoprotein has increased affinity for LDL receptor-independent cell surface binding sites: a potential mechanism for increased atherogenicity

Galeano

Al-Haideri

Keyserman

et al. 1998

Journal of Lipid Research

183

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Small dense low density lipoprotein (LDL) particles have altered apolipoprotein (apo) B conformation and lowered affinity for the LDL receptor ( J. Biol. Chem. 1994. 269: 511-519). Herein, we examine the interaction of small dense LDL with cell LDL receptor-independent binding sites. Compared to normal LDL, at low LDL cell media concentrations ( Ͻ 10 g/ml), small dense LDL had decreased specific binding to the LDL receptor on normal fibroblasts at 4 Њ C, but a 2-fold increased binding to LDL receptor-independent cell sites. At higher LDL concentration (100 g/ ml), LDL receptor-independent binding of small dense LDL was 4.5-fold that of normal LDL in normal fibroblasts, but greater (2-to 14-fold) in LDL receptor-negative fibroblasts. In LDL receptor-negative fibroblasts at 37 ؇ C, small dense LDL had higher (3-fold) cell association than normal size LDL but no effective LDL degradation. At high LDL concentrations ( Ն 100 g/ml), LDL binding to normal or LDL receptor-negative fibroblasts was not affected by several anti-apoB monoclonal antibodies or by cell pretreatment with proteases, chondroitinase, or neuraminidase. In contrast, pretreating normal and receptor-negative fibroblasts with heparinase and heparitinase decreased LDL cell binding by 35% and 50%, respectively. Similarly, preincubation of receptor-negative fibroblasts with sodium chlorate, an inhibitor of proteoglycan sulfation, decreased LDL binding by about 45%. We hypothesize that small dense LDL might be more atherogenic than normal size LDL due to decreased hepatic clearance by the LDL receptor, and enhanced anchoring to LDL receptor-independent binding sites in extrahepatic tissues (e.g., the arterial wall), a process mediated, in part, by cell surface proteoglycans.-Galeano, N. F., M. Al-Haideri, F. Keyserman, S. C. Rumsey, and R. J. Deckelbaum. Small dense low density lipoprotein has increased affinity for LDL receptor-independent cell surface binding sites: a potential mechanism for increased atherogenicity.

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“…The composition of the isolated emulsions was determined by two alternative methods: a ) liquid scintillation spectrometry of the lipids obtained after their separation by thin-layer chromatography (43), and b ) colorimetric assays of TAG (46), cholesterol (47), and PC, determined as inorganic phosphate (48). The size of the isolated emulsions was estimated both according to the method described by Miller and Small (42) and by negativestain electron microscopy after osmium fixation (41,43).…”

Section: Methodsmentioning

confidence: 99%

The N-terminal 17% of apoB binds tightly and irreversibly to emulsions modeling nascent very low density lipoproteins

Herscovitz

Derksen

Walsh

et al. 2001

Journal of Lipid Research

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The N-terminal 17% of apolipoprotein B (apoB-17) readily associates with dimyristoylphosphatidylcholine (DMPC) multilamellar vesicles (MLV) to form large (240-Å diameter) discoidal particles. Because apoB is normally secreted with triacylglycerol (TAG)-rich lipoproteins, we studied the binding of apoB-17 to triolein-rich emulsions modeling nascent TAG-rich very low density-like lipoproteins. Emulsions with the following composition (by weight) were prepared: 85-89% triolein, 1.1-1.4% cholesterol, and 10-14% phosphatidylcholines (PC) including either egg yolk (EY)-, dimyristoyl (DM)-, or dipalmitoyl (DP)-PC representing (at 25 Њ C), respectively, a fluid surface, a surface at transition, and a mainly solid surface. The respective sizes were 1,260 ؎ 500, 1,070 ؎ 450, and 830 ؎ 300 Å mean diameter. The emulsions were incubated with conditioned medium containing apoB-17, and then reisolated by ultracentrifugation. Analysis of the emulsion-bound proteins by gel electrophoresis showed that all three emulsions bound primarily apoB-17. The DPPC emulsions bound more apoB-17 than EYPC or DMPC emulsions. Immunoaffinitypurified apoB-17 exhibited saturable, high affinity binding to EYPC and DPPC emulsions. The respective K d values were 32 Ϯ 23 and 85 Ϯ 27 nM and capacities (N) were 10 and 58 molecules of apoB-17 per particle. When apoB-17 bound to emulsions was incubated with DMPC MLV at 26 Њ C for 18 h, it remained bound to the emulsions, indicating that once bound to these emulsions it is unable to exchange off and solubilize DMPC into discs. In contrast, apoE-3 bound to emulsions dissociated from the emulsions when incubated with DMPC MLV and formed discs. Thus, apoB-17 binds strongly and irreversibly to emulsions modeling nascent lipoproteins. It therefore may play an important role in the stabilization of nascent VLDL and chylomicrons. -Herscovitz, H.

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Phosphorus Assay in Column Chromatography

Cited by 12,371 publications

References 6 publications

Effect of spironolactone on cisplatininduced nephrotoxicity in rabbits

Effect of spironolactone on cisplatininduced nephrotoxicity in rabbits

Small dense low density lipoprotein has increased affinity for LDL receptor-independent cell surface binding sites: a potential mechanism for increased atherogenicity

The N-terminal 17% of apoB binds tightly and irreversibly to emulsions modeling nascent very low density lipoproteins

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