Apolipoprotein B-Containing Lipoprotein Particles in Progressive Renal Insufficiency

2015 ◽  
pp. 11-19 ◽  
Author(s):  
Per-Ola Attman ◽  
Marcelo Tavella ◽  
Carolyn Knight-Gibson ◽  
Ola Samuelsson ◽  
Petar Alaupovic
Keyword(s):  
Renal Insufficiency ◽  
Apolipoprotein B ◽  
Lipoprotein Particles ◽  
Progressive Renal Insufficiency

Relationship between Amphipathic β Structures in the β1Domain of Apolipoprotein B and the Properties of the Secreted Lipoprotein Particles in McA-RH7777 Cells

Biochemistry ◽  
2017 ◽  
Vol 56 (31) ◽  
pp. 4084-4094
Author(s):  
Medha Manchekar ◽  
Richa Kapil ◽  
Zhihuan Sun ◽  
Jere P. Segrest ◽  
Nassrin Dashti
Keyword(s):  
Apolipoprotein B ◽  
Lipoprotein Particles

Apolipoprotein-B-Containing Lipoproteins and the Progression of Renal Insufficiency

Nephron ◽  
1993 ◽  
Vol 63 (3) ◽  
pp. 279-285 ◽  
Author(s):  
Ola Samuelsson ◽  
Mattias Aurell ◽  
Carolyn Knight-Gibson ◽  
Petar Alaupovic ◽  
Per-Ola Attman
Keyword(s):  
Renal Insufficiency ◽  
Apolipoprotein B

scholarly journals Palmitoylation of Apolipoprotein B Is Required for Proper Intracellular Sorting and Transport of Cholesteroyl Esters and Triglycerides

2000 ◽  
Vol 11 (2) ◽  
pp. 721-734 ◽  
Author(s):  
Yang Zhao ◽  
James B. McCabe ◽  
Jean Vance ◽  
Luc G. Berthiaume
Keyword(s):  
Apolipoprotein B ◽  
Neutral Lipids ◽  
Low Density Lipoproteins ◽  
Low Density ◽  
Hydrophobic Core ◽  
Wild Type ◽  
Very Low Density Lipoproteins ◽  
Structural Requirement ◽  
Lipoprotein Particles ◽  
Intracellular Sorting

Apolipoprotein B (apoB) is an essential component of chylomicrons, very low density lipoproteins, and low density lipoproteins. ApoB is a palmitoylated protein. To investigate the role of palmitoylation in lipoprotein function, a palmitoylation site was mapped to Cys-1085 and removed by mutagenesis. Secreted lipoprotein particles formed by nonpalmitoylated apoB were smaller and denser and failed to assemble a proper hydrophobic core. Indeed, the relative concentrations of nonpolar lipids were three to four times lower in lipoprotein particles containing mutant apoB compared with those containing wild-type apoB, whereas levels of polar lipids isolated from wild-type or mutant apoB lipoprotein particles appeared identical. Palmitoylation localized apoB to large vesicular structures corresponding to a subcompartment of the endoplasmic reticulum, where addition of neutral lipids was postulated to occur. In contrast, nonpalmitoylated apoB was concentrated in a dense perinuclear area corresponding to the Golgi compartment. The involvement of palmitoylation as a structural requirement for proper assembly of the hydrophobic core of the lipoprotein particle and its intracellular sorting represent novel roles for this posttranslational modification.

A 66-year-old woman with progressive renal insufficiency, nephrotic syndrome, and monoclonal protein

2003 ◽  
Vol 41 (2) ◽  
pp. 508-517 ◽  
Author(s):  
Ingrid J. Chang ◽  
Boonyarit Cheunsuchon ◽  
Frank J. Miller ◽  
Agnes B. Fogo
Keyword(s):  
Nephrotic Syndrome ◽  
Renal Insufficiency ◽  
Monoclonal Protein ◽  
Progressive Renal Insufficiency

scholarly journals Environmental Lead Exposure and Progressive Renal Insufficiency

2001 ◽  
Vol 161 (2) ◽  
pp. 264 ◽  
Author(s):  
Ja-Liang Lin ◽  
Dan-Tzu Tan ◽  
Kuan-Huang Hsu ◽  
Chun-Chen Yu
Keyword(s):  
Renal Insufficiency ◽  
Lead Exposure ◽  
Environmental Lead ◽  
Environmental Lead Exposure ◽  
Progressive Renal Insufficiency

Abnormal concentrations of CII, CIII, and E apolipoproteins among apolipoprotein B-containing, B-free, and A-I-containing lipoprotein particles in hemodialysis patients

1991 ◽  
Vol 37 (3) ◽  
pp. 387-393 ◽  
Author(s):  
Naji Alsayed ◽  
RegIs Rebourcet
Keyword(s):  
Total Cholesterol ◽  
Apolipoprotein B ◽  
Marked Decrease ◽  
Hemodialysis Patients ◽  
Serum Concentrations ◽  
Dialysis Patients ◽  
Apo B ◽  
Lipoprotein Particles ◽  
Apo E ◽  
Anephric Patients

Abstract Serum concentrations of total cholesterol, triglycerides, and apolipoproteins (apo) A-I, B, CII, CIII, and E in 36 hemodialysis patients and nine anephric patients were compared with the concentrations in 34 normolipidemic subjects. The dialysis patients displayed a moderate hypertriglyceridemia (1.94 +/- 0.12 vs 1.09 +/- 0.11 mmol/L in controls, mean +/- SEM; P less than 0.001), apo CIII concentrations were also increased (130.2 +/- 2.1 vs 108.4 +/- 0.7 mg/L; P less than 0.001), whereas apo CII (34.5 +/- 0.5 vs 36 +/- 0.5 mg/L; P less than 0.05), apo E (22.7 +/- 0.3 vs 27.9 +/- 0.2 mg/L; P less than 0.001), and apo A-I (1.18 +/- 0.05 vs 1.31 +/- 0.04 g/L; P less than 0.05) were decreased. Concentrations of serum apo B were normal (0.86 +/- 0.03 vs 0.97 +/- 0.07 g/L). In the hemodialysis patients, apo CIII concentrations were increased in apo B-containing lipoproteins (30.1 +/- 0.5 vs 25.0 +/- 0.1 mg/L; P less than 0.001), whereas CII and E were decreased below control values (14.4 +/- 0.2 vs 16.8 +/- 0.1, and 8.2 +/- 0.2 vs 11.4 +/- 0.1 mg/L, respectively; P less than 0.001 each). By calculation, non-B-containing lipoproteins in the hemodialysis group had increased concentrations of apo CIII (100.1 +/- 2.1 vs 83.3 +/- 0.7 mg/L; P less than 0.001) and decreased amounts of apo E (14.5 +/- 0.4 vs 16.4 +/- 0.3 mg/L; P less than 0.001); apo CII content was unchanged (20.1 +/- 0.5 vs 19.3 +/- 0.5 mg/L). Results for apo CII, CIII, and E among apo A-I-containing lipoproteins in both normolipidemic and hemodialysis groups were similar to those in non-B-containing lipoproteins. Finally, the sole significant (P less than 0.01) difference between the anephric and hemodialysis groups was the lower apo E concentrations in the former group. Accumulation of triglyceride-rich lipoproteins in hemodialysis patients may thus be related to the enrichment of apo CIII in apo B-containing lipoproteins and to a marked decrease in the apo CII and E contents.

scholarly journals A role for palmitoylation in the quality control, assembly and secretion of apolipoprotein B

2004 ◽  
Vol 377 (1) ◽  
pp. 121-130 ◽  
Author(s):  
Gonzalo L. VILAS ◽  
Luc G. BERTHIAUME
Keyword(s):  
Quality Control ◽  
Apolipoprotein B ◽  
Neutral Lipids ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Low Density ◽  
Wild Type ◽  
Er Quality Control ◽  
Lipoprotein Particles ◽  
Secretion Efficiency

ApoB (apolipoprotein B)-containing lipoprotein particles, such as chylomicrons, very-low-density and low-density lipoprotein particles, transport triacylglycerol and cholesteryl esters in the bloodstream. A palmitoylation site was previously mapped to Cys-1085 in a functional truncated apoB variant (apoB-29) and abolished by mutagenesis. This Cys-1085Ser mutation resulted in secretion of smaller and denser lipoprotein particles containing 80% less cholesteryl ester and triacylglycerol than wild-type controls. We show that palmitoylation of apoB-29 occurs in the ER (endoplasmic reticulum), stimulates the ER–Golgi transport rate of apoB-29 almost 2-fold, doubles the secretion efficiency of wild-type apoB-29 in comparison with (Cys-1085Ser)apoB-29 and reduces significantly the association of wild-type apoB-29 with calnexin in comparison with (Cys-1085Ser)apoB-29. While non-palmitoylated apoB-29 co-localized extensively with constitutively secreted transferrin, wild-type apoB-29 did so only partially and was enriched in ER extensions. Our results suggest that palmitoylation of apoB regulates the biogenesis of nascent apoB-containing lipoprotein particles by concentrating apoB in a specialized ER compartment and by stimulating dissociation from constituents of the ER quality-control machinery. This reduced interaction would lead to a faster ER–Golgi transit time and a higher secretion efficiency of wild-type apoB-29. Palmitoylation could regulate the amount of apoB available for secretion of neutral lipids.

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