Effect of carbonyl cyanide m-chlorophenylhydrazone (CCCP) on the dimerization of lipoprotein lipase

Park, Jin-Woo; Lee, Sam-Yeol; Yang, Jeong‐Yeh; Rho, Hye-Won; Park, Byung‐Hyun; Lim, Seong-Nam; Kim, Jong‐Suk; Kim, Hyung-Rho

doi:10.1016/s0005-2760(96)00146-4

Cited by 30 publications

(23 citation statements)

References 39 publications

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“…Culture of 3T3-L1 cells The 3T3-L1 cells that were obtained from the American Type Culture Collection (ATCC CCL 92.1) were grown to confluence in 24-well culture plates with a standard medium (DMEM containing 10% fetal bovine serum, 100 U/ml penicillin, 0.1 mg/ml streptomycin, and 0.25 µg/ml amphotericin B), as described by Park et al (1997). Confluent cells were stimulated to differentiate into adipocytes by supplementing the standard medium with 1 µM dexamethasone, 10 µg/ml insulin, and 0.5 mM isobutylmethylxanthine for 2 days.…”

Section: Methodsmentioning

confidence: 99%

“…At the end of experiment, the cells were rinsed with ice-cold phosphate-buffered saline (PBS), harvested with 0.5 ml of a MNT-buffer (20 mM 2-(N-morpholino) ethanesulfonic acid, 100 mM NaCl, 30 mM Tris-HCl, and 1 mM CaCl 2 , pH 7.6) that contained 1% Triton X-100, and sonicated briefly at 4 o C. The suspension was centrifuged at 15,000 × g for 20 min at 4 o C, and LPL activity in the infranatant was measured, as described by Park et al (1997). Secreted LPL activity was determined from the medium.…”

Section: Assay Of Lpl Activitymentioning

confidence: 99%

“…An aliquot of the supernatant was treated with endo-β-Nacetylglucosaminidase H (endo H, Sigma Chemical Co. St. Louis, USA) as described previously (Park et al, 1997). Then 50 µl of the supernatant was mixed with 5 µl of 2% mercaptoethanol in 1 M sodium citrate (pH 5.5), 5 µl of protease inhibitor mix (1 mg/ml aprotinin, 1 mg/ml leupeptin, 1 mg/ml antipain, and 10 mg/ml benzamide), and 3 µl of 1 unit/ml endo H. After incubation at 37 o C for 24 h, the reaction was stopped by the addition of an electrophoresis sample buffer (62.5 mM Tris-HCl, 2% SDS, 5% 2-mercaptoethanol, 10% glycerol, 0.001% bromophenol blue, pH 6.8), and boiled for 5 min.…”

Section: Endoglycosidase H Treatment and Immunoblotting Of Lplmentioning

confidence: 99%

“…The production of active LPL by cells involves the following: the synthesis and N-linked glycosylation of lipase subunits in endoplasmic reticulum (ER), processing of oligosaccharide chains to make them endoglycosidase Hresistant through ER and Golgi, dimerization of subunits, development of high affinity for heparin, acquisition of catalytic activity, and secretion (Masuno et al, 1991;Braun and Severson, 1992;Park et al, 1995;Park et al, 1996a;Park et al, 1997;Park, 2001). LPL in mouse adipocytes has two Nlinked oligosaccharide chains per subunit (Vannier and Ailhaud, 1989).…”

Section: Introductionmentioning

confidence: 99%

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Effect of Nordihydroguaiaretic Acid on the Secretion of Lipoprotein Lipase

Kim

Park²,

Park³

2002

BMB Reports

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Nordihydroguaiaretic acid (NDGA), an inhibitor of lipoxygenase, inhibits the secretion of proteins and causes the redistribution of resident Golgi proteins into the endoplasmic reticulum (ER). In this study, the effect of NDGA on lipoprotein lipase (LPL) secretion was investigated in 3T3-L1 adipocytes, and compared with those of brefeldin A (BFA), a well-known fungal metabolite that exhibits similar ER-Golgi redistribution. Both BFA and NDGA blocked secretions of LPL. In the presence of BFA, the active and dimeric LPL was accumulated in adipocytes. After endoglycosidase H (endo H) digestion, the proportion of LPL subunits with partially endo Hsensitive oligosaccharide was significantly increased with BFA. However, in the presence of NDGA, the cellular LPL became inactive, and only the endo H-sensitive fraction of the LPL subunit was observed. An increase of the aggregated forms was observed in the fractions of the sucrose-density gradient ultracentrifugation. These properties of LPL in the NDGA-treated cells were similar to those of LPL that is retained in ER, and the effects of NDGA could not be reversed by BFA. These results indicate that the inhibitory mechanism of NDGA on the LPL secretion is functionally different from the ER-Golgi redistribution that is induced by BFA.

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Section: Methodsmentioning

confidence: 99%

Section: Assay Of Lpl Activitymentioning

confidence: 99%

Section: Endoglycosidase H Treatment and Immunoblotting Of Lplmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Effect of Nordihydroguaiaretic Acid on the Secretion of Lipoprotein Lipase

Kim

Park²,

Park³

2002

BMB Reports

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“…At the end of the experiment, medium was harvested, and the secreted LPL activity was determined as described previously (21). A stock triacylglycerol emulsion containing 5 mCi of tri[9,10(n)-3 H]oleoylglycerol (Amersham, Buckinghamshire, UK), 1.13 mmole of trioleoylglycerol, 60 mg of 1-α-phosphatidylcholine (bovine liver) and 9 ml of glycerol was prepared according to the method of NilssonEhle and Schotz (22).…”

Section: Methodsmentioning

confidence: 99%

Effect of scopoletin on lipoprotein lipase activity in 3T3-L1 adipocytes

Yang

Koo²,

Yoon³

et al. 2007

Int J Mol Med

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Abstract. Hypertriglyceridemia is an independent risk factor of cardiovascular diseases. It is caused by the imbalance between hepatic triglyceride production and peripheral removal. Lipoprotein lipase (LPL) plays a central role in the removal of plasma triglyceride. During the screening of possible anti-dyslipidemic drugs, we observed that scopoletin (6-methoxy-7-hydroxycoumarin) significantly increased LPL activity in adipocytes. Scopoletin increased LPL activity in culture medium of 3T3-L1 adipocytes in dose-and timedependent manners. It did not release LPL from the adipocyte membrane and, instead, increased the LPL mRNA level, suggesting transcriptional control. Scopoletin also partially reversed tumor necrosis factor-α-induced suppression of LPL activity. These results suggest the possible action of scopoletin as a facilitator of plasma triglyceride clearance.

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Microenvironment‐Induced In Situ Self‐Assembly of Polymer–Peptide Conjugates That Attack Solid Tumors Deeply

Gao

et al. 2019

Angewandte Chemie

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In cancer treatment, the unsatisfactory solid-tumor penetration of nanomaterials limits their therapeutic efficacy. We employed an in vivo self-assembly strategy and designed polymer-peptide conjugates (PPCs) that underwent an acidinduced hydrophobicity increase with an arrowp H-response range (from 7.4 to 6.5). In situ self-assembly in the tumor microenvironment at appropriate molecular concentrations (around the IC 50 values of PPCs) enabled drug delivery deeper into the tumor.Acytotoxic peptide KLAK, decorated with the pH-sensitive moiety cis-aconitic anhydride (CAA), and acellpenetrating peptide TATw ere conjugated onto poly(b-thioester) backbones to produce PT-K-CAA,w hich can penetrate deeply into solid tumors owing to its small sizea sas ingle chain. During penetration in vivo,C AA responds to the weak acid, leading to the self-assembly of PPCs and the recovery of therapeutic activity.T herefore,adeep-penetration ability for enhanced cancer therapyi sp rovided by this in vivo assembly strategy.

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Effect of carbonyl cyanide m-chlorophenylhydrazone (CCCP) on the dimerization of lipoprotein lipase

Cited by 30 publications

References 39 publications

Effect of Nordihydroguaiaretic Acid on the Secretion of Lipoprotein Lipase

Effect of Nordihydroguaiaretic Acid on the Secretion of Lipoprotein Lipase

Effect of scopoletin on lipoprotein lipase activity in 3T3-L1 adipocytes

Microenvironment‐Induced In Situ Self‐Assembly of Polymer–Peptide Conjugates That Attack Solid Tumors Deeply

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