Developmental regulation of lipoprotein lipase in rats

Tavangar, Kamran; Murata, Yoshihiko; Patel, Shushma; Kalinyak, Judith E.; Pedersen, M. Elizabeth; Goers, John F.; Hoffman, Andrew R.; Kraemer, Fredric B.

doi:10.1152/ajpendo.1992.262.3.e330

Cited by 18 publications

(25 citation statements)

References 26 publications

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“…The reasons for this are unclear but may be due to different tissue preparations, incubation conditions, the presence of inhibitors, interfering substances, or the sensitivity ofour assays. In this regard, we have found immunoreactive LPL protein, but not activity, in the brains ofnewborn rats that declines to undetectable levels by 1 mo of age (9). In contrast, LPL mRNA could be detected in the brains of adult rats and neither diabetes nor insulin treatment of diabetic rats had any effect on brain LPL mRNA levels.…”

Section: Discussionmentioning

confidence: 67%

“…Total LPL activity was measured as previously described (9). Briefly, tissue samples were delipidated with acetone/ether and the acetone-ether powders were extracted into 100-200 M1 of5 mM sodium barbital, pH 7.5, 20% (vol/vol) glycerol and 0.1% Triton X-100, by a 30-min incubation at 4VC with intermittent vortexing.…”

Section: Methodsmentioning

confidence: 99%

“…Total cellular RNA was isolated from frozen tissue as previously described (9,11). All glassware and plasticware were autoclaved before use.…”

Section: Methodsmentioning

confidence: 99%

“…The specific activity of the probes was 1-7 X I08 cpm/Ag and probes were used within a day ofpreparation. Total LPL mRNA was quantitated by slot blot hybridization as previously described (9,11 (9,15). Briefly, aliquots of tissue extracts in buffer containing I M NaCl, 0.1% Triton X-100, 0.1% albumin, protease inhibitors, and Tris-HCl (pH 7.4) were added to 96-well microtiter plates which had been previously coated overnight with 100 Ml of affinity-purified chicken anti-LPL antibody (number 227 1-X 5400) in 0.1 M sodium carbonate, pH 9.3.…”

Section: Methodsmentioning

confidence: 99%

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Regulation of lipoprotein lipase in the diabetic rat.

Tavangar

Murata²,

Pedersen³

et al. 1992

J. Clin. Invest.

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Section: Discussionmentioning

confidence: 67%

Section: Methodsmentioning

confidence: 99%

“…Total cellular RNA was isolated from frozen tissue as previously described (9,11). All glassware and plasticware were autoclaved before use.…”

Section: Methodsmentioning

confidence: 99%

Section: Methodsmentioning

confidence: 99%

See 2 more Smart Citations

Regulation of lipoprotein lipase in the diabetic rat.

Tavangar

Murata²,

Pedersen³

et al. 1992

J. Clin. Invest.

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“…[5][6][7] LPL activity is regulated in a tissue-specific manner by dietary and hormonal factors that modulate the enzyme via transcriptional, posttranscriptional, and posttranslational mechanisms. 8 For example, with fasting, LPL activity decreases in adipose but increases in cardiac tissue; as a result, FFAs from circulating TGs are diverted away from storage to meet the metabolic demands of the heart. 1 Insulin causes LPL activity to increase 3-fold in adipose tissue but reduces LPL activity significantly in skeletal muscle.…”

mentioning

confidence: 99%

Localization of Lipoprotein Lipase in the Diabetic Heart

Sambandam

Abrahani

Pierre

et al. 1999

ATVB

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Abstract-Vascular endothelium-bound lipoprotein lipase (LPL) is rate limiting for free fatty acid (FFA) transport into tissues. In streptozotocin (STZ)-diabetic rats, we have previously demonstrated an increased heparin-releasable LPL activity from perfused hearts. Because heparin can traverse the endothelial barrier, conventional Langendorff retrograde perfusion of the heart with heparin could release LPL from both the capillary luminal and abluminal surfaces. To determine the precise location of the augmented LPL, a modified Langendorff retrograde perfusion was used to isolate the enzyme at the coronary lumen from that in the interstitial effluent. In response to heparin, a 4-fold increase in LPL activity and protein mass was observed in the coronary perfusate after 2 weeks of STZ diabetes. Release of LPL activity into the interstitial fluid of control hearts was slow but progressive, whereas in diabetic hearts, peak enzyme activity was observed within 1 to 2 minutes after heparin, followed by a gradual decline. Immunohistochemical studies of myocardial sections confirmed that the augmented LPL in diabetic hearts was mainly localized at the capillary endothelium. To study the acute effects of insulin on endothelial LPL activity, we examined rat hearts at various times after the onset of hyperglycemia. An increased heparin-releasable LPL activity in diabetic rats was demonstrated shortly (6 to 24 hours) after STZ injection or after withdrawal from exogenous insulin. Heparin-releasable coronary LPL activity was also increased after an overnight fast. These studies indicate that the intravascular heparin-releasable fraction of cardiac LPL activity is acutely regulated by short-term changes in insulin rather than glucose. Thus, during short periods (hours) of hypoinsulinemia, increased LPL activity at the capillary endothelium can increase the delivery of FFAs to the heart. The resultant metabolic changes could induce the subsequent cardiomyopathy that is observed in the chronic diabetic rat.

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Expression and activity of key lipases during the larval development of walking catfish (Clarias magur)

et al. 2019

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The study was conducted to investigate the expression and activity of key lipolytic enzymes during the ontogenetic development of Clarias magur. After partial characterization, the messenger RNA (mRNA) expression analysis of lipoprotein lipase (LPL), pancreatic triacylglycerol lipase (PL), and bile salt-activated lipase (BAL) genes along with the specific lipase activity were performed in larvae from Day 1 after hatching till 34-day posthatch (dph). Heterogeneous patterns of mRNA expression were shown by the important lipolytic enzymes and were detected before first exogenous feeding during the yolk-sac stage. LPL started increasing from 13 dph and peaked at 16 dph followed by a declining trend till 34 dph. However, the PL observed to be peaking at 9, 22, and 30 dph. Similarly, BAL showed an increasing trend from 11 to 22 dph with a significantly high level of mRNA expression at 16 dph. Later, the specific lipase activity was evaluated which appears at Day 1 after hatching with a progressive increase from 7 to 16 dph and a further declining trend afterwards with a peak at 22 dph. The results indicated the development of exocrine pancreas at 16 dph. Furthermore, the transcript levels and the activity of lipases were regulated with the age. Hence, the present study can be helpful in devising different strategies containing optimum lipid levels at a suitable stage of development for improving the survival during larval rearing. Furthermore, the study could be a baseline for elucidating the optimized dietary lipid levels of this catfish during its larval rearing.

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Developmental regulation of lipoprotein lipase in rats

Cited by 18 publications

References 26 publications

Regulation of lipoprotein lipase in the diabetic rat.

Regulation of lipoprotein lipase in the diabetic rat.

Localization of Lipoprotein Lipase in the Diabetic Heart

Expression and activity of key lipases during the larval development of walking catfish (Clarias magur)

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