Characterization of cDNA encoding the mouse hepatic triglyceride lipase and expression by in vitro translation

Chang, Shau-Feng; Netter, Hans Jiirgen; Will, Hans

doi:10.1016/0014-5793(91)80910-u

Cited by 18 publications

(10 citation statements)

References 17 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…The deduced amino acid sequences for dog, frog, and zebrafish HL are shown in Figure 1 together with previously reported sequences for human HL, 3,22 mouse HL, 52 rat HL, 53,54 and horse pancreatic lipase (LIPP) 30 (Table 1). Alignments of human and other vertebrate HL sequences examined showed between 49% and 98% identities, suggesting that they are products of the same family of genes, whereas comparisons of sequence identities of vertebrate HL proteins with human and mouse EL and LPL and horse LIPP exhibited lower levels of sequence identities, EL (38% and 42%, respectively), LPL (44% and 45%, respectively), and LIPP (25%), indicating that they are members of distinct but related neutral lipase families (Table 2).…”

Section: Resultsmentioning

confidence: 81%

Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies

Holmes¹,

VandeBerg²,

Cox³

2011

OAB

View full text Add to dashboard Cite

Hepatic lipase (gene: LIPC; enzyme: HL; E.C.3.1.1.3) is one of three members of the triglyceride lipase family that contributes to vascular lipoprotein degradation and serves a dual role in triglyceride hydrolysis and in facilitating receptor-mediated lipoprotein uptake into the liver. Amino acid sequences, protein structures, and gene locations for vertebrate LIPC (or Lipc for mouse and rat) genes and proteins were sourced from previous reports and vertebrate genome databases. Lipc was distinct from other neutral lipase genes (Lipg encoding endothelial lipase and Lpl encoding lipoprotein lipase [LPL]) and was located on mouse chromosome 9 with nine coding exons on the negative strand. Exon 9 of human LIPC and mouse and rat Lipc genes contained “stop codons” in different positions, causing changes in C-termini length. Vertebrate HL protein subunits shared 58%–97% sequence identities, including active, signal peptide, disulfide bond, and N-glycosylation sites, as well as proprotein convertase (“hinge”) and heparin binding regions. Predicted secondary and tertiary structures revealed similarities with the three-dimensional structure reported for horse and human pancreatic lipases. Potential sites for regulating LIPC gene expression included CpG islands near the 5″-untranslated regions of the mouse and rat LIPC genes. Phylogenetic analyses examined the relationships and potential evolutionary origins of the vertebrate LIPC gene family with other neutral triglyceride lipase gene families (LIPG and LPL). We conclude that the triglyceride lipase ancestral gene for vertebrate neutral lipase genes (LIPC, LIPG, and LPL) predated the appearance of fish during vertebrate evolution.

show abstract

Section: Resultsmentioning

confidence: 81%

Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies

Holmes¹,

VandeBerg²,

Cox³

2011

OAB

View full text Add to dashboard Cite

show abstract

“…The frozen livers were homogenised in 4 M guanidiniuin thiocyanate buffer, layered over a 5.7 M CsCI, 25 mM sodium acetate cushion and centrifuged for 20 h at 31 000 rpm. 20 mmol of total RNNlane was heat-denatured, loaded onto a 1 % agarose/1.85 M formaldehyde gel and transfered to a nylon membrane (Hybond-N, Amersham) according to the manufacturer's protocol ; "P-labelled probes for hepatic lipase (full-length murine cDNA [32], rat and mouse show 91% similarity according to the FASTA programme described by Pearson and Lipman [33]) and LCAT (full-length rat cDNA) [34] were made using the random priming kit (Amersham). The probe used for hepatic lipase northern blots were hybridized at 37°C overnight in 50% formamide hybridization buffer (Hybrysol, Oncor).…”

Section: Methodsmentioning

confidence: 99%

Comparison of the Uptake and Processing of Cholesterol from Chylomicrons of Different Fatty Acid Composition in Rats Fed High‐Fat and Low‐Fat Diets

Bravo

Flora

Cantàfora

et al. 1997

European Journal of Biochemistry

View full text Add to dashboard Cite

The fate of [3H]cholesterol carried in chylomicrons prepared from rats given a meal of palm oil (rich in long-chain saturated fatty acids), olive oil (rich in monounsaturated fatty acids) or corn oil (rich in n-6 polyunsaturated fatty acids) was investigated in vivo in rats fed a low-fat diet or a diet supplemented with the corresponding oil (to provide 40% of the calories) for 21 days. In the low-fat-fed groups, radioactivity was removed from the blood and secreted into bile over 180 min more rapidly when the chylomicrons were derived from corn oil as compared to palm or olive oil. After feeding the corresponding high-fat diets, however, both parameters were decreased in rats fed palm and corn oil, but not olive oil. As a result of these changes, the rates of removal of radioactivity from the blood and secretion into bile were similar in animals given the olive oil and corn oil diets, and higher than those in rats fed the palm oil diet. All the high-fat diets tended to increase the proportion of the radioactivity in the plasma found in the 1.006-1.050-g/ml fraction (low-density lipoprotein) and decrease that in the 1.050-1.25-g/ml (high-density lipoprotein) fraction in comparison to the respective low-fat diet groups, but the transfer of radioactivity to the plasma high-density lipoprotein fraction was particularly slow in palm-oilfed rats. These findings indicate that diets high in saturated or n-6 polyunsaturated fat retard the metabolism of chylomicron cholesterol in comparison to diets low in fat, while those high in monounsaturated fat do not have this effect. As a consequence of this, the rate of removal of cholesterol of dietary origin from the body is slower in animals fed saturated as compared to monounsaturated or n-6 polyunsaturated fat. Thus, differential metabolism of chylomicron cholesterol clearly plays an important role in the hyperand hypo-cholesterolaemic effects of these dietary fats.

show abstract

“…In contrast, mouse HL has a relatively low affinity for heparin-like glycosaminoglycans and is found in circulating plasma presumably due to the lack of a high-affinity binding site (11). Although mouse HL is 86% homologous to the human enzyme there is a significant sequence divergence in the carboxy terminus which may be responsible for the observed differences in heparin-binding affinities of the two enzymes (12).…”

Section: Introductionmentioning

confidence: 98%

Hepatic lipase gene therapy in hepatic lipase-deficient mice. Adenovirus-mediated replacement of a lipolytic enzyme to the vascular endothelium.

et al. 1996

View full text Add to dashboard Cite

Hepatic lipase (HL) is an endothelial-bound lipolytic enzyme which functions as a phospholipase as well as a triacylglycerol hydrolase and is necessary for the metabolism of IDL and HDL. To evaluate the feasibility of replacing an enzyme whose in vivo physiologic function depends on its localization on the vascular endothelium, we have infused recombinant replication-deficient adenovirus vectors expressing either human HL (HL-rAdV; n ϭ 7) or luciferase cDNA (Lucif-rAdV; n ϭ 4) into HL-deficient mice with pretreatment plasma cholesterol, phospholipid, and HDL cholesterol values of 176 Ϯ 9, 314 Ϯ 12, and 129 Ϯ 9, respectively. After infusion of HL-rAdV, HL could be detected in the postheparin plasma of HL-deficient mice by immunoblotting and postheparin plasma HL activities were 25,700 Ϯ 4,810 and 1,510 Ϯ 688 nmol/min/ml on days 5 and 15, respectively. Unlike the mouse HL, 97% of the newly synthesized human HL was heparin releasable, indicating that the human enzyme was virtually totally bound to the mouse vascular endothelium. Infusion of HL-rAdV in HL-deficient mice was associated with a 50-80% decrease in total cholesterol, triglyceride, phospholipids, cholesteryl ester, and HDL cholesterol ( P Ͻ 0.001) as well as normalization of the plasma fast protein liquid chromatography lipoprotein profile by day 8. These studies demonstrate successful expression and delivery of a lipolytic enzyme to the vascular endothelium for ultimate correction of the HL gene defect in HL-deficient mice and indicate that recombinant adenovirus vectors may be useful in the replacement of endothelial-bound lipolytic enzymes in human lipolytic deficiency states. ( J. Clin. Invest. 1996. 97:799-805.)

show abstract

Characterization of cDNA encoding the mouse hepatic triglyceride lipase and expression by in vitro translation

Cited by 18 publications

References 17 publications

Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies

Vertebrate hepatic lipase genes and proteins: a review supported by bioinformatic studies

Comparison of the Uptake and Processing of Cholesterol from Chylomicrons of Different Fatty Acid Composition in Rats Fed High‐Fat and Low‐Fat Diets

Hepatic lipase gene therapy in hepatic lipase-deficient mice. Adenovirus-mediated replacement of a lipolytic enzyme to the vascular endothelium.

Contact Info

Product

Resources

About