Ikeda Y

References (39)

Title : Neuroprotection by dipeptidyl-peptidase-4 inhibitors and glucagon-like peptide-1 analogs via the modulation of AKT-signaling pathway in Alzheimer's disease - Ikeda_2021_World.J.Biol.Chem_12_104
Author(s) : Ikeda Y , Nagase N , Tsuji A , Kitagishi Y , Matsuda S
Ref : World Journal of Biological Chemistry , 12 :104 , 2021
Abstract : Alzheimer's disease (AD) is the most common reason for progressive dementia in the elderly. It has been shown that disorders of the mammalian/mechanistic target of rapamycin (mTOR) signaling pathways are related to the AD. On the other hand, diabetes mellitus (DM) is a risk factor for the cognitive dysfunction. The pathogenesis of the neuronal impairment caused by diabetic hyperglycemia is intricate, which contains neuro-inflammation and/or neurodegeneration and dementia. Glucagon-like peptide-1 (GLP1) is interesting as a possible link between metabolism and brain impairment. Modulation of GLP1 activity can influence amyloid-beta peptide aggregation via the phosphoinositide-3 kinase/AKT/mTOR signaling pathway in AD. The GLP1 receptor agonists have been shown to have favorable actions on the brain such as the improvement of neurological deficit. They might also exert a beneficial effect with refining learning and memory on the cognitive impairment induced by diabetes. Recent experimental and clinical evidence indicates that dipeptidyl-peptidase-4 (DPP4) inhibitors, being currently used for DM therapy, may also be effective for AD treatment. The DPP-4 inhibitors have demonstrated neuroprotection and cognitive improvements in animal models. Although further studies for mTOR, GLP1, and DPP4 signaling pathways in humans would be intensively required, they seem to be a promising approach for innovative AD-treatments. We would like to review the characteristics of AD pathogenesis, the key roles of mTOR in AD and the preventive and/ or therapeutic suggestions of directing the mTOR signaling pathway.
ESTHER : Ikeda_2021_World.J.Biol.Chem_12_104
PubMedSearch : Ikeda_2021_World.J.Biol.Chem_12_104
PubMedID: 34904048

Title : Role of Hormone-sensitive Lipase in Leptin-Promoted Fat Loss and Glucose Lowering - Takanashi_2017_J.Atheroscler.Thromb_24_1105
Author(s) : Takanashi M , Taira Y , Okazaki S , Takase S , Kimura T , Li CC , Xu PF , Noda A , Sakata I , Kumagai H , Ikeda Y , Iizuka Y , Yahagi N , Shimano H , Osuga JI , Ishibashi S , Kadowaki T , Okazaki H
Ref : J Atheroscler Thromb , 24 :1105 , 2017
Abstract : AIM: Myriad biological effects of leptin may lead to broad therapeutic applications for various metabolic diseases, including diabetes and its complications; however, in contrast to its anorexic effect, the molecular mechanisms underlying adipopenic and glucose-lowering effects of leptin have not been fully understood. Here we aim to clarify the role of hormone-sensitive lipase (HSL) in leptin's action. METHODS: Wild-type (WT) and HSL-deficient (HSLKO) mice were made hyperleptinemic by two commonly-used methods: adenovirus-mediated overexpression of leptin and continuous subcutaneous infusion of leptin by osmotic pumps. The amount of food intake, body weights, organ weights, and parameters of glucose and lipid metabolism were measured. RESULTS: Hyperleptinemia equally suppressed the food intake in WT and HSLKO mice. On the other hand, leptin-mediated fat loss and glucose-lowering were significantly blunted in the absence of HSL when leptin was overexpressed by recombinant adenovirus carrying leptin. By osmotic pumps, the fat-losing and glucose-lowering effects of leptin were milder due to lower levels of hyperleptinemia; although the difference between WT and HSLKO mice did not reach statistical significance, HSLKO mice had a tendency to retain more fat than WT mice in the face of hyperleptinemia. CONCLUSIONS: We clarify for the first time the role of HSL in leptin's effect using a genetic model: leptin-promoted fat loss and glucose-lowering are at least in part mediated via HSL-mediated lipolysis. Further studies to define the pathophysiological role of adipocyte lipases in leptin action may lead to a new therapeutic approach to circumvent leptin resistance.
ESTHER : Takanashi_2017_J.Atheroscler.Thromb_24_1105
PubMedSearch : Takanashi_2017_J.Atheroscler.Thromb_24_1105
PubMedID: 28413180

Title : Cardiomyocyte steatosis and defective washout of iodine-123-beta-methyl iodophenyl-pentadecanoic acid in genetic deficiency of adipose triglyceride lipase -
Author(s) : Hirano K , Ikeda Y , Sugimura K , Sakata Y
Ref : Eur Heart J , 36 :580 , 2015
PubMedID: 25336228

Title : Comparative analysis of the Corynebacterium glutamicum group and complete genome sequence of strain R - Yukawa_2007_Microbiology_153_1042
Author(s) : Yukawa H , Omumasaba CA , Nonaka H , Kos P , Okai N , Suzuki N , Suda M , Tsuge Y , Watanabe J , Ikeda Y , Vertes AA , Inui M
Ref : Microbiology , 153 :1042 , 2007
Abstract : The complete genome sequence of Corynebacterium glutamicum strain R was determined to allow its comparative analysis with other corynebacteria. The biology of corynebacteria was explored by refining the definition of the subset of genes that constitutes the corynebacterial core as well as those characteristic of saprophytic and pathogenic ecological niches. In addition, the relative scarcity of corynebacterial sigma factors and the plasticity of their two-component system machinery reflect their relatively exacting nutritional requirements and reduced membrane-associated and secreted proteins. The conservation of key genes and pathways between corynebacteria, mycobacteria and Nocardia validates the use of C. glutamicum to study fundamental processes that are conserved in slow-growing mycobacteria, including pathogenesis-associated mechanisms. The discovery of 39 novel genes in C. glutamicum R that have not been previously reported in other corynebacteria supports the rationale for sequencing additional corynebacterial genomes to better define the corynebacterial pan-genome and identify previously undetected metabolic pathways in these organisms.
ESTHER : Yukawa_2007_Microbiology_153_1042
PubMedSearch : Yukawa_2007_Microbiology_153_1042
PubMedID: 17379713
Gene_locus related to this paper: corgb-a4qhr7 , corgb-a4qhw6 , corgl-199 , corgl-CGL0007 , corgl-CGL0081 , corgl-CGL0340 , corgl-CGL0343 , corgl-CGL0591 , corgl-CGL1031 , corgl-Cgl1133 , corgl-CGL1144 , corgl-CGL1481 , corgl-CGL2002 , corgl-CGL2067 , corgl-CGL2181 , corgl-Cgl2249 , corgl-CGL2254 , corgl-CGL2393 , corgl-CGL2474 , corgl-CGL2878 , corgl-ephli , corgl-metx , corgl-q8nlr5 , corgl-q8nlz1 , corgl-y967 , corgt-g6wsn6

Title : Change in immunoreactive human hepatic triglyceride lipase (HTGL) mass and the shelf-life of the HTGL ELISA kit in long-term storage - Nishimura_2006_J.Immunoassay.Immunochem_27_89
Author(s) : Nishimura M , Iwanaga T , Ohkaru Y , Takagi A , Ikeda Y
Ref : Journal of Immunoassay Immunochem , 27 :89 , 2006
Abstract : Objectives of this work are to study changes in the immunoreactive HTGL mass during storage under various conditions. In addition, the shelf-life of the HTGL ELISA kit was confirmed. The immunological reactivity of HTGL in PHP stored in the liquid, frozen, or lyophilized state was monitored using purified human PHP-HTGL as the standard material. Furthermore, the long-term stability of the HTGL ELISA kit was ascertained. The immunoreactive HTGL mass in the lyophilized PHP maintained its initial immunological reactivity for at least 26 months at 4 degrees C or lower. The other reagents included in the HTGL ELISA kit also have a long shelf-life when they are stored at 4 degrees C or less. HTGL in PHP was stabilized by lyophilization and can be used as the standard material for HTGL ELISA; the HTGL ELISA kit has a long shelf-life, i.e., more than two years.
ESTHER : Nishimura_2006_J.Immunoassay.Immunochem_27_89
PubMedSearch : Nishimura_2006_J.Immunoassay.Immunochem_27_89
PubMedID: 16450871

Title : Glucose-stimulated insulin response in non-diabetic patients with lipoprotein lipase deficiency and hypertriglyceridemia - Tamasawa_2006_Diabetes.Res.Clin.Pract_72_6
Author(s) : Tamasawa N , Matsui J , Murakami H , Tanabe J , Matsuki K , Ogawa Y , Ikeda Y , Takagi A , Suda T
Ref : Diabetes Res Clin Pract , 72 :6 , 2006
Abstract : Elevations in plasma triglyceride (TG) and free fatty acid (FFA) concentrations are generally thought to play a role in the pathogenesis of insulin-resistant diabetes. The objective of this study was to investigate the relationship between hypertriglyceridemia and glucose-stimulated insulin responsiveness in non-diabetic patients. Forty subjects were divided into three BMI-matched groups as follows: one group consisted of 8 patients with a lipoprotein lipase (LPL) deficiency, another consisted of 12 patients with hypertriglyceridemia and a third consisted of 20 subjects with normal TG levels. In response to a 75 g oral glucose tolerance test, plasma insulin levels in the LPL-deficient subjects were higher (106+/-11 microU/ml) than those in the hypertriglyceridemic (69+/-16 microU/ml) and normolipidemic (29+/-3 microU/ml) subjects, at 30 min. On the other hand, their plasma glucose levels (127+/-6 mg/dl) were less than those seen in the normolipidemic group (165+/-9 mg/dl) after 90 min. Thus, LPL-deficient subjects with hypertriglyceridemia displayed an enhanced glucose-stimulated insulin response as well as lower blood glucose levels, the latter of which is not generally seen in those with hypertriglyceridemia and normolipidemia.
ESTHER : Tamasawa_2006_Diabetes.Res.Clin.Pract_72_6
PubMedSearch : Tamasawa_2006_Diabetes.Res.Clin.Pract_72_6
PubMedID: 16256241

Title : [Usefulness of branched-chain amino acid (BCAA)-enriched nutrient mixture for nutritional treatment undergoing endoscopic treatment for esophageal varices] - Shibata_2005_Nihon.Shokakibyo.Gakkai.Zasshi_102_880
Author(s) : Shibata N , Matsui H , Takeshita E , Yokota T , Higaki N , Murakami H , Ikeda Y , Minami H , Matsuura B , Onji M
Ref : Nihon Shokakibyo Gakkai Zasshi , 102 :880 , 2005
Abstract : We investigated the alteration of nutritional status in 144 patients who were treated for the first time with endoscopic sclerotherapy or endoscopic variceal ligation during their therapies. The serum levels of albumin, cholinesterase and total cholesterol were compared before and after treatment. The serum level of cholinesterase declined significantly. To investigate the impact of aging on the changes of nutritional status we divided all patients into two groups: (1) under 65 years, and (2) over 65 years. The decline of serum albumin of elderly patients (n=65) was significantly greater than that of younger patients (n=79). A branched-chain amino acid (BCAA)-enriched nutrient mixture for nutritional treatment significantly suppressed the decline of serum albumin in elderly patients. Nutritional treatment with a BCAA-enriched nutrient mixture should be considered during endoscopic therapy for esophageal varices, especially in elderly patients.
ESTHER : Shibata_2005_Nihon.Shokakibyo.Gakkai.Zasshi_102_880
PubMedSearch : Shibata_2005_Nihon.Shokakibyo.Gakkai.Zasshi_102_880
PubMedID: 16038434

Title : Genotyping of the human lipoprotein lipase gene by ferrocenylnaphthalene diimide-based electrochemical hybridization assay - Nojima_2005_Anal.Sci_21_1437
Author(s) : Nojima T , Yamashita K , Takagi A , Ikeda Y , Kondo H , Takenaka S
Ref : Anal Sci , 21 :1437 , 2005
Abstract : A ferrocenylnaphthalene diimide (FND)-based electrochemical hybridization assay (FND-EHA) was applied to the detection of two mutations in human lipoprotein lipase (LPL) gene, G188E (one base transition) and Arita (one base deletion). A probe oligodeoxyribonucleotide of 13 bases representing the wild type (WT) sequence of LPL was immobilized on a gold electrode, followed by hybridization with a sample PCR product of 350 base pairs under conditions in which both WT and mutated (MT) sequences could form a duplex with the probe. The hybridized electrodes were soaked in an electrolyte containing FND under conditions in which only the mismatched duplex could undergo dissociation. FND was concentrated in proportion to the amount of the duplex remaining on the electrode to give rise to a current signal. Blind tests were run to judge the genotype (WT/WT, WT/MT, or MT/MT) of 10 samples each for the G188E and Arita mutations and then, 8 and 10 of them were judged correctly, respectively.
ESTHER : Nojima_2005_Anal.Sci_21_1437
PubMedSearch : Nojima_2005_Anal.Sci_21_1437
PubMedID: 16379382

Title : [Analysis of lipoprotein lipase activity, immunoreactive mass and gene] -
Author(s) : Takagi A , Ikeda Y
Ref : Nihon Rinsho , 62 Suppl 12 :71 , 2004
PubMedID: 15658266

Title : Enantioselective esterification of racemic ibuprofen in isooctane by immobilized lipase on cellulose acetate-titanium iso-propoxide gel fiber - Ikeda_2002_J.Biosci.Bioeng_93_98
Author(s) : Ikeda Y , Kurokawa Y
Ref : J Biosci Bioeng , 93 :98 , 2002
Abstract : Lipase (Candida rugosa) was entrap-immobilized on cellulose acetate-titanium iso-propoxide gel fiber by the sol-gel method. The immobilized lipase was used for the direct synthesis of (S)-ibuprofen ester from racemic ibuprofen using propyl alcohol as an acyl acceptor in isooctane. The activity of the immobilized lipase was decreased to about 10-20% that of native lipase. However, the reaction was more enantioselective compared to that with native lipase. The stability for repeated use was improved by immobilization.
ESTHER : Ikeda_2002_J.Biosci.Bioeng_93_98
PubMedSearch : Ikeda_2002_J.Biosci.Bioeng_93_98
PubMedID: 16233173

Title : [Lipoprotein lipase deficiency, familial] -
Author(s) : Ikeda Y , Takagi A
Ref : Ryoikibetsu Shokogun Shirizu , :110 , 2001
PubMedID: 11528646

Title : Novel compound heterozygous mutations for lipoprotein lipase deficiency. A G-to-T transversion at the first position of exon 5 causing G154V missense mutation and a 5' splice site mutation of intron 8 - Ikeda_2001_J.Lipid.Res_42_1072
Author(s) : Ikeda Y , Takagi A , Nakata Y , Sera Y , Hyoudou S , Hamamoto K , Nishi Y , Yamamoto A
Ref : J Lipid Res , 42 :1072 , 2001
Abstract : We systematically investigated the molecular defects causing a primary LPL deficiency in a Japanese male infant (patient DI) with fasting hyperchylomicronemia (type I hyperlipoproteinemia) and in his parents. Patient DI had neither LPL activity nor immunoreactive LPL mass in the pre- and post-heparin plasma. The patient was a compound heterozygote for novel mutations consisting of a G-to-T transversion at the first nucleotide of exon 5 [+1 position of 3' acceptor splice site (3'-ass) of intron 4] and a T-to-C transition in the invariant GT at position +2 of the 5' donor splice site (5'-dss) of intron 8 (Int8/5'-dss/t(+2)c). The G-to-T transversion, although affecting the 11 nucleotide of the 3'-consensus acceptor splice site, resulted in a substitution of Gly(154) to Val (G154V; GG(716)C(-->)GTC). The mutant G154V LPL expressed in COS-1 cells was catalytically inactive and hardly released from the cells by heparin. The Int8/5'-dss/t(+2)c mutation inactivated the authentic 5' splice site of intron 8 and led to the utilization of a cryptic 5'-dss in exon 8 as an alternative splice site 133 basepairs upstream from the authentic splice site, thereby causing joining of a part of exon 8 to exon 9 with skipping of a 134-bp fragment of exon 8 and intron 8. These additional mutations in the consensus sequences of the 3' and 5' splice sites might be useful for better understanding the factors that are involved in splice site selection in vivo.
ESTHER : Ikeda_2001_J.Lipid.Res_42_1072
PubMedSearch : Ikeda_2001_J.Lipid.Res_42_1072
PubMedID: 11441134

Title : Improved method for direct DNA sequencing of the human lipoprotein lipase gene using an auto DNA sequencer -
Author(s) : Mori A , Takagi A , Ikeda Y , Yamamoto A
Ref : Clinical Biochemistry , 33 :323 , 2000
PubMedID: 10936594

Title : A compound heterozygote for a novel missense mutation (G105R) in exon 3 and a missense mutation (D204E) in exon 5 of the lipoprotein lipase gene in a Japanese infant with hyperchylomicronaemia - Ikeda_2000_Clin.Sci.(Lond)_99_569
Author(s) : Ikeda Y , Goji K , Takagi A
Ref : Clinical Science (Lond) , 99 :569 , 2000
Abstract : We systematically investigated the molecular defects resulting in primary lipoprotein lipase (LPL) deficiency in a Japanese male infant (hereafter called 'the patient') with severe fasting hypertriglyceridaemia (type I hyperlipoproteinaemia). The primary LPL deficiency was diagnosed on the basis of the findings that no LPL activity was detected in post-heparin plasma (PHP) and that the immunoreactive LPL mass in PHP was less than 2% of the control level. The patient was a compound heterozygote for a novel missense mutation (G(568)GA-->AGA/Gly(105)-->Arg; G105R) in exon 3 and a missense mutation (GAC(867)-->GAG/Asp(204)-->Glu; D204E) in exon 5 of the LPL gene. The biological significance of both missense mutations was examined by an in vitro study of the expression of the mutant G105R LPL cDNA and D204E LPL cDNA in COS-1 cells. Both mutant LPLs were catalytically inactive and were barely released by heparin from the expressing COS-1 cells. These findings explain the failure to detect LPL activity and immunoreactive LPL mass in the patient's PHP. The G105R allele could be detected by digestion with the BsmAI restriction enzyme, and the D204E allele by digestion with HincII. The patient inherited the G105R allele from his mother and the D204E allele from his father. His parents were heterozygotes for the corresponding mutant allele, but normolipidaemic. The novel G105R missense mutation could not be detected by conventional analysis of single-strand conformation polymorphism, but it was identified by extensive sequencing of the entire exons and their flanking regions in the LPL gene.
ESTHER : Ikeda_2000_Clin.Sci.(Lond)_99_569
PubMedSearch : Ikeda_2000_Clin.Sci.(Lond)_99_569
PubMedID: 11099402

Title : A newly identified lipoprotein lipase (LPL) gene mutation (F270L) in a Japanese patient with familial LPL deficiency - Takagi_2000_Biochim.Biophys.Acta_1502_433
Author(s) : Takagi A , Ikeda Y , Takeda E , Yamamoto A
Ref : Biochimica & Biophysica Acta , 1502 :433 , 2000
Abstract : We have systematically investigated the molecular defects resulting in a primary lipoprotein lipase (LPL) deficiency in a Japanese male infant (proband SH) with fasting hyperchylomicronemia. Neither LPL activity nor immunoreactive LPL mass was detected in pre- or postheparin plasma from proband SH. DNA sequence analysis of the LPL gene of proband SH revealed homozygosity for a novel missense mutation of F270L (Phe(270)-->Leu/TTT(1065)-->TTG) in exon 6. The function of the mutant F270L LPL was determined by both biochemical and immunocytochemical studies. In vitro expression experiments on the mutant F270L LPL cDNA in COS-1 cells demonstrated that the mutant LPL protein was synthesized as a catalytically inactive form and its total amount was almost equal to that of the normal LPL. Moreover, the synthesized mutant LPL was non-releasable by heparin because the intracellular transport of the mutant LPL to the cell surface - by which normal LPL becomes heparin-releasable - was impaired due to the abnormal structure of the mutant LPL protein. These findings explain the failure to detect LPL activities and masses in pre- and postheparin plasma of the proband. The mutant F270L allele generated an XcmI restriction enzyme site in exon 6 of the LPL gene. The carrier status of F270L in the proband's family members was examined by digestion with XcmI. The proband was ascertained to be homozygous for the F270L mutation and his parents and sister were all heterozygous. The LPL activities and masses of the parents and the sister (carriers) were half or less than half of the control values. Regarding the phenotype of the carriers, the mother with a sign of hyperinsulinemia manifested hypertriglyceridemia (type IV hyperlipoproteinemia), whereas the healthy father and the sister were normolipidemic. Hyperinsulinemia may be a strong determinant of hypertriglyceridemia in subjects with heterozygous LPL deficiency.
ESTHER : Takagi_2000_Biochim.Biophys.Acta_1502_433
PubMedSearch : Takagi_2000_Biochim.Biophys.Acta_1502_433
PubMedID: 11068186

Title : Improved method for non-denaturing polyacrylamide gradient gel electrophoresis for detection of small-sized LDL produced during postprandial hypertriglyceridaemia - Ashida_1999_Scand.J.Clin.Lab.Invest_59_663
Author(s) : Ashida Y , Takagi A , Ikeda Y
Ref : Scand J Clin Lab Invest , 59 :663 , 1999
Abstract : A reliable method for detection of small-sized low-density lipoprotein (LDL) produced during transient hypertriglyceridaemia induced by ingestion of fat is described. Electrophoresis using a commercial non-denaturing 2.0-16% polyacrylamide gradient gel is commonly utilized to determine the size of LDL particles, but it failed to detect a minor change in LDL size induced during postprandial hypertriglyceridaemia. Detection of small-sized LDL was achieved by adjusting the polyacrylamide concentration. Electrophoresis using a non-denaturing 1.5-10% polyacrylamide gradient gel gave the best resolution for detecting small-sized LDL induced during postprandial hypertriglyceridaemia. This improved method may be useful for elucidating the underlying mechanism of production of small-sized LDL (small dense LDL) in subjects with chronic hypertriglyceridaemia.
ESTHER : Ashida_1999_Scand.J.Clin.Lab.Invest_59_663
PubMedSearch : Ashida_1999_Scand.J.Clin.Lab.Invest_59_663
PubMedID: 10691058

Title : Development and evaluation of a direct sandwich enzyme-linked immunosorbent assay for the quantification of lipoprotein lipase mass in human plasma - Kimura_1999_Clin.Biochem_32_15
Author(s) : Kimura H , Ohkaru Y , Katoh K , Ishii H , Sunahara N , Takagi A , Ikeda Y
Ref : Clinical Biochemistry , 32 :15 , 1999
Abstract : OBJECTIVE: The purpose of this study was to develop and evaluate a direct sandwich enzyme-linked immunosorbent assay (ELISA) for quantification of the lipoprotein lipase (LPL) immunoreactive mass in human plasma using monoclonal antibodies (MAbs) directed against LPL purified from human postheparin plasma (PHP) [corrected]. METHODS AND
RESULTS: The direct sandwich-ELISA was performed using a combination of two distinct types of MAbs that recognize different epitopes on the LPL molecule. The immunoreactive mass of human LPL was specifically measured using a horseradish peroxidase-labeled anti-human LPL MAb [1(1)D2B2] as an enzyme-linked MAb, and an anti-human LPL MAb [2(10)F8F9] coated on a polystyrene microtiter plate as a solid-phase MAb. Purified human PHP-LPL was used as a standard material. The detection range of the sandwich-ELISA was 3.6-460 ng of LPL protein per mL of plasma. The intra- and interassay coefficients of variation were less than 5.9% and 3.3%, respectively. The validity of this method was additionally assured by the recovery test, which resulted in the variation only between 97.5% and 105.1%, and also by the interference test, which resulted in noninterference of LPL assay with a high concentration of triglyceride, hemoglobin, bilirubin, uric acid, or creatinine. To assess the reliability of the LPL mass values obtained with the direct sandwich-ELISA, they were compared with LPL mass values determined by the one-step sandwich-EIA (MARKIT-F LPL EIA kit) previously established by us. This comparison showed a highly significant correlation (r = +0.990) between the two sets of values. The LPL mass concentrations in PHP from 33 healthy subjects were 267 +/- 53 and 257 +/- 59 ng/mL (mean +/- SD), respectively. CONCLUSION: The present direct sandwich-ELISA is useful for rapidly identifying certain abnormalities of LPL in PHP samples from patients with hypertriglyceridemia [corrected].
ESTHER : Kimura_1999_Clin.Biochem_32_15
PubMedSearch : Kimura_1999_Clin.Biochem_32_15
PubMedID: 10074887

Title : Molecular cloning and sequencing of a cDNA encoding the feline T-cell activation antigen CD26 homologue -
Author(s) : Nishimura Y , Miyazawa T , Ikeda Y , Izumiya Y , Nakamura K , Sato E , Mikami T , Takahashi E
Ref : Immunogenetics , 50 :366 , 1999
PubMedID: 10630304
Gene_locus related to this paper: felca-CD26

Title : Pharmacokinetics and safety of Z-321, a novel specific orally active prolyl endopeptidase inhibitor, in healthy male volunteers - Umemura_1999_J.Clin.Pharmacol_39_462
Author(s) : Umemura K , Kondo K , Ikeda Y , Nishimoto M , Hiraga Y , Yoshida Y , Nakashima M
Ref : Journal of Clinical Pharmacology , 39 :462 , 1999
Abstract : This study investigates the pharmacokinetics and safety profile of Z-321, (4R)-3-(indan-2-ylacetyl)-4-(1-pyrrolidinyl-carbonyl)-1,3-thiazoli dine, a novel specific orally active prolyl endopeptidase (PEP) inhibitor. Following a preliminary safety evaluation wherein 2 subjects received 3.75 and 15 mg doses and 2 other subjects received 7.5 and 30 mg doses, 16 subjects were assigned to two groups of 8 subjects each. In each group, 6 subjects were to receive active treatment, and 1 or 2 subjects were to receive placebo treatment. One group received 60 mg under fasted and fed conditions. A separate group of 8 subjects received 60 mg of Z-321 or a placebo in a bid regimen for 6 days and the morning dose on day 7. The concentrations of Z-321 and its main metabolites--R- and S-sulfoxide; RR-, SS-, and RS-indanol; and indanolsulfoxides in plasma and urine--were determined by the HPLC method. In the multiple-dose study, the cholinesterase activity was gradually increased and reached above the normal range on day 8 in 3 of 6 subjects given Z-321 and gradually returned to the normal range after completion of dosing. The elevation of plasma cholinesterase activity was considered to be an action of Z-321, but this remains to be verified. In a single-dose study at a dose of 30 mg, headache and vomiting were observed in 1 of 6 subjects. In the multiple-dose study, slight skin itching and eczema in 3 and 2 of 6 subjects, respectively, and headache in 2 of 6 subjects were observed, but all symptoms were not severe. There were no other abnormal findings in objective signs and laboratory findings, including blood pressure, heart rate, electrocardiogram, body temperature, hematology, blood chemistry, and urinalysis. The Cmax of Z-321 at 30, 60, and 120 mg in the fasting state were 63.7 +/- 23.9, 102.0 +/- 43.1, and 543.3 +/- 437.0 ng/ml (mean +/- SD), respectively, at 0.9 hours after administration, and the t1/2 was about 1.8 hours. There were no dramatic changes in the pharmacokinetics of Z-321 in the presence of food. In the multiple-dose study, there was no drug accumulation trend in plasma. These results indicate that Z-321 has acceptable pharmacodynamic and pharmacokinetics profiles for clinical use without any serious adverse events, as verified in healthy young male volunteers.
ESTHER : Umemura_1999_J.Clin.Pharmacol_39_462
PubMedSearch : Umemura_1999_J.Clin.Pharmacol_39_462
PubMedID: 10234593

Title : [Analysis of lipoprotein lipase activity, immunoreactive mass and gene] -
Author(s) : Takagi A , Ikeda Y
Ref : Nihon Rinsho , 57 Suppl :62 , 1999
PubMedID: 10543050

Title : Identification of compound heterozygous mutations (G188E\/W382X) of lipoprotein lipase gene in a Japanese infant with hyperchylomicronemia: the G188E mutation was newly identified in Japanese - Takagi_1999_Clin.Chim.Acta_285_143
Author(s) : Takagi A , Ikeda Y , Tachi K , Shinozuka T , Yamamoto A
Ref : Clinica Chimica Acta , 285 :143 , 1999
Abstract : We herein report a case of a 5-month-old Japanese female (patient AN) with fasting hyperchylomicronemia due to a primary lipoprotein lipase (LPL) deficiency. Patient AN was compound heterozygous for a missense mutation (GG818G-->GAG/Gly188-->Glu; G188E) in exon 5 and a nonsense mutation (TGG1401-->TGA/Trp382-->Stop; W382X) in exon 8 of the LPL gene. This resulted in less than 10% of the control levels for both the LPL activity and immunoreactive LPL mass in the postheparin plasma. A G188E mutation was thus identified for the first time in a Japanese, and the haplotype of this G188E allele was different from that of the G188E alleles identified in other ethnic groups. This additional mutation might be useful for early diagnosis of LPL gene aberrations in Japanese patients with fasting hyperchylomicronemia.
ESTHER : Takagi_1999_Clin.Chim.Acta_285_143
PubMedSearch : Takagi_1999_Clin.Chim.Acta_285_143
PubMedID: 10481930

Title : Identification of homozygous lipoprotein lipase gene mutation in a woman with recurrent aggravation of hypertriglyceridaemia induced by pregnancy - Suga_1998_J.Intern.Med_243_317
Author(s) : Suga S , Tamasawa N , Kinpara I , Murakami H , Kasai N , Onuma T , Ikeda Y , Takagi A , Suda T
Ref : J Intern Med , 243 :317 , 1998
Abstract : We herein report a case of a 40-year-old Japanese woman (patient IT) with a history of recurrent aggravation of hypertriglyceridaemia, pancreatitis and miscarriages in three previous pregnancies. However, strict dietary intervention was applied during a fourth pregnancy. As a result, acute pancreatitis was avoided, and the patient gave birth to a healthy infant. In patient IT, the underlying etiology of the recurrent aggravation of hypertriglyceridaemia during pregnancy was a lipoprotein lipase (LPL) gene aberration. She was homozygous for LPL deficiency due to a nonsense mutation (TGG1401 --> TGA/Trp382 --> Stop) in exon 8 of the LPL gene, which resulted in the absence of LPL activity and immunoreactive LPL mass. Our findings indicate that, in LPL deficiency, pregnancy seriously exacerbates hypertriglyceridaemia and increases the risk of acute pancreatitis, which endangers both the mother and fetus. Early diagnosis of LPL deficiency and appropriate management thereof are essential for normal childbirth.
ESTHER : Suga_1998_J.Intern.Med_243_317
PubMedSearch : Suga_1998_J.Intern.Med_243_317
PubMedID: 9627147

Title : Development of a direct DNA sequencing method for detecting heterozygous mutations of the human lipoprotein lipase gene - Mori_1997_Clin.Biochem_30_315
Author(s) : Mori A , Takagi A , Ikeda Y , Yamamoto A
Ref : Clinical Biochemistry , 30 :315 , 1997
Abstract : OBJECTIVE: The purpose of this study was to develop an improved method of direct DNA sequencing, which makes it possible to identify heterozygous mutations of the lipoprotein lipase (LPL) gene in order to understand the underlying genetic disorder of type IV hyperlipoproteinemia. METHODS AND
RESULTS: The direct sequencing method was improved by devising primers for amplifying the LPL gene and for sequencing DNA amplified by the polymerase chain reaction (PCR)T since the reported base sequences of the introns flanking exons of the LPL gene were limited to 40 bases. Improvement was achieved by attaching nine additional bases to both the PCR amplification primer and sequencing primer, and by optimizing the Tm value of the sequencing primers by adjusting the sequence of the nine extra bases. Use of the sequencing primers having suitable Tm values (48 degrees C-58 degrees C) made it possible to reduce nonspecific bands on the sequence ladder pattern and to identify heterozygous mutation sites in LPL gene exons 5 and 6 as model cases. CONCLUSION: Our improved direct sequencing method is useful for identifying heterozygous mutation sites in human LPL gene exons and splicing consensus regions.
ESTHER : Mori_1997_Clin.Biochem_30_315
PubMedSearch : Mori_1997_Clin.Biochem_30_315
PubMedID: 9209790

Title : Pharmacokinetics and safety of JTP-4819, a novel specific orally active prolyl endopeptidase inhibitor, in healthy male volunteers - Umemura_1997_Br.J.Clin.Pharmacol_43_613
Author(s) : Umemura K , Kondo K , Ikeda Y , Kobayashi T , Urata Y , Nakashima M
Ref : British Journal of Clinical Pharmacology , 43 :613 , 1997
Abstract : AIMS To investigate the pharmacokinetics and safety profile of JTP-4819, (-)-(2S)-1-benzylaminocarbonyl-[(2S)-2-glycoloylpyrrolidinyl ]-2-pyrrolidinecarboxamide, a novel specific orally active prolyl endopeptidase (PEP) inhibitor. METHODS: JTP-4819 was given orally to 28 healthy male volunteers at single doses of 30 mg (n = 6), 60 mg (n = 6), 120 mg (n = 6) and placebo (n = 3) and multiple doses of 60 mg three times daily (n = 5) and placebo (n = 2) for 7 days to investigate its safety and pharmacokinetics following a preliminary safety evaluation of 3, 10 and 30 mg doses in six healthy volunteers. With the single dose of 60 mg, a cross-over study was conducted to examine the effect of food on the bioavailability of the drug. The concentrations of JTP-4819 in plasma and urine were determined by electrospray ionization-liquid chromatography/mass spectrometry (ESI-LC/MS) method. RESULTS: In the multiple-dose study, the cholinesterase activity was gradually increased and reached above the normal range on days 4 to 8 in all five subjects given JTP-4819 and gradually returned to normal range after completion of dosing. The elevation of plasma cholinesterase activity was considered to be an action of JTP-4819, but this remains to be verified. There were no other abnormal findings in objective symptoms and laboratory findings including blood pressure, heart rate, electrocardiogram, body temperature, haematology, blood chemistry and urinalysis. The Cmax of JTP-4819 at 30, 60 and 120 mg in fasting state were 474, 887 and 1,649 ng ml-1, respectively, at 1 h after administration, and the t1/2 was about 2 h. AUC increased in proportion to the given doses. The cumulative urinary recoveries within 24 h were approximately 66%, Cmax, AUC, t1/2 and urinary recovery were not affected by food intake. In the multiple-dose study, there was no drug accumulation trend in plasma.
CONCLUSIONS: These results indicate that JTP-4819 has acceptable pharmacodynamic and pharmacokinetics profiles for clinical use without any serious adverse events as we verified in healthy young male volunteers.
ESTHER : Umemura_1997_Br.J.Clin.Pharmacol_43_613
PubMedSearch : Umemura_1997_Br.J.Clin.Pharmacol_43_613
PubMedID: 9205821

Title : Racial differences in polymorphic allele heterozygosities of the human hepatic triglyceride lipase gene -
Author(s) : Takagi A , Ikeda Y , Mori A , Ashida Y , Yamamoto A
Ref : Mol Cell Probes , 11 :163 , 1997
PubMedID: 9160333

Title : Identification of a BstNI polymorphism in exon 9 of the human hepatic triglyceride lipase gene -
Author(s) : Takagi A , Ikeda Y , Mori A , Ashida Y , Yamamoto A
Ref : Mol Cell Probes , 10 :313 , 1996
PubMedID: 8865180
Gene_locus related to this paper: human-LIPC

Title : [The improvement of a direct DNA sequencing method by devising the primer design: detection of lipoprotein lipase gene aberrations] - Mori_1996_Rinsho.Byori_44_983
Author(s) : Mori A , Takagi A , Ikeda Y , Yamamoto A
Ref : Rinsho Byori , 44 :983 , 1996
Abstract : We developed an improved method of direct DNA sequencing which makes it possible to detect heterozygous mutations in an exon and the splicing consensus regions (acceptor and donor) in introns even in the cases where there is limited information available regarding the base sequences of the introns flanking the exon. Human lipoprotein lipase (LPL) gene was utilized to develop this method, since the reported intron base sequences of the LPL gene are limited to 40 bases. We constructed PCR primers with extra 9 bases for the LPL gene amplification and 20-mers from 5' end of the PCR primers were used as sequencing primers in order to obtain the necessary distance from the 3' end of the sequencing primer to 5' end of the splicing acceptor consensus sequence for the accurate determination of the sequence of the consensus region. Furthermore, the attachment of the 9 bases made it possible to optimize the Tm value of the sequencing primers by adjusting their G + C/A + T ratio. The direct sequencing method using the sequencing primer with an appropriate Tm value (i.e., 48 degrees C-58 degrees C in this study) was effective in reducing nonspecific bands on the sequence ladder pattern, and allowed the determination of the base sequences of both the sense and antisense strands of the splicing consensus sequences and exon. As a result, this improved direct sequencing method was capable of detecting heterozygous as well as homozygous LPL gene mutations.
ESTHER : Mori_1996_Rinsho.Byori_44_983
PubMedSearch : Mori_1996_Rinsho.Byori_44_983
PubMedID: 8937192

Title : Identification of two new alleles at the lipoprotein lipase (LPL) short tandem repeat (STR) locus results in seven polymorphic alleles in the Japanese population: allele frequency data in comparison with Caucasian populations -
Author(s) : Takagi A , Mori A , Ikeda Y , Yamamoto A
Ref : Mol Cell Probes , 10 :227 , 1996
PubMedID: 8799377

Title : An AvaII polymorphism in exon 5 of the human hepatic triglyceride lipase gene -
Author(s) : Mori A , Takagi A , Ikeda Y , Ashida Y , Yamamoto A
Ref : Mol Cell Probes , 10 :309 , 1996
PubMedID: 8865179
Gene_locus related to this paper: human-LIPC

Title : [The measurements of lipoprotein lipase activity] -
Author(s) : Takagi A , Ikeda Y , Yamamoto A
Ref : Nihon Rinsho , 53 Su Pt 1 :639 , 1995
PubMedID: 8753519

Title : [Alcohol-induced hypertriglyceridemia in subjects with decreased lipoprotein lipase--improvement after cessation of alcohol intake] - Tsutsumi_1995_Nihon.Shokakibyo.Gakkai.Zasshi_92_951
Author(s) : Tsutsumi Z , Ikeda Y , Takagi A , Tsushima M , Higashino K , Yamamoto A
Ref : Nihon Shokakibyo Gakkai Zasshi , 92 :951 , 1995
Abstract : We systematically investigated the effect of lipoprotein lipase (LPL) and alcohol intake on the development of primary type IV hyperlipoproteinemia which is manifested as a moderate increase in serum triglycerides as a consequence of an elevated very low density lipoprotein concentration and a normal level of serum cholesterol. Twenty six type IV hyperlipoproteinemic and 28 normolipidemic males underwent measurement of the immunoreactive LPL mass in postheparin plasma (30 unit of heparin/kg of body weight) and were interviewed as to their alcohol consumption. They were divided into 4 groups, with a LPL mass of 150ng/ml (20 percentile of the normal range) and an alcohol intake of 33g/day as the borderlines. All subjects with LPL mass less than 150ng/ml and alcohol intake of more than 33g/day were prone to manifest type IV hyperlipoproteinemia. One of the subjects in this group showed a recovery to normolipidemic state after cessation of alcohol intake. Subject whose LPL mass value was more than 180ng/ml (50 percentile of the normal range) were not susceptible to type IV hyperlipoproteinemia even though they drank alcohol more than 33g/day.
ESTHER : Tsutsumi_1995_Nihon.Shokakibyo.Gakkai.Zasshi_92_951
PubMedSearch : Tsutsumi_1995_Nihon.Shokakibyo.Gakkai.Zasshi_92_951
PubMedID: 7609317

Title : Ebelactone B, an inhibitor of urinary carboxypeptidase Y-like kininase, prevents the development of deoxycorticosterone acetate-salt hypertension in rats - Majima_1995_Eur.J.Pharmacol_284_1
Author(s) : Majima M , Ikeda Y , Kuribayashi Y , Mizogami S , Katori M , Aoyagi T
Ref : European Journal of Pharmacology , 284 :1 , 1995
Abstract : Kininogen-deficient Brown Norway Katholiek rats (BN-Ka) excrete little urinary kinin, compared with normal rats of the same strain (BN Kitasato rats (BN-Ki)). Deoxycorticosterone acetate-salt treatment increased systolic blood pressure in both rats, but much faster in BN-Ka than in BN-Ki. Daily subcutaneous administration of ebelactone B (15 and 5 mg/kg/day), a rat urinary carboxypeptidase Y-like kininase inhibitor, significantly reduced systolic blood pressure in BN-Ki, but not in BN-Ka. This treatment significantly increased urinary Na+ excretion and reduced Na+ concentration in the erythrocytes in BN-Ki, but not in BN-Ka. An angiotensin-converting enzyme inhibitor, lisinopril (5 mg/kg/day s.c.), did not reduce the systolic blood pressure in either BN-Ki or BN-Ka. These results suggested that ebelactone B has promise as a preventive agent for the development of hypertension acting through the inhibition of urinary kinin degradation.
ESTHER : Majima_1995_Eur.J.Pharmacol_284_1
PubMedSearch : Majima_1995_Eur.J.Pharmacol_284_1
PubMedID: 8549611

Title : [Lipoprotein lipase] - Ikeda_1994_Nihon.Rinsho_52_3146
Author(s) : Ikeda Y , Takagi A , Yamamoto A
Ref : Nihon Rinsho , 52 :3146 , 1994
Abstract : We describe molecular and physiological properties of human lipoprotein lipase (LPL) based on recent advanced knowledges. Human LPL is a lipolytic glycoprotein enzyme synthesized by extrahepatic tissues, mainly adipocytes, and its gene is located on chromosome 8p22 with 10 exons that encode mRNAs of 3.4 kb and 3.8 kb. Clinical and biochemical studies indicate that LPL plays a key role in hydrolyzing the triglycerides of chylomicrons and very low density lipoproteins (VLDL) at the first step in their metabolism. LPL is believed to be taken on a functionally active form at the site of capillary endothelial cell surface following a series of three major processes: (1) the synthesis and secretion of LPL by adipocytes, (2) the transport of LPL from adipocytes to the capillary endothelium, and (3) the binding of LPL to heparan sulfate proteoglycan chains which are localized in the plasma membrane of the endothelium. LPL is released into the circulation after intravenous injection of heparin, and LPL is recovered in postheparin plasma (PHP). LPL purified from human PHP is catalytically active in a monomeric form, and its molecular size is 61 k dalton in good agreement with mature LPL size estimated by cDNA of LPL.
ESTHER : Ikeda_1994_Nihon.Rinsho_52_3146
PubMedSearch : Ikeda_1994_Nihon.Rinsho_52_3146
PubMedID: 7853703

Title : Diuretic and natriuretic effect of ebelactone B in anesthetized rats by inhibition of a urinary carboxypeptidase Y-like kininase - Majima_1994_Jpn.J.Pharmacol_65_79
Author(s) : Majima M , Kuribayashi Y , Ikeda Y , Adachi K , Kato H , Katori M , Aoyagi T
Ref : Japanese Journal of Pharmacology , 65 :79 , 1994
Abstract : Ebelactone B (EB) (10(-7)-10(-5) M) inhibited dose-dependently carboxypeptidase (CP) Y-like exopeptidase, one of the major kininases separated from rat urine, whereas it inhibited neither CPA, CPB or neutral endopeptidase (NEP). Degradation of bradykinin (BK) to BK-(1-8) in rat urine was completely inhibited by EB (10(-5) M) with the increased generation of BK-(1-7). Intraduodenal administration of EB (3 mg/kg) to anesthetized rats caused marked diuresis (by 110%) and natriuresis (130%), in parallel with the increase in urinary kinin levels (110%). Intravenous infusion of a BK antagonist, Hoe140 (3 mg/kg/hr), strongly blocked both EB-induced diuresis and natriuresis. EB may be a novel type of diuretic and natriuretic agent that acts by increasing urinary kinin levels.
ESTHER : Majima_1994_Jpn.J.Pharmacol_65_79
PubMedSearch : Majima_1994_Jpn.J.Pharmacol_65_79
PubMedID: 8089934

Title : A newly identified heterozygous lipoprotein lipase gene mutation (Cys239-->stop\/TGC972-->TGA\; LPLobama) in a patient with primary type IV hyperlipoproteinemia - Takagi_1994_J.Lipid.Res_35_2008
Author(s) : Takagi A , Ikeda Y , Mori A , Tsutsumi Z , Oida K , Nakai T , Yamamoto A
Ref : J Lipid Res , 35 :2008 , 1994
Abstract : We investigated measures for identification of heterozygous lipoprotein lipase (LPL) deficiency in unrelated subjects with primary type IV hyperlipoproteinemia in order to acquire a helpful clue for understanding the correlation between hypertriglyceridemia and the status of being a heterozygous carrier of an LPL gene variant. Identification of heterozygous LPL deficiency was performed by monitoring the immunoreactive LPL mass in postheparin plasma (PHP) using our developed sandwich-enzyme immunoassay technique for first screening. Then, in subjects found to have half or less than half of the control LPL mass value in PHP, the polymerase chain reaction-single strand conformation polymorphism method was used to detect LPL gene aberrations as a second screening. This approach was evaluated as being useful as it succeeded in identifying a subject (proband KD) with heterozygous LPL deficiency. The mutation in the LPL gene of proband KD was newly characterized as a nucleotide C972 to A transversion in exon 6, resulting in substitution of a premature termination codon (TGA) for Cys239 (TGC). This nonsense mutation, designated as LPLobama, creates an MboI restriction site and eliminates an HgiAI restriction site, and this allows rapid screening of subjects with type IV as well as type I hyperlipoproteinemia for the mutation. The homozygous state for the LPLobama allele resulted in neither detectable LPL activity nor immunoreactive LPL mass in PHP, and this was seen in two of proband KD's siblings.
ESTHER : Takagi_1994_J.Lipid.Res_35_2008
PubMedSearch : Takagi_1994_J.Lipid.Res_35_2008
PubMedID: 7868979
Gene_locus related to this paper: human-LPL

Title : Molecular studies on primary lipoprotein lipase (LPL) deficiency. One base deletion (G916) in exon 5 of LPL gene causes no detectable LPL protein due to the absence of LPL mRNA transcript - Takagi_1992_J.Clin.Invest_89_581
Author(s) : Takagi A , Ikeda Y , Tsutsumi Z , Shoji T , Yamamoto A
Ref : J Clinical Investigation , 89 :581 , 1992
Abstract : We have systematically investigated a genetic defect resulting in a primary lipoprotein lipase (LPL) deficiency in a proband TN and his affected brother SN, both manifesting familial hyperchylomicronemia. Neither LPL activity nor immunoreactive LPL mass was detected in postheparin plasma from the two patients. Immunocytochemical and biosynthetic studies on the proband's monocyte-derived macrophages with rabbit anti-human LPL antiserum revealed that no immunochemically detectable LPL protein was found in either the cells or culture medium, whereas LPL having a molecular mass of 61 kD was detected in normal cells. No detectable LPL mRNA was identified from poly(A)+RNA of the proband's macrophages by Northern blot analysis, and grossly visible LPL gene rearrangement was not observed by Southern blot analysis. Sequence analysis of polymerase chain reaction-amplified LPL gene exons detected one base deletion of G (first position of Ala221) at base 916 in exon 5 which leads to a premature termination by a frameshift. This mutation, designated as LPLArita and resulting in the loss of an AluI restriction enzyme site, was newly identified. We further analyzed the LPL gene from the two patients and their family members by digestion with AluI. Both patients were homozygous for LPLArita allele, while their spouses did not have this mutation. As genetically expected, their children were all heterozygous for LPLArita. We conclude that primary LPL deficiency in the proband was caused by a lack of enzyme synthesis due to the absence of LPL mRNA resulting from one base deletion of G in exon 5, and that heterozygous LPLArita deficient subjects show almost half value of control LPL mass.
ESTHER : Takagi_1992_J.Clin.Invest_89_581
PubMedSearch : Takagi_1992_J.Clin.Invest_89_581
PubMedID: 1737848

Title : DNA sequence of lipoprotein lipase cDNA cloned from human monocytic leukemia THP-1 cells -
Author(s) : Takagi A , Ikeda Y , Yamamoto A
Ref : Nucleic Acids Research , 18 :6436 , 1990
PubMedID: 2243796

Title : Purification and characterization of lipoprotein lipase and hepatic triglyceride lipase from human postheparin plasma: production of monospecific antibody to the individual lipase - Ikeda_1989_Biochim.Biophys.Acta_1003_254
Author(s) : Ikeda Y , Takagi A , Yamamoto A
Ref : Biochimica & Biophysica Acta , 1003 :254 , 1989
Abstract : Lipoprotein lipase (LPL) and hepatic triglyceride lipase (HTGL) were purified to homogeneity from human postheparin plasma. Molecular, catalytic and immunological properties of the purified enzymes were investigated. The native molecular weights of LPL and HTGL were 67,200 and 65,500, respectively, by gel chromatography. The subunit molecular weights of LPL and HTGL were 60,600 and 64,600, respectively, suggesting that these enzymes are catalytically active in a monomeric form. In addition, the purified LPL and HTGL each gave a single protein band when they were detected as glycoproteins with a probe of concanavalin A. The purified enzyme preparations were free of detectable antithrombin III by Western blot analysis. Catalytic properties of the purified enzymes were examined using triolein-gum arabic emulsion and triolein particles stabilized with phospholipid monolayer as substrates. LPL catalyzed the complete hydrolysis of triolein to free oleate and monooleate in the presence of apolipoprotein C-II. Apparent Km values for triolein and apolipoprotein C-II were 1.0 mM and 0.6 microM, and Vmax was 40.7 mmol/h per mg. HTGL hydrolyzed triolein substrate at a rate much slower than LPL, and produced mainly free oleate with little monooleate. Apparent Km and Vmax values were 2.5 mM and 16.1 mmol/h per mg, respectively. Polyclonal antibodies were developed against the purified LPL and HTGL. The purity and specificity of these antisera were ascertained by immunotitration, Ouchterlony double diffusion and Western blot analyses. The anti-human LPL and anti-human HTGL antiserum specifically reacted with the corresponding either native or denaturated enzyme, indicating that two enzymes were immunologically distinct. We developed an assay system for LPL and HTGL in human PHP by selective immunoprecipitation of each enzyme with the corresponding antiserum.
ESTHER : Ikeda_1989_Biochim.Biophys.Acta_1003_254
PubMedSearch : Ikeda_1989_Biochim.Biophys.Acta_1003_254
PubMedID: 2663075

Title : [Hypertriglyceridemia in a deficiency of lipoprotein lipase and hepatic lipase] -
Author(s) : Ikeda Y , Takagi A
Ref : Tanpakushitsu Kakusan Koso , 33 :783 , 1988
PubMedID: 3270893