Ameis D

References (15)

Title : Overexpression of lysosomal acid lipase and other proteins in atherosclerosis - Zschenker_2006_J.Biochem_140_23
Author(s) : Zschenker O , Illies T , Ameis D
Ref : J Biochem , 140 :23 , 2006
Abstract : Atherosclerosis is one of the major causes of morbidity and mortality in the western world. The existing data of elevated expression levels of proteins like DNA damage and DNA repair enzymes in human atherosclerotic plaques are reviewed. From the literature, the effect of overexpression of different proteins using adenoviral vectors or the model of transgenic mice on the development of atherosclerosis will be discussed. Special focus is placed on the lysosomal acid lipase (LAL), because LAL connects extra-cellular with intra-cellular lipid metabolism and is the only hydrolase for cleavage of cholesteryl esters delivered to the lysosomes. Patients with a deficiency of LAL show an accumulation of lipids in the cells and develop pre-mature atherosclerosis. To answer the question of the influence of LAL in atherosclerosis if overexpressed, we show for the first time data of transgenic mice overexpressing LAL and the effect on the lipid level.
ESTHER : Zschenker_2006_J.Biochem_140_23
PubMedSearch : Zschenker_2006_J.Biochem_140_23
PubMedID: 16877765
Gene_locus related to this paper: human-LIPA

Title : Systematic mutagenesis of potential glycosylation sites of lysosomal acid lipase - Zschenker_2005_J.Biochem_137_387
Author(s) : Zschenker O , Bahr C , Hess UF , Ameis D
Ref : J Biochem , 137 :387 , 2005
Abstract : Lysosomal acid lipase (LAL; EC is a key enzyme in the intracellular lipid metabolism. It hydrolyzes exogenous triglycerides and cholesterol esters taken up by various cell types. LAL has six potential N-glycosylation sites and one potential O-glycosylation site. Elimination of each of the six Asn-(X)-Ser/Thr sites by site-directed mutagenesis and expression in baculovirus-infected Spodoptera frugiperda cells resulted in two single-mutant enzymes without lipolytic activities (N134Q and N246Q) and four mutants with preserved activities. The two inactive mutants were not detectable on immunoblot analysis, indicating that they were not secreted. Six double mutants in all possible combinations except for the two inactive single mutants were produced and expressed. Double mutants in combination with the N9 glycosylation site showed reduced activities as compared to the other mutants or the wild-type enzyme. Kinetic data of LAL glycosylation mutants indicate that substrate affinity of N9Q was not changed, but k (cat) of N9 mutants was reduced distinctly compared to the wild-type enzyme. Peanut agglutinin lectin did not recognize LAL, demonstrating that the protein has no core1 structure (Galbeta 1-3 GalNAc) of O-glycosylation. These data indicate that at least two of the six N-glycosylation sites are used in native lipase. N134 and N246 were found to be essential for LAL activity. We conclude that glycosylation plays an important role in the formation of functional LAL.
ESTHER : Zschenker_2005_J.Biochem_137_387
PubMedSearch : Zschenker_2005_J.Biochem_137_387
PubMedID: 15809341
Gene_locus related to this paper: human-LIPA

Title : Lysosomal Acid lipase deficiency: correction of lipid storage by adenovirus-mediated gene transfer in mice - Du_2002_Hum.Gene.Ther_13_1361
Author(s) : Du H , Heur M , Witte DP , Ameis D , Grabowski GA
Ref : Hum Gene Therapy , 13 :1361 , 2002
Abstract : Lysosomal acid lipase (LAL) is the essential enzyme for hydrolysis of triglycerides (TGs) and cholesteryl esters (CEs) in lysosomes. Its deficiency produces two human phenotypes: Wolman disease (WD) and cholesteryl ester storage disease (CESD). The LAL null (lal(-/-)) mouse mimicks aspects of human WD and CESD. The potential for gene therapy of LAL deficiency was tested with first-generation adenoviral vectors containing human LAL cDNA (Ad-hLAL) by intravenous injection into lal(-/-) mice. Compared with phosphate-buffered saline-injected controls, the mice receiving Ad-hLAL had increased hepatic LAL activity, decreased hepatomegaly, and normalization of histopathology. hLAL protein and mRNA were detected by immunohistochemical staining and in situ hybridization in hepatic parenchymal and sinusoid lining cells, splenic sinusoidal cells, lung macrophages, and adrenal cortical cells. Mice showed TG reductions in liver, spleen, and small intestine of 68, 54, and 50%, respectively, and cholesterol reductions of 55, 52, and 34%, respectively, at 20 days postinjection. These studies provide the basis for the use of gene therapy, in the form of gene transfer via intravenously administered adenovirus, to correct deficiency states, such as WD and CESD, and histopathology of a variety of tissues.
ESTHER : Du_2002_Hum.Gene.Ther_13_1361
PubMedSearch : Du_2002_Hum.Gene.Ther_13_1361
PubMedID: 12162818
Gene_locus related to this paper: mouse-1llip

Title : Characterization of lysosomal acid lipase mutations in the signal peptide and mature polypeptide region causing Wolman disease - Zschenker_2001_J.Lipid.Res_42_1033
Author(s) : Zschenker O , Jung N , Rethmeier J , Trautwein S , Hertel S , Zeigler M , Ameis D
Ref : J Lipid Res , 42 :1033 , 2001
Abstract : Wolman disease results from an inherited deficiency of lysosomal acid lipase (LAL; EC This enzyme is essential for the hydrolysis of cholesteryl esters and triacylglycerols derived from endocytosed lipoproteins. Because of a complete absence of LAL activity, Wolman patients accumulate progressive amounts of cholesteryl esters and triacylglycerols in affected tissues. To investigate the nature of the genetic defects causing this disease, mutations in the LAL gene from three subjects of Moslem-Arab and Russian descent living in Israel were determined. Two homozygotes for a novel 1-bp deletion introducing a premature in-frame termination codon at amino acid position 106 (S106X) were identified. A third subject was a homozygote for a G-5R signal peptide substitution and a G60V missense mutation. The functional significance of these mutations was tested by in vitro expression of single and double mutants in Spodoptera frugiperda cells. Single mutants G60V and S106X and double mutant G-5R/G60V displayed a virtual absence of lipase activity in cell extracts and culture medium. Signal peptide mutant G-5R retained lipase activity in cell extracts and showed a drastically reduced enzyme activity in culture supernatant, indicating that the mutation may affect secretion of active enzyme from cells. These results support the notion that Wolman disease is a genetically heterogeneous disorder of lipid metabolism.
ESTHER : Zschenker_2001_J.Lipid.Res_42_1033
PubMedSearch : Zschenker_2001_J.Lipid.Res_42_1033
PubMedID: 11441129
Gene_locus related to this paper: human-LIPA

Title : Different missense mutations in histidine-108 of lysosomal acid lipase cause cholesteryl ester storage disease in unrelated compound heterozygous and hemizygous individuals - Ries_1998_Hum.Mutat_12_44
Author(s) : Ries S , Buchler C , Schindler G , Aslanidis C , Ameis D , Gasche C , Jung N , Schambach A , Fehringer P , Vanier MT , Belli DC , Greten H , Schmitz G
Ref : Hum Mutat , 12 :44 , 1998
Abstract : Cholesteryl ester storage disease (CESD) and Wolman disease (WD) are both autosomal recessive disorders associated with reduced activity of lysosomal acid lipase (LAL), that leads to the tissue accumulation of cholesteryl esters in endosomes and lysosomes. WD is caused by genetic defects of LAL that leave no residual enzymatic activity, while in CESD patients a residual LAL activity can be identified. We have analyzed the LAL cDNA in three CESD patients from two nonrelated families and identified the mutations responsible for the disease. The associated genetic defects characterized revealed compound heterozygosity for a splice defect leading to skipping of exon 8, due to a G-->A transition at position -1 of the exon 8 splice donor site, and a point mutation leading to a Hisl08Pro change (CAT-->CCT) in two patients (siblings) with mild CESD phenotype. A further CESD patient was hemizygous for a His108-->Arg missense mutation (CAT-->CGT) in combination with a partial deletion of the LAL gene and was affected more severely. Expression of the LAL enzymes with the His108-->Pro and His108-->Arg mutation in insect cells revealed residual enzymatic activities of 4.6% versus 2.7%, respectively, compared with controls. Therefore, His108 seems to play a crucial role in folding or catalytic activity of the lysosomal acid lipase. This is the first description of two different, naturally occurring mutations involving the same amino acid residue in the lysosomal acid lipase in unrelated CESD patients. Moreover, our results demonstrate that the variable manifestation of CESD can be explained by mutation-dependent, variable inactivation of the LAL enzyme.
ESTHER : Ries_1998_Hum.Mutat_12_44
PubMedSearch : Ries_1998_Hum.Mutat_12_44
PubMedID: 9633819
Gene_locus related to this paper: human-LIPA

Title : A 5' splice-region mutation and a dinucleotide deletion in the lysosomal acid lipase gene in two patients with cholesteryl ester storage disease - Ameis_1995_J.Lipid.Res_36_241
Author(s) : Ameis D , Brockmann G , Knoblich R , Merkel M , Ostlund RE, Jr. , Yang JW , Coates PM , Cortner JA , Feinman SV , Greten H
Ref : J Lipid Res , 36 :241 , 1995
Abstract : Cholesteryl ester storage disease (CESD) results from inherited deficiencies of the lysosomal hydrolase, acid lipase (LAL; E.C. To establish the molecular defects in LAL deficiency, two unrelated probands with severely reduced LAL activity were examined. DNA amplification by reverse-transcription polymerase chain reaction and subsequent sequence analysis of LAL cDNA identified two mutant alleles. Patient 1, presenting with hepatosplenomegaly, mildly elevated liver function tests, and hyperlipidemia, was homozygous for a deletion of nucleotides 823 to 894 of the LAL cDNA. This 72-bp deletion maintained the reading frame and resulted in a loss of 24 amino acids from the LAL protein. Analysis of genomic DNA revealed that the 72 bp corresponded to an exon of the LAL gene. A single G to A point mutation at the last exon position was observed in the genomic DNA of patient 1, indicating a splicing defect with consecutive exon skipping underlying the 72-bp deletion. Patient 2 was a compound heterozygote for the 72-bp deletion and a dinucleotide deletion at positions 967 and 968. This deletion resulted in a shifted reading frame carboxyterminal of codon 296, and 43 random amino acids followed the frame shift. A premature stop at codon 339 truncated the mutant LAL protein by 34 amino acids. Allele-specific hybridization confirmed that patient 1 was homozygous for the 72-bp deletion mutation, and that patient 2 was a compound heterozygote for the 72-bp deletion and the 2-bp deletion.
ESTHER : Ameis_1995_J.Lipid.Res_36_241
PubMedSearch : Ameis_1995_J.Lipid.Res_36_241
PubMedID: 7751811
Gene_locus related to this paper: human-LIPA

Title : Purification, characterization and molecular cloning of human hepatic lysosomal acid lipase - Ameis_1994_Eur.J.Biochem_219_905
Author(s) : Ameis D , Merkel M , Eckerskorn C , Greten H
Ref : European Journal of Biochemistry , 219 :905 , 1994
Abstract : Lysosomal acid lipase (LAL) is a hydrolase essential for the intracellular degradation of cholesteryl esters and triacylglycerols. This report describes a multi-step procedure for the purification of LAL from human liver. After solubilization with non-ionic detergent, acid hydrolase activity was purified 17000-fold to apparent homogeneity by sequential chromatography on Concanavalin A Sepharose, carboxymethyl-cellulose, phenyl Superose, Mono S cation exchange and Superose 12 gel-filtration columns. This procedure yielded two silver-staining protein bands of 56 kDa and 41 kDa on SDS/PAGE. Size-exclusion chromatography of the 41-kDa protein indicated that the enzyme was catalytically competent as a monomer of approximately 38 kDa. When assayed in the presence of cholesteryl oleate or trioleoylglycerol, purified acid lipase had Vmax values of 4390 nmol fatty protein and 4756 nmol fatty protein-1, and apparent Km values of 0.142 mM and 0.138 mM, respectively. The purified enzyme was most active at low pH (4.5-5.0) and required non-ionic detergent and ethylene glycol for optimal stability. Incubation of the 41-kDa acid lipase with endoglucosaminidase H reduced the molecular mass by 4-6 kDa, demonstrating Asn-linked glycosylation with high-mannose oligosaccharides. Deglycosylation did not affect enzymic activity, indicating that carbohydrates are not required for LAL activity. Based on partial peptide sequence, an oligonucleotide was synthesized and utilized to isolate LAL cDNA clones from a human liver cDNA library. A full-length LAL cDNA contained 2626 nucleotides and coded for a predicted protein of 372 amino acids, preceded by a 27 residue hydrophobic signal peptide. Hepatic LAL differed from fibroblast acid lipase at the N-terminus and revealed extensive similarities with human gastric lipase and rat lingual lipase, confirming a gene family of acid lipases. Northern hybridization using the complete LAL cDNA as a radiolabeled probe indicated striking differences in mRNA expression among human tissues. LAL mRNA was most abundant in brain, lung, kidney and mammary gland. Placenta and HeLa cells expressed intermediate amounts of LAL mRNA, while RNA extracted from liver and heart showed low levels of expression.
ESTHER : Ameis_1994_Eur.J.Biochem_219_905
PubMedSearch : Ameis_1994_Eur.J.Biochem_219_905
PubMedID: 8112342
Gene_locus related to this paper: human-LIPA

Title : Trp64->nonsense mutation in the lipoprotein lipase gene - Sprecher_1992_J.Lipid.Res_33_859
Author(s) : Sprecher DL , Kobayashi J , Rymaszewski M , Goldberg IJ , Harris BV , Bellet PS , Ameis D , Yunker RL , Black DM , Stein EA , Schotz MC , Wiginton DA
Ref : J Lipid Res , 33 :859 , 1992
Abstract : A lipoprotein lipase (LpL) gene defect has been identified, a G->A transition at nucleotide position 446 of exon 3, resulting in a premature termination codon (Trp----stop) at amino acid residue 64. This defect was identified in a Type I hyperlipoproteinemic subject with an amino acid residue 194 defect in the other allele. Plasma lipoprotein values as well as LpL mass and activity in postheparin plasma were determined in the subjects with the residue 64 defect and in other LpL-deficient heterozygotes. LpL mass levels in both the Type I and the other subject with a 64 LpL defect were markedly reduced. This may be explained by rapid degradation of LpL protein or decreased secretion from the 64 defective allele. Alternatively, the marked reduction or absence of mass associated with the 64 defect may be due to synthesis of a severely truncated protein which escapes immunologic detection.
ESTHER : Sprecher_1992_J.Lipid.Res_33_859
PubMedSearch : Sprecher_1992_J.Lipid.Res_33_859
PubMedID: 1512512

Title : Hepatic and plasma lipases -
Author(s) : Ameis D , Greten H , Schotz MC
Ref : Semin Liver Dis , 12 :397 , 1992
PubMedID: 1465623

Title : A heterozygous mutation (the codon for Ser447----a stop codon) in lipoprotein lipase contributes to a defect in lipid interface recognition in a case with type I hyperlipidemia - Kobayashi_1992_Biochem.Biophys.Res.Commun_182_70
Author(s) : Kobayashi J , Nishida T , Ameis D , Stahnke G , Schotz MC , Hashimoto H , Fukamachi I , Shirai K , Saito Y , Yoshida S
Ref : Biochemical & Biophysical Research Communications , 182 :70 , 1992
Abstract : Previously, we reported a case with type I hyperlipidemia due to a lipid interface recognition deficiency in lipoprotein lipase (LPL) (1). The LPL from postheparin plasma of this patient did not hydrolyze TritonX-100-triolein or very low density lipoprotein-triolein but did hydrolyze tributyrin and LysoPC-triolein substrates. Sequence analysis of the probands DNA revealed a heterozygous nucleotide change: a C----G transversion at position of 1595, resulting in changing the codon for Ser447 to a stop codon. Expression studies of this mutant LPLcDNA in Cos-1 cells produced and secreted considerable amounts of LPL mass in the culture media. The mutated LPL hydrolyzed much less TritonX-100-triolein than wild type LPL, whereas hydrolysis of tributyrin and LysoPC--triolein was the same with both the mutant and wild type LPL. These results suggest that this mutation might be responsible for the property of the LPL with a defect in lipid interface recognition in the type I patient we reported.
ESTHER : Kobayashi_1992_Biochem.Biophys.Res.Commun_182_70
PubMedSearch : Kobayashi_1992_Biochem.Biophys.Res.Commun_182_70
PubMedID: 1731801

Title : cDNA cloning of carboxyl ester lipase from human pancreas reveals a unique proline-rich repeat unit - Reue_1991_J.Lipid.Res_32_267
Author(s) : Reue K , Zambaux J , Wong H , Lee G , Leete TH , Ronk M , Shively JE , Sternby B , Borgstrom B , Ameis D , Schotz MC
Ref : J Lipid Res , 32 :267 , 1991
Abstract : We report the isolation and nucleotide sequence of the cDNA for carboxyl ester lipase (CEL) from human pancreas. CEL was purified from human pancreas and microsequence analysis was performed on the amino-terminal and internal peptides. Peptide sequence was used to design oligonucleotide probes for screening a human pancreas cDNA library. Partial length cDNAs for CEL were isolated from the library, and the 5' portion of the cDNA was obtained using the anchored polymerase chain reaction. The deduced amino acid sequence indicates that mature CEL contains 722 amino acids and is synthesized with a 20 amino acid leader peptide. The amino acid sequence is rich in proline (12.2%), with 68% of the proline residues occurring within the final 25% of protein length. This is due to the occurrence of a series of proline-rich tandem repeat units near the carboxyl terminus, and accounts for the previously observed species variation in CEL size and amino acid composition. The primary sequence of CEL shows strong similarity to members of the serine esterase family, including the identical G-E-S-A-G motif at the putative active site. A striking homology also occurs between CEL and acetylcholinesterase and cholinesterase, essential enzymes of the nervous system. Proteins with cholesteryl esterase activity have been detected in extra-pancreatic tissues including liver, intestine, kidney, aorta, macrophage, and in the milk of some species (human, gorilla, cat, dog), but not others (rat, cow). To clarify the structural relationships between these various esterases and CEL, we used the CEL cDNA to study expression in pancreas and liver. CEL mRNA was abundant in pancreas of human and rat, with the human CEL mRNA approximately 300 nucleotides larger than that from rat. CEL mRNA was not detected in human adult or fetal liver, nor in rat liver. These results indicate that CEL is not synthesized in significant amounts in liver, and suggest that the cholesterol esterase activity that has been described in liver may be due to a distinct enzyme, or may be derived from pancreas, as has been proposed for the cholesterol esterase activity in intestine.
ESTHER : Reue_1991_J.Lipid.Res_32_267
PubMedSearch : Reue_1991_J.Lipid.Res_32_267
PubMedID: 2066663
Gene_locus related to this paper: human-CEL

Title : Familial chylomicronemia (type I hyperlipoproteinemia) due to a single missense mutation in the lipoprotein lipase gene - Ameis_1991_J.Clin.Invest_87_1165
Author(s) : Ameis D , Kobayashi J , Davis RC , Ben-Zeev O , Malloy MJ , Kane JP , Lee G , Wong H , Havel RJ , Schotz MC
Ref : J Clinical Investigation , 87 :1165 , 1991
Abstract : Complete deficiency of lipoprotein lipase (LPL) causes the chylomicronemia syndrome. To understand the molecular basis of LPL deficiency, two siblings with drastically reduced postheparin plasma lipolytic activities were selected for analysis of their LPL gene. We used the polymerase chain reaction to examine the nine coding LPL exons in the two affected siblings and three relatives. DNA sequence analysis revealed a single nucleotide change compared with the normal LPL cDNA: a G----A substitution at nucleotide position 680. This transition caused a replacement of glutamic acid for glycine at amino acid residue 142 of the mature LPL protein. Amino acid sequence comparisons of the region surrounding glycine-142 indicated that it is highly conserved among lipases from different species, suggesting a crucial role of this domain for the LPL structure. Expression studies of the mutant LPL cDNA in COS-7 cells produced normal amounts of enzyme mass. However, the mutated LPL was not catalytically active, nor was it efficiently secreted from the cells. This established that the Gly----Glu substitution at amino acid 142 is sufficient to abolish enzymatic activity and to result in the chylomicronemia syndrome observed in these patients.
ESTHER : Ameis_1991_J.Clin.Invest_87_1165
PubMedSearch : Ameis_1991_J.Clin.Invest_87_1165
PubMedID: 2010533
Gene_locus related to this paper: human-LPL

Title : Hepatic lipase: site-directed mutagenesis of a serine residue important for catalytic activity - Davis_1990_J.Biol.Chem_265_6291
Author(s) : Davis RC , Stahnke G , Wong H , Doolittle MH , Ameis D , Will H , Schotz MC
Ref : Journal of Biological Chemistry , 265 :6291 , 1990
Abstract : Hepatic lipase (HL) is a member of the lipoprotein lipase/pancreatic lipase gene family and is believed to function in processing of intermediate and high density lipoproteins. As a lipase, HL is presumed to have a lipid interfacial binding domain, distinct from the esterase catalytic site, orienting the enzyme at aqueous-lipid interfaces and resulting in activation of esterase activity. However, the structural domains responsible for these separate functions have not been identified. Amino acid sequence homology to serine proteases, thioesterases and other lipases, identified Ser147 of rat HL as part of a highly conserved element in an esterase gene family. In order to better define the function of this domain in HL, site-directed mutagenesis was utilized to produce mutant cDNAs with amino acid substitutions for Ser147, Ser133, or Ser228. Following injection of Xenopus oocytes with SP6 transcripts for normal or mutant HL, media from the oocytes were assayed for lipolytic activity and immunoprecipitable HL protein. Mutations of Ser133 and Ser228 produced no decrease in activity whereas the mutant protein in which Ser147 was replaced with glycine had little, if any activity against emulsified triolein substrates. Replacing HL Ser147 with glycine also resulted in a protein with little or no measurable activity for tributyrin, a substrate which does not provide a lipid interface. These results suggest that Ser147 in rat HL is either located at the catalytic site or is required for maintaining the structural integrity of the catalytic site.
ESTHER : Davis_1990_J.Biol.Chem_265_6291
PubMedSearch : Davis_1990_J.Biol.Chem_265_6291
PubMedID: 2108159

Title : Isolation and characterization of the human hepatic lipase gene - Ameis_1990_J.Biol.Chem_265_6552
Author(s) : Ameis D , Stahnke G , Kobayashi J , McLean J , Lee G , Buscher M , Schotz MC , Will H
Ref : Journal of Biological Chemistry , 265 :6552 , 1990
Abstract : Overlapping bacterial phage and cosmid genomic clones were isolated spanning an area of approximately 60 kilobases that contains the human hepatic lipase (HL) gene. It is composed of 9 exons spanning approximately 35 kilobases of DNA. The entire coding regions, the 5'-flanking sequences, and the exon-intron junctions were sequenced. The intron positions correspond to those of human lipoprotein lipase and canine pancreatic lipase, supporting the concept that these genes constitute a dispersed gene family of lipases and have evolved by duplication of a common ancestral gene. A region of the HL gene, which displays a significant homology with various other lipolytic enzymes and contains the putative catalytic site serine residue of HL, was encoded by exon 4. A major transcription start site of the human HL gene was located by primer extension analysis, 43 nucleotides upstream of the translation initiation codon. Two possible promoter elements were located 25 and 63 nucleotides upstream of the transcription initiation site: a "TATA" box-like sequence, TAATA, and a sequence found in the promoter region of many liver-specific genes, AGGTTAATTATTAAT. In addition, sequences homologous to glucocorticoid and cAMP-responsive elements were identified in the 5'-nontranscribed region.
ESTHER : Ameis_1990_J.Biol.Chem_265_6552
PubMedSearch : Ameis_1990_J.Biol.Chem_265_6552
PubMedID: 2324091
Gene_locus related to this paper: human-LIPC

Title : Organization of the human lipoprotein lipase gene and evolution of the lipase gene family - Kirchgessner_1989_Proc.Natl.Acad.Sci.U.S.A_86_9647
Author(s) : Kirchgessner TG , Chuat JC , Heinzmann C , Etienne J , Guilhot S , Svenson K , Ameis D , Pilon C , d'Auriol L , Andalibi A , et al.
Ref : Proc Natl Acad Sci U S A , 86 :9647 , 1989
Abstract : The human lipoprotein lipase gene was cloned and characterized. It is composed of 10 exons spanning approximately equal to 30 kilobases. The first exon encodes the 5'-untranslated region, the signal peptide plus the first two amino acids of the mature protein. The next eight exons encode the remaining 446 amino acids, and the tenth exon encodes the long 3'-untranslated region of 1948 nucleotides. The lipoprotein lipase transcription start site and the sequence of the 5'-flanking region were also determined. We compared the organization of genes for lipoprotein lipase, hepatic lipase, pancreatic lipase, and Drosophila yolk protein 1, which are members of a family of related genes. A model for the evolution of the lipase gene family is presented that involves multiple rounds of gene duplication plus exon-shuffling and intron-loss events.
ESTHER : Kirchgessner_1989_Proc.Natl.Acad.Sci.U.S.A_86_9647
PubMedSearch : Kirchgessner_1989_Proc.Natl.Acad.Sci.U.S.A_86_9647
PubMedID: 2602366