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PubMed1995

Differential responses of hormone-sensitive lipase gene to nutritional transition in adipose tissue, liver, and skeletal muscle of pigs.

To study the regulation of hormone-sensitive lipase gene in pigs, we amplified and sequenced partial porcine hormone-sensitive lipase cDNA. Nucleotide analysis indicated that porcine hormone-sensitive lipase cDNA was 86% homologous with the rat. In agreement with the rat, a 3.3 kb mRNA transcript was detected in adipose tissue but not in skeletal muscle of pigs by Northern hybridization. With more sensitive PCR method, hormone-sensitive lipase mRNA was found in adipose tissue, liver, heart, skeletal muscle, testis, and spleen. The gene expression in adipose tissue and liver was elevated after 2 days of fasting, and refeeding for another 2 days decreased the mRNA abundance. In contrast, the levels in skeletal muscle were not altered during identical nutritional transition. Combined evidences suggest that differential control may occur in porcine hormone-sensitive lipase gene in a tissue-specific fashion.

Adipose Tissue↗
PubMed2006

Use of an inhibitor to identify members of the hormone-sensitive lipase family.

Hormone-sensitive lipase (HSL) contributes importantly to the mobilization of fatty acids from the triacylglycerols stored in adipocytes, which provide the main source of energy in mammals. On the basis of amino acid sequence alignments and three-dimensional structures, this enzyme was previously found to be a suitable template for defining a family of serine carboxylester hydrolases. In this study, the HSL family members are characterized rather on the basis of their inhibition by 5-methoxy-3-(4-phenoxyphenyl)-3H-[1,3,4]oxadiazol-2-one (compound 7600). This compound inhibits mammalian HSL as well as other HSL family members, such as EST2 from the thermophilic eubacterium Alicyclobacillus acidocaldarius and AFEST from the hyperthermophilic archaeon Archaeoglobus fulgidus. Various carboxylester hydrolases that are not members of the HSL family were found not to be inhibited by compound 7600 under the same experimental conditions. These include nonlipolytic hydrolases such as Torpedo californica acetylcholinesterase and pig liver esterase, as well as lipolytic hydrolases such as human pancreatic lipase, dog gastric lipase, Thermomyces lanuginosus lipase, and Bacillus subtilis LipA. When vinyl esters were used as substrates, the residual activity of HSL, AFEST, and EST2 decreased with an increase in compound 7600 concentration in the incubation mixture. The inhibitor concentration at which the enzyme activity decreased to 50% after incubation for 5 min was 70, 20, and 15 nM with HSL, AFEST, and EST2, respectively. Treating EST2 and AFEST with the inhibitor resulted in an increase in the molecular mass, as established by performing matrix-assisted laser desorption ionization time-of-flight mass spectrometry analysis. This increase in the molecular mass, which corresponds approximately to the molecular mass of the inhibitor, indicates that a covalent enzyme-inhibitor complex has been formed. Surface-enhanced laser desorption ionization time-of-flight mass spectrometry analysis of a trypsin digest of AFEST treated with the inhibitor or not treated showed the occurrence of an increase in the molecular masses of the "GESAGG"-containing peptide, which is compatible with the formation of a covalent complex with the inhibitor.

Amino Acid Sequence↗
PubMed1996

[The hormonal sensitivity of glomerulonephritis patients].

Hormone sensitivity in patients suffering from glomerulonephritis of nephrotic type was assessed cytochemically by corticosteroid action on activity of mitochondrial enzymes (alpha-glycerophosphate dehydrogenase, succinate dehydrogenase) and by sensitivity of peripheral blood mononuclear cells to antiproliferative effect of dexamethasone in vitro. In glucocorticosteroid-sensitive patients the activity of alpha-glycerophosphate dehydrogenase, succinate dehydrogenase rises in interaction with prednisolone in vitro. In the resistant patients enzymatic activity in lymphocytes came down, peripheral blood mononuclear cells before and in the course of treatment retained resistance to glucocorticoids irrespective of the treatment results. Alpha-glycerophosphate dehydrogenase to succinate dehydrogenase index varied from 0 to 0.33 and 0.4 to 5.1 in the resistant and sensitive patients, respectively.

Adult↗
PubMed1987

Immunological evidence for the presence of hormone-sensitive lipase in rat tissues other than adipose tissue.

A polyclonal rabbit antibody was used to detect hormone-sensitive lipase in rat organs other than white adipose tissue. Inhibition of tissue diacylglycerol lipase activity by the anti-hormone-sensitive lipase, and by NaF, Hg2+ and diisopropyl fluorophosphate, known inhibitors of the hormone-sensitive lipase, demonstrated its presence in the adrenals, ovaries, testes, heart and skeletal muscle, but not in the liver and kidneys. After enrichment by immunoprecipitation an immunoreactive protein, corresponding to the adipose tissue hormone-sensitive lipase 84 kDa subunit, and some additional, higher Mrapp proteins, were detected by Western blotting in the same tissues. The adipose tissue contained greater than 80% of the total hormone-sensitive lipase, with 5-10- and 50-100-fold lower specific activity in the steroid-producing and the muscle tissues, respectively.

Adipose Tissue↗
PubMed1992

Adipose hormone-sensitive lipase preferentially releases polyunsaturated fatty acids from triglycerides.

Rat adipose hormone-sensitive lipase-mediated release of fatty acids from triglycerides was studied in three model systems: i) cultured preadipocytes containing polyunsaturated fatty acid-enriched triglyceride; ii) perfused epididymal fat pads; and iii) in vitro incubations of crude preparations of hormone-sensitive lipase with synthetic triglyceride-analogues as substrates. We found that cultured preadipocytes challenged with 10 microM norepinephrine tended to release more omega 6 and omega 3 polyunsaturated fatty acids than saturated fatty acids. Fat pads perfused with 10 microM norepinephrine preferentially released arachidonate and alpha-linolenate but tended to retain oleate and linoleate. Finally, crude preparations of hormone-sensitive lipase released from the triglyceride-analogue substrates alpha-linolenate twice as fast as oleate. We conclude that rat adipose hormone-sensitive lipase preferentially releases polyunsaturated fatty acids from triglycerides. We suggest that this may be a mechanism by which these fatty acids are kept from being trapped in fat depots and maintained in the circulation.

Adipose Tissue↗
PubMed1983

Hormone-sensitive magnesium transport in murine S49 lymphoma cells: characterization and specificity for magnesium.

1. The hormone-sensitive transport of Mg(2+) into murine S49 lymphoma cells and its relationship to other divalent cation transport systems have been investigated.2. Mg(2+) influx, measured with (28)Mg(2+), is saturable with an apparent extracellular ion concentration at half-maximal influx (K(in)) for Mg(2+) of 330 muM and a maximal influx rate of 360 p-mole/min.10(7) cells (2.9 n-mole/min.mg cell protein or a flux rate of about 0.12 p-mole/sec.cm(2)). Efflux of Mg(2+) is biphasic with half-times of 55 and 240 min at 37 degrees C and is temperature-sensitive.3. beta-Adrenergic agonists inhibit influx but not efflux of Mg(2+) in S49 cells. Efflux of Mg(2+) is also unaffected by extracellular [Mg(2+)] or [Ca(2+)]. These results imply that the mechanism of the transport system does not involve Mg-Mg exchange.4. Mn(2+) is a non-competitive inhibitor of Mg(2+) influx with an inhibition constant, K(i), of about 200 muM. The weak inhibition exhibited by Ca(2+) (K(i) > 5 mM) is also non-competitive. La(3+) inhibits Mg(2+) transport half-maximally at about 100 muM; Ni(2+), Zn(2+), Co(2+) and Sc(3+) are all less effective than La(3+). The Ca(2+)-channel blockers cis-diltiazem, verapamil, and nifedipine and the monovalent cations Na(+) and K(+) also have no effect on Mg(2+) influx. However, increasing the extracellular pH stimulates Mg(2+) influx.5. Total cellular Mg(2+) is about 85 n-mole/10(7) cells; however, at apparent isotopic equilibrium with (28)Mg(2+) less than 3% of total cellular Mg(2+) has been exchanged. This indicates that cellular Mg(2+) is highly compartmented and that recently transported Mg(2+) exchanges very slowly with bulk intracellular Mg(2+).6. Ca(2+) influx has a K(in) of 80 muM and is much slower than Mg(2+) influx. V(max) varied in different experiments from 3 to 15 p-mole/min.10(7) cells (25-125 p-mole/min.mg cell protein). Efflux of Ca(2+) is biphasic with half-times of 22 and 200 min and is temperature-sensitive. Hormonal stimulation has no effect on either influx or efflux of Ca(2+). Mg(2+) is a competitive inhibitor of Ca(2+) influx (K(i) = 3 mM).7. Two kinetic components of Mn(2+) influx are present with apparent K(in)s of 4 muM and 100 muM. Maximal influx rates are 5 and 60 p-mole/min.10(7) cells (40 and 480 p-mole/min.mg cell protein), respectively. Influx of Mn(2+) is not altered by beta-adrenergic agonist.8. Uptake of Na(+) or K(+) is unaltered by beta-adrenergic stimulation. These data in the S49 lymphoma cell indicate that (a) Mg(2+) is translocated by a transport system independent of those that transport other divalent cations, (b) hormonal inhibition of divalent ion transport is specific for Mg(2+) and (c) cellular Mg(2+) is highly compartmented.

Animals↗
PubMed2003

Increased hepatic insulin sensitivity together with decreased hepatic triglyceride stores in hormone-sensitive lipase-deficient mice.

Hormone-sensitive lipase (HSL) is a major enzyme for triglyceride (TG) lipolysis in adipose tissue. In HSL-knockout mice, plasma free fatty acid and TG levels are low, associated with low liver TG content. Because a decreased hepatic insulin sensitivity has been reported to be associated with high liver TG levels, our aim was to determine whether a hepatic TG content lower than normal, as observed in HSL-knockout mice, leads to increased hepatic insulin sensitivity. Therefore, hyperinsulinemic clamp experiments in combination with D-(3)H-glucose were used. Furthermore, hepatic insulin receptor and phosphorylated protein kinase B (PKB-P)/akt were analyzed by Western blotting. No significant differences where observed in insulin-mediated whole-body glucose uptake between HSL-knockout and control mice. Interestingly, hepatic insulin sensitivity of HSL-knockout mice was increased, because insulin caused a greater reduction in endogenous glucose production ( approximately 71% compared with approximately 31% in control mice; P < 0.05), despite decreased plasma adiponectin levels. PKB/akt phosphorylation and phosphatidylinositol-3-kinase activity was significantly higher in livers of HSL-knockout mice after insulin stimulation. In HSL-knockout mice, reduced hepatic TG stores result in an increased suppressive effect of insulin on hepatic glucose production, in line with an increased hepatic PKB-P/akt and phosphatidylinositol-3 kinase activity. Thus, hepatic insulin sensitivity is indeed increased after reducing hepatic TG stores below normal.

Adiponectin↗
PubMed1990

Biomodulator-mediated susceptibility of endogenous lipid droplets from rat adipocytes to hormone-sensitive lipase.

The amount of fatty acid release by a fat cell homogenate without pretreatment with epinephrine was found to be slightly more than that released from fat cells by epinephrine, suggesting that fat cells contain high lipolytic activity even in the absence of lipolytic agents. Fat cells contain high hormone-sensitive lipase activity (1383 mumole free fatty acids/g/hr) in the absence of epinephrine, and addition of epinephrine to the cells did not increase the activity, significantly. Like epinephrine, DBcAMP and/or theophylline also elicited marked release of glycerol from fat cells without activating the hormone-sensitive lipase activity. However, although fat cells contain a large amount of hormone-sensitive lipase, lipolysis was negligible in the absence of these lipolytic agents. These results suggest that lipolytic agents such as epinephrine, DBcAMP, and theophylline induce lipolysis in fat cells through some mechanism other than activation of hormone-sensitive lipase and that in the absence of lipolytic agents, some system in fat cells inhibits lipolysis of endogenous lipid droplets by hormone-sensitive lipase. The lipid droplets in fat cells consist mainly of triglyceride with phospholipids, cholesterol, carbohydrate, and protein as minor constituents. The phospholipid fraction was found to consist of 75% phosphatidylcholine and 25% phosphatidylethanolamine. Of the minor constituents of endogenous lipid droplets, only phosphatidylcholine strongly inhibited hormone-sensitive lipase activity in a [3H]triolein emulsion. These results suggest that phosphatidylcholine in endogenous lipid droplets may be responsible for inhibition of hormone-sensitive lipase. Then, a cell-free system was established in which epinephrine, DBcAMP, and theophylline stimulated lipolysis of endogenous lipid droplets from fat cells by lipase solution. In this system, these lipolytic agents did not induce lipolysis in the absence of added lipase. Lipolysis in the mixture of the endogenous lipid droplets and lipase solution was accelerated by phospholipase C with concomitant loss of epinephrine-induced lipolysis. After pretreatment of the endogenous lipid droplets with phospholipase C, these lipolytic agents no longer induced lipolysis. Pretreatment of the endogenous lipid droplets with phospholipase C reduced their phospholipid content with the formation of phosphorylcholine, but did not affect their triglyceride and cholesterol contents. Treatment of the endogenous lipid droplets with phospholipase D did not affect lipolysis in the cell-free system. These results suggest that phosphatidylcholine in the endogenous lipid droplets may inhibit their lipolysis by hormone-sensitive lipase in fat cells and also be involved in the mechanisms of the stimulatory effects of epinephrine, DBcAMP, and theophylline on lipolysis.

Adipose Tissue↗
PubMed1995

The hormone-sensitive early postnatal periods for sexual differentiation of feminine behavior and luteinizing hormone secretion in male and female rats.

The purpose of this study was to determine the duration of the hormone-sensitive postnatal period during which a single injection of testosterone propionate (TP) influences feminine behavior and luteinizing hormone (LH) secretion in male and female rats. Male pups were castrated on the day of birth (day 1) between 6 and 12 h postpartum. On postnatal day 3, 4, 5, 6, 7, 8, or 9 female pups and castrated males (fales) were injected subcutaneously with testosterone propionate (TP-500 micrograms). The females were laparotomized at 60 days of age, and ovarian tissue was removed for histological analysis. Female behavior was evaluated at 100 days of age. At 150 days of age, the ability of steroids to facilitate LH secretion was determined. Tests for lordosis indicated a diminished lordotic quotient (LQ) with both females and fales treated with TP on postnatal day 3, 4, 5, 6, or 7. On day 8 or 9, however, the lordotic response was at control levels. Females in all TP treated groups had significantly reduced number of corpora lutea. Females and fales treated with TP on postnatal day 3, 4, 5, 6, 7, 8, or 9 failed to exhibit an LH surge as adults. The results indicate that the neural control of feminine behavior (LQ) is hormone-sensitive to a single injection of TP up through the 7th day of postnatal life, whereas the neural substrate regulating LH secretion was sensitive in the present study at least up through day 9 in both fales and females.

Animals↗
PubMed2004

Hormone sensitivity is reflected in the phospholipid profiles of breast cancer cell lines.

We have found that the profiles of total phospholipids in malignant breast cancer cell lines change going from hormone sensitive to highly hormone resistant cells lines. In particular, two phospholipid components that were absent or at very low levels in hormone sensitive MCF7 cells and moderately hormone sensitive cell lines (MIII, LCC2) were found in relatively high proportions in highly hormone resistant cell lines (MB435, MB231). These two components were shown to be the alkylacylphosphatidylcholine (AAPtdC) and the unsaturated analog plasmenylphosphatidylethanolamine (plasmenyl-PtdE). Another component phosphatidylethanolamine (PtdE) increased in correlation with the degree of hormone insensitivity. This was shown using 31P NMR spectroscopy of lipid extracts of the cells, and was confirmed using HPLC analysis, as well as other techniques. The significance of these results for the metabolic characteristics of these cell lines is related to the therapeutic responsiveness of breast cancer.

Antineoplastic Agents, Hormonal↗
PubMed1992

[The criteria of the hormonal sensitivity of breast cancer].

The study deals with a complex approach to prognosis of hormone sensitivity in breast cancer patients on the basis of certain biological characteristics of tumor and the host. A number of clinical and morphological parameters were tested in 71 patients suffering breast tumors. The said parameters proved useful in determining hormone sensitivity and were used as a basis for indirect assay of estrogen receptors levels. Levels of estrogen (ER) and progesterone (PR) receptors and tumor sex chromatin (SC) were measured in 46 patients. Indirect determination of ER level should be recommended as an additional criterion for evaluating hormone sensitivity in breast cancer patients considering its findings matching (76-78.2%) those obtained in ER and PR assay by the labeled ligand binding method which uses dextran-covered charcoal. Close correlations (80.4%) and (sensitivity +1) were obtained for ER and PR, on the one hand, and that of sex chromatin, on the other, particularly, in ER+PR(+)-tumors. High concentration of sex chromatin in tumor is one of the most reliable criteria of measuring hormone sensitivity levels in breast cancer patients.

Adult↗
PubMed1983

Phosphorylation of hormone-sensitive lipase by cyclic AMP-dependent protein kinase.

Hormone-sensitive lipase, detergent-solubilized and purified from rat adipose tissue, was phosphorylated with the catalytic subunit of cyclic AMP-dependent protein kinase from the same tissue. Maximally 1.05 +/- 0.05 (mean +/- S.E. (n = 3) ) mol of phosphate/mol of hormone-sensitive lipase Mr = 84,000 subunit was incorporated. Phosphoserine was the only phosphorylated amino acid residue. A single phosphorylation site was demonstrated by digestion with Staphylococcus aureus V8 protease and trypsin that produced a single acidic phosphopeptide of about 10 amino acid residues length, which was isolated by two-dimensional electrophoresis-thin layer chromatography. Enzyme activity was enhanced, 2.5-fold against trioleoylglycerol, concomitant with phosphorylation, with half-maximal effect within 30 sec, a rate of phosphorylation of the enzyme comparable to that obtained in vivo (Nilsson, N. O., Strålfors, P., Fredrikson, G., and Belfrage, P. (1980) FEBS Lett. 111, 125-130). The initial rate of phosphorylation was approximately half that with phosphorylase kinase as substrate. The effects of modifications of hormone-sensitive lipase and of various additions and variation in pH were examined.

Adipose Tissue↗
PubMed1999

Lipotransin: a novel docking protein for hormone-sensitive lipase.

Lipotransin is a novel hormone-sensitive lipase (HSL)-interacting protein that appears to translocate HSL to the lipid droplet. The interaction of the two proteins depends upon the phosphorylation of HSL by protein kinase A. Once formed, the complex is dissociated by ATP hydrolysis, due to the ATPase activity of lipotransin. In 3T3L1 adipocytes, insulin produces a stable complex between the proteins, due to a modification of lipotransin. Thus, lipotransin is a novel docking protein that may direct the hormonally regulated redistribution of hormone-sensitive lipase.

3T3 Cells↗
PubMed1976

Effect of exercise on hormone-sensitive lipase activity in rat adipocytes.

Hormone-sensitive lipase activity was measured in adipocytes of rats subjected to a 12-wk program of treadmill running. Enzyme activity in the runners sacrificed immediately after exercise increased 2.5-fold (P less than 0.001) in tissue exposed to epinephrine and threefold (P less than 0.001) in tissue not exposed to epinephrine, when the results were expressed per gram of adipose tissue. Increases of almost the same magnitude were observed in runners sacrificed 24 h after their last bout of work. These significant increases in enzyme activity, however, were the result of a significant reduction in the size of cells in the epididymal fat pads of the exercisers compared with those of the freely eating sedentary animals (68.7 +/- 2.7 mum vs. 82.0 +/- 2.7 mum; P less than 0.01). When the results were expressed on a per-cell basis, therefore, hormone-sensitive lipase activity, assayed in the presence or absence of epinephrine, was unaffected by the exercise program. These results provide evidence that the lipolytic capacity of adipocytes of normal, untrained rats is sufficiently large to meet the increased demand for free fatty acids imposed by the exercise program without the need for an adaptive increase in enzyme activity.

Adipose Tissue↗
PubMed1983

Positional specificity of hormone-sensitive lipase from rat adipose tissue.

Hormone-sensitive lipase, purified from rat adipose tissue (Fredrikson, G., Strålfors, P., Nilsson, N. O., and Belfrage, P. (1981) J. Biol. Chem. 256, 6311-6320), has been incubated with tri-, di-, and monooleoyl[3H]glycerol, and the acylglycerol reaction products were isolated by thin layer chromatography on silicic acid, impregnated with boric acid. Trioleoylglycerol was hydrolyzed with the intermediate accumulation of monooleoylglycerol, mainly the 2-isomer, and a small amount of 1,2(2,3)-, but no measurable, 1,3-dioleoylglycerol. 2-Monooleoylglycerol was also the major acylglycerol reaction product from 1,2(2,3)-dioleoylglycerol hydrolysis, which occurred at a Vmax of 60% of that with the 1,3-isomer. Part of the 1(3)-monooleoylglycerols found were formed by acyl migration, but 2-ester bond cleavage was directly demonstrated by the use of 1,3-dioleoyl-2-[14C]oleoyl[3H]glycerol as substrate, and by determination of the 14C/3H ratios of the acylglycerol reaction products. Based on the hydrolysis of specific monooleoylglycerol isomers, it was estimated that the 1(3)-ester bonds of the acylglycerols were hydrolyzed 3- to 4-fold faster than the 2-ester bonds. The main lipolytic reaction sequence catalyzed by hormone-sensitive lipase is thus triacylglycerol leads to 1,2(2,3)-diacylglycerol leads to 2-monoacylglycerol. However, the preference for the 1(3)-ester bonds is less marked than that of, e.g. pancreatic and lipoprotein lipase.

Adipose Tissue↗
PubMed2005

Orbital metastasis from prostate cancer: an atypical case of neuroendocrine dedifferentiation during progression from hormone-sensitive to refractory stage.

We report a case of orbital metastasis from a neuroendocrine dedifferentiated prostate cancer during progression from hormone-sensitive to hormone refractory stage. A patient receiving androgen deprivation for hormone-sensitive prostate cancer presented with sudden-onset right-sided ptosis and an increasing serum prostate-specific antigen level. Imaging studies revealed a mixed blastic and lytic lesion involving the right orbital wall and the right cavernous sinus. Comparison of the metastatic histology with the original pathology confirmed a histologic change to poorly differentiated prostate adenocarcinoma with neuroendocrine features. Local radiation of the lesion and palliative systemic chemotherapy resulted in marked short-term improvement of all presenting symptoms. Because prostate cancer metastasis involves hematogenous and lymphatic routes, we also evaluated expression of the vascular endothelial growth factor (VEGF) and receptors (VEGFR-1, VEGFR-2, and VEGFR-3) in the metastatic deposit by immunohistochemistry. Strong expression of VEGFR-2 and VEGFR-3 restricted to the malignant epithelium was noted. We recommend a second biopsy of atypical prostate metastasis associated with sudden change to aggressive clinical behavior in order to evaluate for dedifferentiation features before planning appropriate treatment interventions especially in patients who are candidates for systemic chemotherapy.

Carcinoma, Neuroendocrine↗
PubMed1991

Expression of biologically active hormone-sensitive lipase in mammalian (COS) cells.

cDNAs encoding rat adipose tissue hormone-sensitive lipase were expressed in COS cells, under the control of the SV40 promoter to half the level in rat adipocytes, the richest native source of the enzyme. A cDNA lacking most of the long 5'-untranslated region of the full-length rat hormone-sensitive lipase cDNA was, with regard to the lipase activity, on the average 70% more efficiently expressed that the full-length cDNA. The recombinant protein was almost identical to hormone-sensitive lipase of rat adipose tissue with respect to specific activity, susceptibility to inhibitors, molecular size, phosphorylation and activation by cyclic AMP-dependent protein kinase. The described eukaryotic expression system will allow analysis of effects of amino acid substitutions introduced into the lipase molecule by site-directed mutagenesis.

Adenosine Monophosphate↗
PubMed2005

[Sequence and polymorphism analysis of porcine hormone-sensitive lipase gene 5'-UTR and exon I].

Hormone-sensitive lipase (HSL) is the key enzyme responsible for the mobilization of free acids from adipose tissue, and it is also the most important enzyme that affect fat deposition. In this paper, the porcine hormone-sensitive lipase gene 5'-UTR and exon I were sequenced. The sequence number in GenBank are AY332499, AY332497, AY332504, AY332505. A GC-CG in the DNA sequence -13 - -12 bp of porcine HSL gene 5'-UTR was detected between Duroc, Meishan, Qingping pig, Largewhite and Landrace. A G-->A missense mutation was detected in HSL gene exon I of different pig breeds. The characterization of the BsaH I PCR-RFLP polymorphism in exon I of the porcine HSL gene of different breeds and "Largewhite x Meishan" F2 group was analyzed. By association analysis between BsaH I PCR-RFLP polymorphism and GG, GG, AA genotypes of HSL gene exon I, a significant difference of pig eye area was found between AG and GG genotypes (P<0.05) in F2 group.

5' Flanking Region↗