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• W2094580301 abstract "Apolipoprotein A-II (apoA-II) is the second major apolipoprotein following apolipoprotein A-I (apoA-I) in HDL. ApoA-II has multiple physiological functions and can form senile amyloid fibrils (AApoAII) in mice. Most circulating apoA-II is present in lipoprotein A-I/A-II. To study the influence of apoA-I on apoA-II and AApoAII amyloidosis, apoA-I-deficient (C57BL/6J.Apoa1−/−) mice were used. Apoa1−/− mice showed the expected significant reduction in total cholesterol (TC), HDL cholesterol (HDL-C), and triglyceride (TG) plasma levels. Unexpectedly, we found that apoA-I deficiency led to redistribution of apoA-II in HDL and an age-related increase in apoA-II levels, accompanied by larger HDL particle size and an age-related increase in TC, HDL-C, and TG. Aggravated AApoAII amyloidosis was induced in Apoa1−/− mice systemically, especially in the heart. These results indicate that apoA-I plays key roles in maintaining apoA-II distribution and HDL particle size. Furthermore, apoA-II redistribution may be the main reason for aggravated AApoAII amyloidosis in Apoa1−/− mice. These results may shed new light on the relationship between apoA-I and apoA-II as well as provide new information concerning amyloidosis mechanism and therapy. Apolipoprotein A-II (apoA-II) is the second major apolipoprotein following apolipoprotein A-I (apoA-I) in HDL. ApoA-II has multiple physiological functions and can form senile amyloid fibrils (AApoAII) in mice. Most circulating apoA-II is present in lipoprotein A-I/A-II. To study the influence of apoA-I on apoA-II and AApoAII amyloidosis, apoA-I-deficient (C57BL/6J.Apoa1−/−) mice were used. Apoa1−/− mice showed the expected significant reduction in total cholesterol (TC), HDL cholesterol (HDL-C), and triglyceride (TG) plasma levels. Unexpectedly, we found that apoA-I deficiency led to redistribution of apoA-II in HDL and an age-related increase in apoA-II levels, accompanied by larger HDL particle size and an age-related increase in TC, HDL-C, and TG. Aggravated AApoAII amyloidosis was induced in Apoa1−/− mice systemically, especially in the heart. These results indicate that apoA-I plays key roles in maintaining apoA-II distribution and HDL particle size. Furthermore, apoA-II redistribution may be the main reason for aggravated AApoAII amyloidosis in Apoa1−/− mice. These results may shed new light on the relationship between apoA-I and apoA-II as well as provide new information concerning amyloidosis mechanism and therapy. HDL contains two major proteins, apoA-I and apoA-II, which compose about 70% and 20%, respectively, of the total HDL protein mass in humans. Both apoA-I and apoA-II have important physiological functions in lipid transport and metabolism. ApoA-I is distributed approximately equally between lipoprotein A-I (LpA-I) and lipoprotein A-I/lipoprotein A-II (LpA-I/A-II), whereas virtually all apoA-II is found with LpA-I/A-II (1Kontush A. Chapman M.J. Functionally defective HDL: a new therapeutic target at the crossroads of dyslipidemia, inflammation and atherosclerosis.Pharmacol. Rev. 2006; 58: 342-374Crossref PubMed Scopus (609) Google Scholar). LpA-I is a major component of both HDL2 and HDL3, while LpA-I/A-II is found predominantly in HDL3 (1Kontush A. Chapman M.J. Functionally defective HDL: a new therapeutic target at the crossroads of dyslipidemia, inflammation and atherosclerosis.Pharmacol. Rev. 2006; 58: 342-374Crossref PubMed Scopus (609) Google Scholar). This distribution suggests that there is a close relationship between these two apolipoproteins. ApoA-I, the major HDL protein in all vertebrates reported to date (2Chapman M.J. Animal lipoproteins: chemistry, structure, and comparative aspects.J. Lipid Res. 1980; 21: 789-853Abstract Full Text PDF PubMed Google Scholar), plays crucial roles in lipid transport and metabolism by activating LCAT and promoting cholesterol efflux from peripheral tissues (3Sorci-Thomas M.G. Bhat S. Thomas M.J. Activation of lecithin:cholesterol acyltransferase by HDL ApoA-I central helices.Clin. Lipidol. 2009; 4: 113-124Crossref PubMed Scopus (57) Google Scholar). Abundant data show that apoA-I has protective effects against atherosclerosis and cardiovascular disease in humans and mice, mainly by enhancing reverse cholesterol transport (RCT) and anti-inflammatory, antioxidant, or nitric-oxide-promoting properties (4Duffy D. Rader D.J. Update on strategies to increase HDL quantity and function.Nat. Rev. Cardiol. 2009; 6: 455-463Crossref PubMed Scopus (159) Google Scholar). Clinically, the majority of patients with severe HDL and apoA-I deficiencies suffer from premature atherosclerosis (5Schaefer E.J. Santos R.D. Asztalos B.F. Marked HDL deficiency and premature coronary heart disease.Curr. Opin. Lipidol. 2010; 21: 289-297Crossref PubMed Scopus (99) Google Scholar). The negative correlation between plasma HDL cholesterol (HDL-C) concentrations and atherosclerosis is not observed in all disorders involving apoA-I deficiency, however (4Duffy D. Rader D.J. Update on strategies to increase HDL quantity and function.Nat. Rev. Cardiol. 2009; 6: 455-463Crossref PubMed Scopus (159) Google Scholar). There are reports of mutations in the Apoa1 gene that cause severe reductions in HDL-C concentrations in plasma but do not appear to increase coronary risk (6Al-Sarraf A. Al-Ghofaili K. Sullivan D.R. Wasan K.M. Hegele R. Frohlich J. Complete ApoAI deficiency in an Iraqi Mandaean family: case studies and review of the literature.J. Clin. Lipidol. 2010; 4: 420-426Abstract Full Text Full Text PDF PubMed Scopus (14) Google Scholar). In addition, apoA-I deficiency alone does not promote development of atherosclerotic lesions in B6/129 mice (7Li H. Reddick R.L. Maeda N. Lack of apoA-I is not associated with increased susceptibility to atherosclerosis in mice.Arterioscler. Thromb. 1993; 13: 1814-1821Crossref PubMed Scopus (163) Google Scholar). Indeed, studies with transgenic mice highlight the physiological redundancy of HDL apolipoproteins (8Kalopissis A.D. Chambaz J. Transgenic animals with altered high-density lipoprotein composition and functions.Curr. Opin. Lipidol. 2000; 11: 149-153Crossref PubMed Scopus (17) Google Scholar). In addition to apoA-I, other apolipoproteins, such as apoE, apoA-II (9Lee M. Calabresi L. Chiesa G. Franceschini G. Kovanen P.T. Mast cell chymase degrades apoE and apoA-II in apoA-I-knockout mouse plasma and reduces its ability to promote cellular cholesterol efflux.Arterioscler. Thromb. Vasc. Biol. 2002; 22: 1475-1481Crossref PubMed Scopus (48) Google Scholar), and apoA-IV, are active in inducing cholesterol efflux from cells and may play important roles in substituting for the loss of apoA-I (10Duverger N. Tremp G. Caillaud J.M. Emmanuel F. Castro G. Fruchart J.C. Steinmetz A. Denefle P. Protection against atherogenesis in mice mediated by human apolipoprotein A-IV.Science. 1996; 273: 966-968Crossref PubMed Scopus (222) Google Scholar). ApoA-II, the second most abundant protein present in human, mouse, rat, and fish plasma HDL (11Blanco-Vaca F. Escolà-Gil J.C. Martín-Campos J.M. Julve J. Role of apoA-II in lipid metabolism and atherosclerosis: advances in the study of an enigmatic protein.J. Lipid Res. 2001; 42: 1727-1739Abstract Full Text Full Text PDF PubMed Google Scholar), was long considered to be of minor physiologically importance in lipoprotein metabolism because apoA-II deficiency is not associated with a high susceptibility to coronary heart disease (12Deeb S.S. Takata K. Peng R.L. Kajiyama G. Albers J.J. A splice-junction mutation responsible for familial apolipoprotein A-II deficiency.Am. J. Hum. Genet. 1990; 46: 822-827PubMed Google Scholar). However, recent studies show that apoA-II plays multiple metabolic roles in maintaining the plasma HDL pool (13Koike T. Kitajima S. Yu Y. Li Y. Nishijima K. Liu E. Sun H. Waqar A.B. Shibata N. Inoue T. et al.Expression of human apoAII in transgenic rabbits leads to dyslipidemia: a new model for combined hyperlipidemia.Arterioscler. Thromb. Vasc. Biol. 2009; 29: 2047-2053Crossref PubMed Scopus (45) Google Scholar–15Weng W. Breslow J.L. Dramatically decreased high density lipoprotein cholesterol, increased remnant clearance, and insulin hypersensitivity in apolipoprotein A-II knockout mice suggest a complex role for apolipoprotein A-II in atherosclerosis susceptibility.Proc. Natl. Acad. Sci. USA. 1996; 93: 14788-14794Crossref PubMed Scopus (123) Google Scholar), promoting obesity and insulin resistance (15Weng W. Breslow J.L. Dramatically decreased high density lipoprotein cholesterol, increased remnant clearance, and insulin hypersensitivity in apolipoprotein A-II knockout mice suggest a complex role for apolipoprotein A-II in atherosclerosis susceptibility.Proc. Natl. Acad. Sci. USA. 1996; 93: 14788-14794Crossref PubMed Scopus (123) Google Scholar, 16Castellani L.W. Goto A.M. Lusis A.J. Studies with apolipoprotein A-II transgenic mice indicate a role for HDLs in adiposity and insulin resistance.Diabetes. 2001; 50: 643-651Crossref PubMed Scopus (84) Google Scholar), augmenting monocyte responses to lipopolysaccharides (LPS) (17Thompson P.A. Berbée J.F. Rensen P.C. Kitchens R.L. Apolipoprotein A-II augments monocyte responses to LPS by suppressing the inhibitory activity of LPS-binding protein.Innate Immun. 2008; 14: 365-374Crossref PubMed Scopus (28) Google Scholar), and decreasing triglyceride catabolism, mainly by impairing lipoprotein lipase (LPL) activity (13Koike T. Kitajima S. Yu Y. Li Y. Nishijima K. Liu E. Sun H. Waqar A.B. Shibata N. Inoue T. et al.Expression of human apoAII in transgenic rabbits leads to dyslipidemia: a new model for combined hyperlipidemia.Arterioscler. Thromb. Vasc. Biol. 2009; 29: 2047-2053Crossref PubMed Scopus (45) Google Scholar). Although human apoA-II is either atheroprotective or pro-atherogenic in transgenic mice, depending on an atherogenic diet (18Escolà-Gil J.C. Marzal-Casacuberta A. Julve-Gil J. Ishida B.Y. Ordóñez-Llanos J. Chan L. González-Sastre F. Blanco-Vaca F. Human apolipoprotein A-II is a pro-atherogenic molecule when it is expressed in transgenic mice at a level similar to that in humans: evidence of a potentially relevant species-specific interaction with diet.J. Lipid Res. 1998; 39: 457-462Abstract Full Text Full Text PDF PubMed Google Scholar), mouse apoA-II is pro-atherogenic in chow-fed transgenic mice (19Warden C.H. Hedrick C.C. Qiao J.H. Castellani L.W. Lusis A.J. Atherosclerosis in transgenic mice overexpressing apolipoprotein A-II.Science. 1993; 261: 469-472Crossref PubMed Scopus (326) Google Scholar). In human hereditary amyloidosis, a rare disorder that may cause progressive and life-threatening organ dysfunction, apoA-II can form AApoAII amyloid fibrils, which are mainly deposited in the kidney (20Benson M.D. Liepnieks J.J. Yazaki M. Yamashita T. Hamidi A.K. Guenther B. Kluve-Beckerman B. A new human hereditary amyloidosis: the result of a stop-codon mutation in the apolipoprotein AII gene.Genomics. 2001; 72: 272-277Crossref PubMed Scopus (129) Google Scholar). In mice, apoA-II is a precursor of senile amyloid fibrils (AApoAII), which were first isolated from a senescence-accelerated inbred strain (SAMP1) having severe amyloidosis and were later found to be present universally in mice (21Xing Y. Higuchi K. Amyloid fibril proteins.Mech. Ageing Dev. 2002; 123: 1625-1636Crossref PubMed Scopus (61) Google Scholar). Mouse AApoAII amyloidosis fibrils are spontaneously deposited systemically (excluding the brain) in an age-associated manner (21Xing Y. Higuchi K. Amyloid fibril proteins.Mech. Ageing Dev. 2002; 123: 1625-1636Crossref PubMed Scopus (61) Google Scholar), resulting in a 20% shortened life span for R1.P1-Apoa2c mice (22Higuchi K. Wang J. Kitagawa K. Matsushita T. Kogishi K. Naiki H. Kitado H. Hosokawa M. Accelerated senile amyloidosis induced by amyloidogenic Apoa-II gene shortens the life span of mice but does not accelerate the rate of senescence.J. Gerontol. A Biol. Sci. Med. Sci. 1996; 51: B295-B302Crossref PubMed Scopus (20) Google Scholar). In laboratory mice, there are three major alleles for Apoa2: Apoa2a, Apoa2b, and Apoa2c (21Xing Y. Higuchi K. Amyloid fibril proteins.Mech. Ageing Dev. 2002; 123: 1625-1636Crossref PubMed Scopus (61) Google Scholar, 23Kitagawa K. Wang J. Mastushita T. Kogishi K. Hosokawa M. Fu X. Guo Z. Mori M. Higuchi K. Polymorphisms of mouse apolipoprotein A-II: seven alleles found among 41 inbred strains of mice.Amyloid. 2003; 10: 207-214Crossref PubMed Scopus (28) Google Scholar). We confirmed that strains carrying Apoa2a and Apoa2c are more susceptible to AApoAII amyloidosis than strains having Apoa2b (14Ge F. Yao J. Fu X. Guo Z. Yan J. Zhang B. Zhang H. Tomozawa H. Miyazaki J. Sawashita J. et al.Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2c).Lab. Invest. 2007; 87: 633-643Crossref PubMed Scopus (22) Google Scholar, 21Xing Y. Higuchi K. Amyloid fibril proteins.Mech. Ageing Dev. 2002; 123: 1625-1636Crossref PubMed Scopus (61) Google Scholar, 23Kitagawa K. Wang J. Mastushita T. Kogishi K. Hosokawa M. Fu X. Guo Z. Mori M. Higuchi K. Polymorphisms of mouse apolipoprotein A-II: seven alleles found among 41 inbred strains of mice.Amyloid. 2003; 10: 207-214Crossref PubMed Scopus (28) Google Scholar, 24Xing Y. Nakamura A. Korenaga T. Guo Z. Yao J. Fu X. Matsushita T. Kogishi K. Hosokawa M. Kametani F. et al.Induction of protein conformational change in mouse senile amyloidosis.J. Biol. Chem. 2002; 277: 33164-33169Abstract Full Text Full Text PDF PubMed Scopus (49) Google Scholar). To date, the influence of apoA-I on apoA-II is not clear. Although LpA-II, which lacks apoA-I and contains apoA-II as the main apolipoprotein constituent, was found in apoA-I-deficient patients (25Bekaert E.D. Alaupovic P. Knight-Gibson C. Norum R.A. Laux M.J. Ayrault-Jarrier M. Isolation and partial characterization of lipoprotein A-II (LP-A-II) particles of human plasma.Biochim. Biophys. Acta. 1992; 1126: 105-113Crossref PubMed Scopus (34) Google Scholar), there are no detailed data concerning the distribution of apoA-II. For mice lacking apoA-I, apoE is confirmed to increase in compensation, although whether this also occurs for apoA-II is not known (7Li H. Reddick R.L. Maeda N. Lack of apoA-I is not associated with increased susceptibility to atherosclerosis in mice.Arterioscler. Thromb. 1993; 13: 1814-1821Crossref PubMed Scopus (163) Google Scholar, 9Lee M. Calabresi L. Chiesa G. Franceschini G. Kovanen P.T. Mast cell chymase degrades apoE and apoA-II in apoA-I-knockout mouse plasma and reduces its ability to promote cellular cholesterol efflux.Arterioscler. Thromb. Vasc. Biol. 2002; 22: 1475-1481Crossref PubMed Scopus (48) Google Scholar). Recently, it was shown that apoA-I may also affect amyloidosis pathogenesis (26Lefterov I. Fitz N.F. Cronican A.A. Fogg A. Lefterov P. Kodali R. Wetzel R. Koldamova R. Apolipoprotein A-I deficiency increases cerebral amyloid angiopathy and cognitive deficits in APP/PS1 DeltaE9 mice.J. Biol. Chem. 2010; 285: 36945-36957Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). ApoA-I can bind amyloid β (Aβ), and decrease Aβ-induced cytotoxicity in vitro, as well as attenuate formation of Aβ amyloid deposits on central nervous system blood vessel walls in vivo (26Lefterov I. Fitz N.F. Cronican A.A. Fogg A. Lefterov P. Kodali R. Wetzel R. Koldamova R. Apolipoprotein A-I deficiency increases cerebral amyloid angiopathy and cognitive deficits in APP/PS1 DeltaE9 mice.J. Biol. Chem. 2010; 285: 36945-36957Abstract Full Text Full Text PDF PubMed Scopus (92) Google Scholar). However, there are few studies concerning the role of ApoA-I in other amyloidoses, including those associated with pathological disorders, such as primary (AL) amyloidosis, reactive (AA) amyloidosis, polyneuropathy (FAP), prion diseases, and familial, systemic, and sporadic amyloidosis. Using C57BL/6J.Apoa1−/− mice (with Apoa2a allele), we confirmed that apoA-I deficiency results in significantly reduced plasma levels of TC, HDL-C, and TG, as well as a 2-fold increased apoE level that was previously described by other studies (7Li H. Reddick R.L. Maeda N. Lack of apoA-I is not associated with increased susceptibility to atherosclerosis in mice.Arterioscler. Thromb. 1993; 13: 1814-1821Crossref PubMed Scopus (163) Google Scholar). Unexpectedly, we also found i) age-related increases in the levels of plasma apoA-II, TC, HDL-C, and TG; ii) redistribution of apoA-II and larger HDL particles; and iii) aggravated systemic AApoAII amyloidosis and heart amyloidosis in Apoa1−/− mice. These results prompted us to explore how the loss of apoA-I affects the metabolism of apoA-II. C57BL/6J mice were purchased from Japan SLC, Inc. (Hamamatsu, Japan), and C57BL/6J.Apoa1−/− mice (B6.129P2-Apoa1tm1Unc/J) were purchased from Jackson Laboratories (Bar Harbor, ME). The Apoa1tm1Unc mutant strain was developed in the laboratory of Dr. Nobuyo Maeda (27Williamson R. Lee D. Hagaman J. Maeda N. Marked reduction of high density lipoprotein cholesterol in mice genetically modified to lack apolipoprotein A-I.Proc. Natl. Acad. Sci. USA. 1992; 89: 7134-7138Crossref PubMed Scopus (190) Google Scholar). The C57BL/6J strain was produced by backcrossing the Apoa1tm1Unc mutation 10 times to C57BL/6J inbred mice. Mice were maintained by sister-brother matings under specific pathogen free (SPF) conditions at 24 ± 2°C with a light-controlled regimen (12 h light/dark cycle). Mouse pups were weaned at four weeks and then fed a commercial diet containing 5.6% fat (C18:2 linoleic acid, 48.4%; C18:1 linoleic acid, 23.2%; C16 palmitic acid, 14.1%; C18:3 linolenic acid, 4%; C18 stearic acid, 2.5%; C20:5 eicosapentaenoic acid, 1.6%; C22:6 docosahexaenoic acid, 1.4%; C16:1 palmitoleic acid, 1.4%; C14 myristic acid, 0.4%; and others, 2.0%) that was purchased from Oriental Yeast (Tokyo, Japan). Tap water was provided ad libitum. Only female mice were used in this study to avoid AA amyloidosis or other adverse impacts caused by fighting and other behaviors among mice reared in the same cage. Mice were euthanized by cardiac puncture under diethyl ether anesthesia. All experimental procedures were carried out in accordance with the Regulations for Animal Experimentation of Shinshu University. After an overnight fast, mice were sacrificed for plasma collection and other experiments, such as pathologic investigation. Levels of plasma TC, HDL-C, and TG were detected in duplicate determinations using commercially available kits (total cholesterol E-test kit, 439-17501; HDL-cholesterol E-test kit, 431-52501; Triglyceride E-test kit, 432-40201; Wako Pure Chemical Industries, Osaka, Japan). Pooled plasma of some groups was also analyzed with a dual-detection, high-performance liquid chromatography (HPLC) system (Liposearch System, Skylight Biotech, Inc., Akita, Japan) (28Okazaki M. Usui S. Ishigami M. Sakai N. Nakamura T. Matsuzawa Y. Yamashita S. Identification of unique lipoprotein subclasses for visceral obesity by component analysis of cholesterol profile in high-performance liquid chromatography.Arterioscler. Thromb. Vasc. Biol. 2005; 25: 578-584Crossref PubMed Scopus (196) Google Scholar). HDL-C values determined by the HDL-cholesterol E-test kit were confirmed by HPLC procedures (supplemental Table I). To determine HDL particle size, plasma (5 μl for WT mice; 10 μl for Apoa1−/− mice) prestained for lipids with Sudan Black B was electrophoresed on a nondenaturing PAGE gel with a 5-15% linear polyacrylamide gradient. Electrophoresis was carried out at 25 mA for 2 h (14Ge F. Yao J. Fu X. Guo Z. Yan J. Zhang B. Zhang H. Tomozawa H. Miyazaki J. Sawashita J. et al.Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2c).Lab. Invest. 2007; 87: 633-643Crossref PubMed Scopus (22) Google Scholar, 29Umezawa M. Tatematsu K. Korenaga T. Fu X. Matushita T. Okuyama H. Hosokawa M. Takeda T. Higuchi K. Dietary fat modulation of apoA-II metabolism and prevention of senile amyloidosis in the senescence- accelerated mouse.J. Lipid Res. 2003; 44: 762-769Abstract Full Text Full Text PDF PubMed Scopus (18) Google Scholar). The distribution of apoA-I, apoA-II, apoE, apoA-IV, and apoC- II protein among the HDL species was determined by Western blot analysis of 0.5, 2, 1, 1, and 2 μl plasma, respectively, separated by nondenaturing PAGE. To further determine the cholesterol profiles in plasma lipoproteins, pooled plasma from mice (n = 3) was analyzed with HPLC. Isolated HPLC fractions with different particle diameters (ranging from 7.6 nm to >80 nm) from 4 μl pooled plasma were separated by SDS-PAGE, and apoA-II protein was determined by Western blot analysis. Plasma (1 and 2 μl for apoE and apo-II, respectively) from C57BL/6J and Apoa1−/− mice was separated by electrophoresis at 15 mA for 6 h on Tris-Tricine/SDS-16.5% polyacrylamide gels (SDS-PAGE). After electrophoresis, proteins were transferred to a polyvinylidene difluoride (PVDF) membrane using a semidry Western blot apparatus at 150 mA for 1.5 h. The membrane was then probed with goat anti-apolipoprotein E polyclonal antibody diluted 1:2,000 (AB947, Chemicon International) or polyclonal rabbit anti-mouse apoA-II diluted 1:1,500 in 3% skim milk in PBS containing 0.1% Tween-20 (T-PBS) for 1 h at room temperature. Subsequently, membranes were incubated for 1 h with horseradish peroxidase (HRP)-conjugated anti-goat IgG solution (1:3,000) or anti-rabbit IgG solution (1:3,000). ApoE and ApoA-II were detected with the enhanced chemiluminescence (ECL) system and quantified using a densitometric image analyzer with NIH Image version 1.61 (Bethesda, MD). Pooled plasma from two-month-old wild-type (WT) mice was used as standard plasma to calculate the relative apoE concentration. Plasma with 25 mg/dl apoA-II concentration, determined by purified apoA-II protein (30Higuchi K. Yonezu T. Kogishi K. Matsumura A. Takeshita S. Higuchi K. Kohno A. Matsushita M. Hosokawa M. Takeda T. Purification and characterization of a senile amyloid-related antigenic substance (apoSASSAM) from mouse serum. apoSASSAM is an apoA-II apolipoprotein of mouse high density lipoproteins.J. Biol. Chem. 1986; 261: 12834-12840Abstract Full Text PDF PubMed Google Scholar), was used as standard plasma to calculate the concentration of apoA-II (supplemental Fig. I). Anti-apoA-II antiserum was produced in rabbits by injecting type C apoA-II protein purified from AApoAII amyloid fibrils deposited in the liver of a SAMP1 mouse (31Higuchi K. Matsumura A. Honma A. Takeshita S. Hashimoto K. Hosokawa M. Yasuhira K. Takeda T. Systemic senile amyloid in senescence-accelerated mice. A unique fibril protein demonstrated in tissues from various organs by the unlabeled immunoperoxidase method.Lab. Invest. 1983; 48: 231-240PubMed Google Scholar). This anti-apoA-II antiserum can react specifically with plasma type A, type B, and type C apoA-II on a Western blot. This anti-apoA-II antiserum can also react specifically with type A, type B, and type C AApoAII fibrils on a Western blot or immunohistochemistry (14Ge F. Yao J. Fu X. Guo Z. Yan J. Zhang B. Zhang H. Tomozawa H. Miyazaki J. Sawashita J. et al.Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2c).Lab. Invest. 2007; 87: 633-643Crossref PubMed Scopus (22) Google Scholar, 24Xing Y. Nakamura A. Korenaga T. Guo Z. Yao J. Fu X. Matsushita T. Kogishi K. Hosokawa M. Kametani F. et al.Induction of protein conformational change in mouse senile amyloidosis.J. Biol. Chem. 2002; 277: 33164-33169Abstract Full Text Full Text PDF PubMed Scopus (49) Google Scholar, 32Korenaga T. Fu X. Xing Y. Matsusita T. Kuramoto K. Syumiya S. Hasegawa K. Naiki H. Ueno M. Ishihara T. et al.Tissue distribution, biochemical properties, and transmission of mouse type A AApoAII amyloid fibrils.Am. J. Pathol. 2004; 164: 1597-1606Abstract Full Text Full Text PDF PubMed Scopus (33) Google Scholar). Total RNA was extracted from livers or hearts (including the atrium cordis and ventriculus cordis) of two- and six-month-old mice using TRIzol Reagent (Invitrogen), followed by treatment with DNA-Free (Applied Biosystems, Foster City, CA) to remove contaminating DNA. Then it was subjected to reverse transcription using an Omniscript RT kit (Applied Biosystems) with random primers (Applied Biosystems). The cycling parameters for reverse transcriptase-polymerase chain reaction (RT-PCR) amplification were initial denaturation for 1 min at 94°C, followed by 23 cycles of 30 s at 94°C, 30 s at 60°C, and 45 s at 72°C for GAPDH; 24 cycles for hepatic Apoa1; 21 cycles for hepatic Apoa2; and 32 cycles for cardiac Apoa2. Quantitative real-time RT-PCR analysis was carried out using an ABI PRISM 7500 Sequence Detection System (Applied Biosystems) with SYBR Green (Takara Bio, Tokyo, Japan), and values were normalized with respect to GAPDH. The following primers were used: Apoa1-F 5′-GTGGCTCTGGTCTTCCTGAC-3′, Apoa1-R 5′-ACGGTTGAACCCAGAGTGTC-3′ (218 bp); Apoa2-F 5′-GCCTGTTCACTCAGTACTTTCAG-3′ and Apoa2-R 5′-CAGACTAGTTCCTGCTGACC-3′ (155 bp); and GAPDH-F 5′-TGCACCACCAACTGCTTAG-3′ and GAPDH-R 5′-GGATGCAGGGATGATGTTC-3′ (177 bp). AApoAII(C) fibrils were isolated from the liver of a 12-month-old R1.P1-Apoa2c mouse, a congenic strain carrying the amyloidogenic Apoa2c allele from the SAMP1 strain in the genetic background of SAMR1 (33Higuchi K. Kitado H. Kitagawa K. Kogishi K. Naiki H. Takeda T. Development of congenic strains of mice carrying amyloidogenic apolipoprotein A-II (Apoa2c). Apoa2c reduces the plasma level and the size of high density lipoprotein.FEBS Lett. 1993; 317: 207-210Crossref PubMed Scopus (27) Google Scholar), which also had severe amyloid deposition induced by intravenous injection of AApoAII(C) fibrils. AApoAII(A) fibrils were isolated from the liver of a 12-month-old C57BL/6 mouse, which had severe amyloid deposition induced by intravenous injection of AApoAII(C) amyloid fibrils. Both amyloid fibril fractions were isolated by Pras's method with some modification (14Ge F. Yao J. Fu X. Guo Z. Yan J. Zhang B. Zhang H. Tomozawa H. Miyazaki J. Sawashita J. et al.Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (Apoa2c).Lab. Invest. 2007; 87: 633-643Crossref PubMed Scopus (22) Google Scholar). Isolated amyloid fibrils were suspended in distilled deionized water (DDW) at a concentration of 1.0 mg/ml and kept at −70°C. Of this mixture, 1 ml was placed in a 1.5 ml Eppendorf tube and sonicated on ice for 30 s with an ultrasonic homogenizer VP-5S (Tietech Co., Ltd., Tokyo, Japan) at maximum power. This procedure was repeated five times at 30 s intervals. Sonicated AApoAII samples were used immediately. Previously we have shown that AApoAII(A) amyloidosis could be induced by AApoAII(C) amyloid fibrils by cross-seeding, and confirmed that the depositions in C57BL/6 mice with Apoa2a were endogenous AApoAII(A) amyloid fibrils (32). Therefore, to induce AApoAII amyloidosis, 10 or 100 μg sonicated AApoAII(C) amyloid fibrils suspended in 100 μl DDW were injected into the tail vein of two-month-old female Apoa1−/− and WT mice. After two or four months, the treated mice were euthanized, and amyloid deposition was determined. We also induced amyloidosis by self-seeding with AApoAII(A) amyloid fibrils and compared the amyloid deposition. Control mice were injected with 100 μl DDW containing no amyloid fibrils. The mice were euthanized by cardiac puncture under diethyl ether anesthesia, and major tissues were fixed in 10% neutral buffered formalin, embedded in paraffin, and cut into 4 μm sections for Congo Red staining and immunohistochemistry. Deposition of amyloid fibrils in each mouse was identified by polarizing microscopy using Congo Red-stained sections, where green birefringence indicates the presence of amyloid. The intensity of amyloid deposition was determined semiquantitatively using the amyloid index (AI) as a parameter. The AI parameter represents the average degree of deposition, graded from 0 to 4, in the seven organs (heart, liver, spleen, stomach, intestine, tongue, and skin) examined in Congo Red-stained sections. Amyloid fibril proteins were identified by immunohistochemistry using the avidin-biotin horseradish peroxidase complex method. Specific antisera against mouse AApoAII and mouse AA were used (31Higuchi K. Matsumura A. Honma A. Takeshita S. Hashimoto K. Hosokawa M. Yasuhira K. Takeda T. Systemic senile amyloid in senescence-accelerated mice. A unique fibril protein demonstrated in tissues from various organs by the unlabeled immunoperoxidase method.Lab. Invest. 1983; 48: 231-240PubMed Google Scholar). Tissues were examined by two independent observers who were blinded to the experimental protocol. We used the StatView software package (Abacus Concepts, Berkley, CA) for data analysis. All data are presented as the mean ± SD. Because the AI is nonlinear, the AIs of different groups of mice were compared using the nonparametric Mann-Whitney U-test. One-way Anova and Student's t-test were used for all data except AI. To determine whether apoA-I deficiency influences the metabolism of apoA-II and apoE, the major protein constituents of HDL from Apoa1−/− mice (7Li H. Reddick R.L. Maeda N. Lack of apoA-I is not associated with increased susceptibility to atherosclerosis in mice.Arterioscler. Thromb. 1993; 13: 1814-1821Crossref PubMed Scopus (163) Google Scholar, 9Lee M. Calabresi L. Chiesa G. Franceschini G. Kovanen P.T. Mast cell chymase degrades apoE and apoA-II in apoA-I-knockout mouse plasma and reduces its ability to promote cellular cholesterol efflux.Arterioscler. Thromb. Vasc. Biol. 2002; 22: 1475-1481Crossref PubMed Scopus (48) Google Scholar), we determined the plasma levels of apoA-I, apoA-II, and apoE in two-, four-, and six-month-old WT and Apoa1−/− mice by Western blot analysis after separating plasma proteins by SDS-PAGE. In" @default.
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• W2094580301 title "ApoA-I deficiency in mice is associated with redistribution of apoA-II and aggravated AApoAII amyloidosis" @default.
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