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D Corella - One of the best experts on this subject based on the ideXlab platform.
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epigenomics and metabolomics reveal the mechanism of the APOA2 saturated fat intake interaction affecting obesity
The American Journal of Clinical Nutrition, 2018Co-Authors: Caren E Smith, Laurence D. Parnell, D Corella, Paul N Hopkins, Bertha Hidalgo, Stella Aslibekyan, Michael A Province, Devin Absher, Donna K Arnett, Katherine L TuckerAbstract:Background The putative functional variant −265T>C (rs5082) within the APOA2 promoter has shown consistent interactions with saturated fatty acid (SFA) intake to influence the risk of obesity.
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Apolipoprotein A2 Polymorphism Interacts with Intakes of Dairy Foods to Influence Body Weight in 2 U.S. Populations
Journal of Nutrition, 2013Co-Authors: Caren E Smith, D Corella, Stella Aslibekyan, Donna K Arnett, Katherine L Tucker, Sabrina E. Noel, Ingrid B. Borecki, Mary F. Feitosa, Laurence D. ParnellAbstract:The interaction between a functional apolipoprotein A2 gene (APOA2) variant and saturated fatty acids (SFAs) for the outcome of body mass index (BMI) is among the most widely replicated gene-nutrient interactions. Whether this interaction can be extrapolated to food-based sources of SFAs, specifically dairy foods, is unexplored. Cross-sectional analyses were performed in 2 U.S. population–based samples. We evaluated interactions between dairy foods and APOA2 −265T > C (rs5082) for BMI in the Boston Puerto Rican Health Study (n = 955) and tested for replication in the Genetics of Lipid Lowering Drugs and Diet Network (GOLDN) study (n = 1116). Dairy products were evaluated as total dairy, higher-fat dairy (>1%), and low-fat dairy (≤1%) in servings per day, dichotomized into high and low based on each population median and also as continuous variables. We identified a statistically significant interaction between the APOA2 −265T > C variant and higher-fat dairy food intake in the Boston Puerto Ricans (P-interaction = 0.028) and replicated this relation in the GOLDN study (P-interaction = 0.001). In both groups, individuals with the previously demonstrated SFA-sensitive genotype (CC) who consumed a greater amount of higher-fat dairy foods had greater BMI (P = 0.013 in Boston Puerto Ricans; P = 0.0007 in GOLDN women) compared with those consuming less of the higher-fat dairy foods. The results expand the understanding of the metabolic influence of dairy products, an important food group for which variable relations to body weight may be in part genetically based. Moreover, these findings suggest that other strongly demonstrated gene-nutrient relations might be investigated through appropriate food-based, translatable avenues and may be relevant to dietary management of obesity.
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Apolipoprotein A2 Polymorphism Interacts with Intakes of Dairy Foods to Influence Body Weight
2013Co-Authors: Caren E Smith, D Corella, Stella Aslibekyan, Donna K Arnett, Katherine L Tucker, Sabrina E. Noel, Ingrid B. Borecki, Mary F. Feitosa, Laurence D. ParnellAbstract:The interaction between a functional apolipoprotein A2 gene (APOA2) variant and saturated fatty acids (SFAs) for the outcome of body mass index (BMI) is among the most widely replicated gene-nutrient interactions. Whether this interaction can be extrapolated to food-based sources of SFAs, specifically dairy foods, is unexplored. Cross-sectional analyses were performed in 2 U.S. population‐based samples. We evaluated interactions between dairy foods and APOA2 2265T > C (rs5082) for BMI in the Boston Puerto Rican Health Study (n = 955) and tested for replication in the Genetics of Lipid Lowering Drugs and Diet Network (GOLDN) study (n = 1116). Dairy products were evaluated as total dairy, higher-fat dairy (>1%), and low-fat dairy (#1%) in servings per day, dichotomized into high and low based on each population median and also as continuous variables. We identified a statistically significant interaction between the APOA2 2265T > C variant and higher-fat dairy food intake in the Boston Puerto Ricans (P-interaction = 0.028) and replicated this relation in the GOLDN study (P-interaction = 0.001). In both groups, individuals with the previously demonstrated SFA-sensitive genotype (CC) who consumed a greater amount of higher-fat dairy foods had greater BMI (P = 0.013 in Boston Puerto Ricans; P = 0.0007 in GOLDN women) compared with those consuming less of the higher-fat dairy foods. The results expand the understanding of the metabolic influence of dairy products, an important food group for which variable relations to body weight may be in part genetically based. Moreover, these findings suggest that other strongly demonstrated gene-nutrient relations might be investigated through appropriate food-based, translatable avenues and may be relevant to dietary management of obesity. J. Nutr. 143: 1865‐1871, 2013.
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Association between the APOA2 promoter polymorphism and body weight in Mediterranean and Asian populations: replication of a gene–saturated fat interaction
International Journal of Obesity, 2011Co-Authors: D Corella, J V Sorlí, S K Chew, O Coltell, M Sotos-prieto, A García-rios, R Estruch, J M OrdovasAbstract:Objective: The APOA2 gene has been associated with obesity and insulin resistance (IR) in animal and human studies with controversial results. We have reported an APOA2 –saturated fat interaction determining body mass index (BMI) and obesity in American populations. This work aims to extend our findings to European and Asian populations. Methods: Cross-sectional study in 4602 subjects from two independent populations: a high-cardiovascular risk Mediterranean population ( n =907 men and women; aged 67±6 years) and a multiethnic Asian population ( n =2506 Chinese, n =605 Malays and n =494 Asian Indians; aged 39±12 years) participating in a Singapore National Health Survey. Anthropometric, clinical, biochemical, lifestyle and dietary variables were determined. Homeostasis model assessment of insulin resistance was used in Asians. We analyzed gene–diet interactions between the APOA2 −265T>C polymorphism and saturated fat intake (C polymorphism on body-weight-related measures was modulated by saturated fat in Mediterranean and Asian populations.
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association between the APOA2 promoter polymorphism and body weight in mediterranean and asian populations replication of a gene saturated fat interaction
International Journal of Obesity, 2011Co-Authors: D Corella, J V Sorlí, S K Chew, O Coltell, Mercedes SotosprietoAbstract:Association between the APOA2 promoter polymorphism and body weight in Mediterranean and Asian populations: replication of a gene–saturated fat interaction
Keiichi Higuchi - One of the best experts on this subject based on the ideXlab platform.
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Apolipoprotein A-II induces acute-phase response associated AA amyloidosis in mice through conformational changes of plasma lipoprotein structure
Scientific Reports, 2018Co-Authors: Mu Yang, Lin Li, Masayuki Mori, Jinko Sawashita, Xin Ding, Zhe Xu, Hiroki Miyahara, Keiichi HiguchiAbstract:During acute-phase response (APR), there is a dramatic increase in serum amyloid A (SAA) in plasma high density lipoproteins (HDL). Elevated SAA leads to reactive AA amyloidosis in animals and humans. Herein, we employed apolipoprotein A-II (ApoA-II) deficient (APOA2 −/− ) and transgenic (APOA2Tg) mice to investigate the potential roles of ApoA-II in lipoprotein particle formation and progression of AA amyloidosis during APR. AA amyloid deposition was suppressed in APOA2 −/− mice compared with wild type (WT) mice. During APR, APOA2 −/− mice exhibited significant suppression of serum SAA levels and hepatic Saa1 and Saa2 mRNA levels. Pathological investigation showed APOA2 −/− mice had less tissue damage and less inflammatory cell infiltration during APR. Total lipoproteins were markedly decreased in APOA2 −/− mice, while the ratio of HDL to low density lipoprotein (LDL) was also decreased. Both WT and APOA2 −/− mice showed increases in LDL and very large HDL during APR. SAA was distributed more widely in lipoprotein particles ranging from chylomicrons to very small HDL in APOA2 −/− mice. Our observations uncovered the critical roles of ApoA-II in inflammation, serum lipoprotein stability and AA amyloidosis morbidity, and prompt consideration of therapies for AA and other amyloidoses, whose precursor proteins are associated with circulating HDL particles.
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Amyloidosis-inducing activity of blood cells in mouse AApoAII amyloidosis.
Experimental Animals, 2017Co-Authors: Xin Ding, Lin Li, Masayuki Mori, Mu Yang, Zhe Xu, Hiroki Miyahara, Kiyoshi Matsumoto, Keiichi HiguchiAbstract:Mouse senile amyloidosis is a disorder in which apolipoprotein A-II (APOA2) deposits as amyloid fibrils (AApoAII) in many organs. We previously reported that AApoAII amyloidosis can be transmitted by feces, milk, saliva and muscle originating from mice with amyloid deposition. In this study, the ability of blood components to transmit amyloidosis was evaluated in our model system. Blood samples were collected from SAMR1.SAMP1-APOA2c amyloid-laden or amyloidosis-negative mice. The samples were fractionated into plasma, white blood cell (WBC) and red blood cell (RBC) fractions. Portions of each were further separated into soluble and insoluble fractions. These fractions were then injected into recipient mice to determine amyloidosis-induction activities (AIA). The WBC and RBC fractions from amyloid-laden mice but not from amyloidosis-negative mice induced AApoAII amyloid deposition in the recipients. The AIA of WBC fraction could be attributed to AApoAII amyloid fibrils because amyloid fibril-like materials and APOA2 antiserum-reactive proteins were observed in the insoluble fraction of the blood cells. Unexpectedly, the plasma of AApoAII amyloidosis-negative as well as amyloid-laden mice showed AIA, suggesting the presence of substances in mouse plasma other than AApoAII fibrils that could induce amyloid deposition. These results indicated that AApoAII amyloidosis could be transmitted across tissues and between individuals through blood cells.
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Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (APOA2^c)
Laboratory Investigation, 2007Co-Authors: Fengxia Ge, Xiaoying Fu, Masayuki Mori, Beiru Zhang, Huanyu Zhang, Hiroshi Tomozawa, Junichi Miyazaki, Jinko Sawashita, Keiichi HiguchiAbstract:In mice, apolipoprotein A-II (apoA-II) self-associates to form amyloid fibrils (AApoAII) in an age-associated manner. We postulated that the two most important factors in apoA-II amyloidosis are the APOA2 ^ c allele, which codes for the amyloidogenic protein APOA2C (Gln5, Ala38) and transmission of amyloid fibrils. To characterize further the contribution of the APOA2 ^ c allele to amyloidogenesis and improve detection of amyloidogenic materials, we established transgenic mice that overexpress APOA2C protein under the cytomegalovirus (CMV) immediate early gene (CMV-IE) enhancer/chicken β promoter. Compared to transgene negative (Tg^−/−) mice that express apoA-II protein mainly in the liver, mice homozygous (Tg^+/+) and heterozygous (Tg^+/−) for the transgene express a high level of apoA-II protein in many tissues. They also have higher plasma concentrations of apoA-II, higher ratios of ApoA-II/apolipoprotein A-I (ApoA-I) and higher concentrations of high-density lipoprotein (HDL) cholesterol. Following injection of AApoAII fibrils into Tg^+/+ mice, amyloid deposition was observed in the testis, liver, kidney, heart, lungs, spleen, tongue, stomach and intestine but not in the brain. In Tg^+/+ mice, but not in Tg^−/− mice, amyloid deposition was induced by injection of less than 10^−8 μ g AApoAII fibrils. Furthermore, deposition in Tg^+/+ mice occurred more rapidly and to a greater extent than in Tg^−/− mice. These studies indicate that increased levels of APOA2C protein lead to earlier and greater amyloid deposition and enhanced sensitivity to the transmission of amyloid fibrils in transgenic mice. This transgenic mouse model should prove valuable for studies of amyloidosis.
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Relationship between immune activity, senile amyloidosis and life span of hybrids of SAMP1 and B10.BR mice
International Congress Series, 2004Co-Authors: Eiko Toichi, Masanori Hosokawa, Keiichi Higuchi, Takatoshi Matsushita, Tomohide Hosokawa, Masamichi HosonoAbstract:Abstract SAMP1 mice show impaired immune activity as young adults and suffer from senile amyloidosis due to APOA2 gene expression at around a year of age, and this factor may be responsible for their short life. To examine the relationship between low immune activity, senile amyloidosis and a shortened life span, we investigated hybrid mice from original parental strains of SAMP1 ( APOA2c ) and B10.BR ( APOA2a ), an ordinary strain of mice. Our results show that more than 90% of APOA2c -homozygous siblings had shortened life spans with either low or high immune activity in equal proportions. Thus, the development of senile amyloidosis may directly cause the shorter life span, while low immune activity does not seem to correlate with a shorter life span. Siblings with both the APOA2 gene of a/c heterozygous type and high immune activity showed a wide distribution in length of life. Among those who died early there was a heavy deposit of inflammatory amyloyd A-protein (AA)- but not any deposits of AApoAII senile amyloid. It is interesting that 2 out of 24 mice homozygous for APOA2c displayed relatively long life spans, even though they showed heavy deposition of AApoAII and that these two were found to have low autoimmune antibodies. This means that age-related pathogenesis and life span could be delayed and controlled by some factors other than senile amyloidogenesis.
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Polymorphisms of mouse apolipoprotein A-11: seven alleles found among 41 inbred strains of mice
Amyloid, 2003Co-Authors: Kaori Kitagawa, Jing Wang, Takatoshi Mastushita, Kumiko Kogishi, Masanori Hosokawa, Xiaoying Fu, Masayuki Mori, Keiichi HiguchiAbstract:In mice, apolipoprotein A-II (apoA-II) associates to form amyloid fibrils in an age-associated manner. We determined the complete nucleotide sequences of the apoA-II gene (APOA2) cDNA in 41 inbred strains of mice including Mus musculus domesticus (laboratory mouse), Mus musculus castaneus, Mus musculus molossinus, Mus musculus musculus and Mus spretus. Among these strains we identified 7 alleles (APOA2a1, APOA2a2, APOA2b, APOA2c, APOA2d, APOA2e and APOA2f). Polymorphisms of nucleotides at 15 positions were detected and amino acid substitutions were found at 8 positions. APOA2a1 was found in all mouse subspecies, but APOA2b and APOA2c were found only in Mus musculus domesticus. Two strains of Mus spretus have the unique alleles APOA2eand APOA2f which resemble APOA2c. We confirmed that VICS in which we found severe amyloidosis here and other amyloidoneic strains in published reports have APOA2c allele.We determined the plasma concentrations of total and HDL cholesterol in the strains of Mus musculus domesti...
Fengxia Ge - One of the best experts on this subject based on the ideXlab platform.
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Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (APOA2^c)
Laboratory Investigation, 2007Co-Authors: Fengxia Ge, Xiaoying Fu, Masayuki Mori, Beiru Zhang, Huanyu Zhang, Hiroshi Tomozawa, Junichi Miyazaki, Jinko Sawashita, Keiichi HiguchiAbstract:In mice, apolipoprotein A-II (apoA-II) self-associates to form amyloid fibrils (AApoAII) in an age-associated manner. We postulated that the two most important factors in apoA-II amyloidosis are the APOA2 ^ c allele, which codes for the amyloidogenic protein APOA2C (Gln5, Ala38) and transmission of amyloid fibrils. To characterize further the contribution of the APOA2 ^ c allele to amyloidogenesis and improve detection of amyloidogenic materials, we established transgenic mice that overexpress APOA2C protein under the cytomegalovirus (CMV) immediate early gene (CMV-IE) enhancer/chicken β promoter. Compared to transgene negative (Tg^−/−) mice that express apoA-II protein mainly in the liver, mice homozygous (Tg^+/+) and heterozygous (Tg^+/−) for the transgene express a high level of apoA-II protein in many tissues. They also have higher plasma concentrations of apoA-II, higher ratios of ApoA-II/apolipoprotein A-I (ApoA-I) and higher concentrations of high-density lipoprotein (HDL) cholesterol. Following injection of AApoAII fibrils into Tg^+/+ mice, amyloid deposition was observed in the testis, liver, kidney, heart, lungs, spleen, tongue, stomach and intestine but not in the brain. In Tg^+/+ mice, but not in Tg^−/− mice, amyloid deposition was induced by injection of less than 10^−8 μ g AApoAII fibrils. Furthermore, deposition in Tg^+/+ mice occurred more rapidly and to a greater extent than in Tg^−/− mice. These studies indicate that increased levels of APOA2C protein lead to earlier and greater amyloid deposition and enhanced sensitivity to the transmission of amyloid fibrils in transgenic mice. This transgenic mouse model should prove valuable for studies of amyloidosis.
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Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (APOA2c).
Laboratory Investigation, 2007Co-Authors: Fengxia Ge, Xiaoying Fu, Beiru Zhang, Huanyu Zhang, Hiroshi Tomozawa, Junichi Miyazaki, Jinko SawashitaAbstract:Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II ( APOA2 c )
Jinko Sawashita - One of the best experts on this subject based on the ideXlab platform.
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Apolipoprotein A-II induces acute-phase response associated AA amyloidosis in mice through conformational changes of plasma lipoprotein structure
Scientific Reports, 2018Co-Authors: Mu Yang, Lin Li, Masayuki Mori, Jinko Sawashita, Xin Ding, Zhe Xu, Hiroki Miyahara, Keiichi HiguchiAbstract:During acute-phase response (APR), there is a dramatic increase in serum amyloid A (SAA) in plasma high density lipoproteins (HDL). Elevated SAA leads to reactive AA amyloidosis in animals and humans. Herein, we employed apolipoprotein A-II (ApoA-II) deficient (APOA2 −/− ) and transgenic (APOA2Tg) mice to investigate the potential roles of ApoA-II in lipoprotein particle formation and progression of AA amyloidosis during APR. AA amyloid deposition was suppressed in APOA2 −/− mice compared with wild type (WT) mice. During APR, APOA2 −/− mice exhibited significant suppression of serum SAA levels and hepatic Saa1 and Saa2 mRNA levels. Pathological investigation showed APOA2 −/− mice had less tissue damage and less inflammatory cell infiltration during APR. Total lipoproteins were markedly decreased in APOA2 −/− mice, while the ratio of HDL to low density lipoprotein (LDL) was also decreased. Both WT and APOA2 −/− mice showed increases in LDL and very large HDL during APR. SAA was distributed more widely in lipoprotein particles ranging from chylomicrons to very small HDL in APOA2 −/− mice. Our observations uncovered the critical roles of ApoA-II in inflammation, serum lipoprotein stability and AA amyloidosis morbidity, and prompt consideration of therapies for AA and other amyloidoses, whose precursor proteins are associated with circulating HDL particles.
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Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (APOA2^c)
Laboratory Investigation, 2007Co-Authors: Fengxia Ge, Xiaoying Fu, Masayuki Mori, Beiru Zhang, Huanyu Zhang, Hiroshi Tomozawa, Junichi Miyazaki, Jinko Sawashita, Keiichi HiguchiAbstract:In mice, apolipoprotein A-II (apoA-II) self-associates to form amyloid fibrils (AApoAII) in an age-associated manner. We postulated that the two most important factors in apoA-II amyloidosis are the APOA2 ^ c allele, which codes for the amyloidogenic protein APOA2C (Gln5, Ala38) and transmission of amyloid fibrils. To characterize further the contribution of the APOA2 ^ c allele to amyloidogenesis and improve detection of amyloidogenic materials, we established transgenic mice that overexpress APOA2C protein under the cytomegalovirus (CMV) immediate early gene (CMV-IE) enhancer/chicken β promoter. Compared to transgene negative (Tg^−/−) mice that express apoA-II protein mainly in the liver, mice homozygous (Tg^+/+) and heterozygous (Tg^+/−) for the transgene express a high level of apoA-II protein in many tissues. They also have higher plasma concentrations of apoA-II, higher ratios of ApoA-II/apolipoprotein A-I (ApoA-I) and higher concentrations of high-density lipoprotein (HDL) cholesterol. Following injection of AApoAII fibrils into Tg^+/+ mice, amyloid deposition was observed in the testis, liver, kidney, heart, lungs, spleen, tongue, stomach and intestine but not in the brain. In Tg^+/+ mice, but not in Tg^−/− mice, amyloid deposition was induced by injection of less than 10^−8 μ g AApoAII fibrils. Furthermore, deposition in Tg^+/+ mice occurred more rapidly and to a greater extent than in Tg^−/− mice. These studies indicate that increased levels of APOA2C protein lead to earlier and greater amyloid deposition and enhanced sensitivity to the transmission of amyloid fibrils in transgenic mice. This transgenic mouse model should prove valuable for studies of amyloidosis.
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Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II (APOA2c).
Laboratory Investigation, 2007Co-Authors: Fengxia Ge, Xiaoying Fu, Beiru Zhang, Huanyu Zhang, Hiroshi Tomozawa, Junichi Miyazaki, Jinko SawashitaAbstract:Amyloidosis in transgenic mice expressing murine amyloidogenic apolipoprotein A-II ( APOA2 c )
Mercedes Sotosprieto - One of the best experts on this subject based on the ideXlab platform.
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association between the APOA2 promoter polymorphism and body weight in mediterranean and asian populations replication of a gene saturated fat interaction
International Journal of Obesity, 2011Co-Authors: D Corella, J V Sorlí, S K Chew, O Coltell, Mercedes SotosprietoAbstract:Association between the APOA2 promoter polymorphism and body weight in Mediterranean and Asian populations: replication of a gene–saturated fat interaction
