Serum amyloid A1 levels and amyloid deposition following a high-fat diet challenge in transgenic mice overexpressing hepatic serum amyloid A1

Jang, Woo Young; Jeong, Jin Woo; Kim, Seonggon; Kang, Min‐Cheol; Sung, Yong Hun; Choi, Minjee; Park, Si Jun; Kim, Myoung Ok; Kim, Sung Hyun; Ryoo, Zae Young

doi:10.1139/apnm-2015-0369

Cited by 17 publications

(16 citation statements)

References 40 publications

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“…Therefore, increased plasma levels of TG, which contribute to oxidative stress, are expected to shift the dynamic equilibrium from the HDL-bound to free apolipoproteins and thereby generate the protein precursor of amyloid. We speculate that this effect may be one of the contributing factors to the observed link between the severity of AA amyloidosis and elevated TG in conditions such as obesity, metabolic syndrome and diabetes [67,68]. …”

Section: Discussionmentioning

confidence: 99%

Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases

Jayaraman

Sánchez-Quesada²,

Gursky

2017

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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Lipids in the body are transported via lipoproteins that are nanoparticles comprised of lipids and amphipathic proteins termed apolipoproteins. This family of lipid surface-binding proteins is over-represented in human amyloid diseases. In particular, all major proteins of high-density lipoproteins (HDL), including apoA-I, apoA-II and serum amyloid A, can cause systemic amyloidoses in humans upon protein mutations, post-translational modifications or overproduction. Here, we begin to explore how the HDL lipid composition influences amyloid deposition by apoA-I and related proteins. First, we summarize the evidence that, in contrast to lipoproteins that are stabilized by kinetic barriers, free apolipoproteins are labile to misfolding and proteolysis. Next, we report original biochemical and biophysical studies showing that increase in triglyceride content in the core of plasma or reconstituted HDL destabilizes the lipoprotein assembly, making it more labile to various perturbations (oxidation, thermal and chemical denaturation and enzymatic hydrolysis), and promotes apoA-I release in a lipid-poor/free aggregation-prone form. Together, the results suggest that decreasing plasma levels of triglycerides will shift the dynamic equilibrium from the lipid-poor/free (labile) to the HDL-bound (protected) apolipoprotein state, thereby decreasing the generation of the protein precursor of amyloid. This prompts us to propose that triglyceride-lowering therapies may provide a promising strategy to alleviate amyloid diseases caused by the deposition of HDL proteins.

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Section: Discussionmentioning

confidence: 99%

Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases

Jayaraman

Sánchez-Quesada²,

Gursky

2017

Biochimica et Biophysica Acta (BBA) - Molecular Basis of Diseas

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“…SAA1, an inflammatory protein mainly produced by hepatocytes, is upregulated by factors that enhance inflammatory cytokines (30). In blood circulation, it is closely related to high-density lipoprotein (HDL) and is of great importance in liver metabolism, responses to infection, and renal cell carcinoma (31)(32)(33). HGFAC is a serine protease and key determinant in tissue injury and the progression of renal cell carcinoma (34,35).…”

Section: Discussionmentioning

confidence: 99%

iTRAQ-based comparative proteomics analysis reveals specific urinary biomarkers for various kidney diseases

Jin

Gong

Zhao

et al. 2019

Preprint

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Background Urinary proteomics has been extensively applied to investigate renal diseases including acute kidney injury (AKI), chronic kidney disease (CKD), IgA nephropathy (IgAN) and diabetic CKD. However, differential urinary proteome studies have not been reported for multiple diseases. The present study was aimed to explore early clinical diagnosis biomarkers for patients with AKI, AKI+CKD, diabetic CKD, non-diabetic CKD with IgAN and non-diabetic CKD without IgAN. Methods Differentially expressed proteins (DEPs) were screened by iTRAQ labeling and 2-D LC-MS/MS. Bioinformatics analysis was performed by subsequent GO enrichment and KEGG pathway analysis. DEPs were authenticated by ELISA assay. Results 156, 156, 286, 187 and 184 differentially abundant proteins were identified in patients with AKI, AKI+CKD, diabetic CKD, and non-diabetic CKD with or without IgAN. Comparative analysis indicated that 34, 35 and 17 unique DEPs were found in AKI, AKI+CKD and CKD samples, respectively. 91 and 14 specific DEPs were screened out in diabetic CKD and non-diabetic CKD. In comparison with Non-diabetic CKD with IgAN (38 DEPs), 47 unique urinary proteins were found in Non-diabetic CKD without IgAN. Among these DEPs, urinary SAA1 and HGFAC were only unregulated in AKI and Non-diabetic CKD without IgAN implying that they might be employed as the potential indicators of the two diseases. C5, APOC1 and Reg3A upregulation was not exclusively expressed in each disease which suggested that they could not be used for biomarker to distinguish one disease from the other. Conclusion Collectively, this research contributes to the urinary biomarker discovery from multiple renal diseases.

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“…26 Western blotting was performed using primary antibodies against mouse Lin28a, GFP, β-actin, cleaved Caspase-9, cleaved Caspase-3, phosphorylated-PI3K, PI3K, phosphorylated-Akt, and Akt. 26 Western blotting was performed using primary antibodies against mouse Lin28a, GFP, β-actin, cleaved Caspase-9, cleaved Caspase-3, phosphorylated-PI3K, PI3K, phosphorylated-Akt, and Akt.…”

Section: Western Blottingmentioning

confidence: 99%

“…Total protein was extracted from cells and tissues using the Pro-Prep lysis buffer (iNtRON Biotechnology, Seoul, Korea) as described previously. 26 Western blotting was performed using primary antibodies against mouse Lin28a, GFP, β-actin, cleaved Caspase-9, cleaved Caspase-3, phosphorylated-PI3K, PI3K, phosphorylated-Akt, and Akt.…”

Section: Western Blottingmentioning

confidence: 99%

Lin28a expression protects against streptozotocin‐induced β‐cell destruction and prevents diabetes in mice

Sung

Jeong

Kang

et al. 2019

Cell Biochemistry & Function

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Lin28, which is highly expressed during embryogenesis, has been shown to play an important role in cell growth and embryonic development. Meanwhile, Lin28 represses let-7 miRNA biogenesis and block pre-let-7 processing in the cytoplasm.The let-7 family of miRNAs is known to repress oncogenesis and cell cycle progression by targeting oncogenic genes and signalling pathways. Consequently, Lin28 acts as an oncogene by upregulating let-7 targets through the repression of let-7 biogenesis. A recent genome-wide association study (GWAS) showed that many genes related to Type 2 diabetes (T2D) are also oncogenes or cell cycle regulators. The role of Lin28 in mouse growth and glucose metabolism in metabolic-related tissues has also been studied. In these studies, whole-body Lin28 overexpression was found to promote glucose utilization and prevent weight gain by inhibiting let-7 biogenesis.Furthermore, Lin28 has been found to directly stimulate skeletal myogenesis and cell growth. Therefore, we determined whether similar effects mediated by Lin28a, which is essential for cell growth and proliferation, may also apply to pancreatic ß-cells. We found that overexpression of Lin28a protects pancreatic β-cells from streptozotocin (STZ)-induced β-cell destruction in vitro and in vivo. Furthermore, Lin28aoverexpressing transgenic (Tg) mice had higher insulin secretion in the presence of glucose than in control mice. Our findings suggest that the Lin28/let-7 axis is an important regulator of pancreatic β-cell functions and that precise modulation of this axis may be helpful in treating metabolic diseases such as diabetes.Significance of the study: We demonstrate that Lin28a prevents pancreatic β-cell death against streptozotocin (STZ)-induced β-cell destruction in vitro and in vivo. Furthermore, Lin28a promotes cell survival and proliferation by activating the PI3K-Akt signalling pathway, which may be dependent on let-7 regulation. Taken together, our results imply that the Lin28a/let-7 axis is an important regulator of pancreatic β-cell functions and that precise modulation of this axis may be helpful in treating metabolic diseases such as diabetes.

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Serum amyloid A1 levels and amyloid deposition following a high-fat diet challenge in transgenic mice overexpressing hepatic serum amyloid A1

Cited by 17 publications

References 40 publications

Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases

Triglyceride increase in the core of high-density lipoproteins augments apolipoprotein dissociation from the surface: Potential implications for treatment of apolipoprotein deposition diseases

iTRAQ-based comparative proteomics analysis reveals specific urinary biomarkers for various kidney diseases

Lin28a expression protects against streptozotocin‐induced β‐cell destruction and prevents diabetes in mice

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