From infancy to aging: Biological and behavioral modifiers of Fetuin-A

Robinson, Katie N.; Terán-García, Margarita

doi:10.1016/j.biochi.2015.12.016

Cited by 33 publications

(32 citation statements)

References 101 publications

(170 reference statements)

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“…Following collagen, AHSG is one of the most abundant proteins in bone and its ability to bind calcium and other minerals supports the notion that it is essential for osteogenesis [74,75]. Current studies suggest that circulating AHSG is highest during infancy, declines in childhood and varies in adults owing to genetic factors, obesity and diet [73]. AHSG might also be impacted by the natural ageing process [76].…”

Section: Discussionmentioning

confidence: 98%

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Proteomic profiling of archaeological human bone

et al. 2017

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Ancient protein analysis provides clues to human life and diseases from ancient times. Here, we performed shotgun proteomics of human archeological bones for the first time, using rib bones from the Hitotsubashi site (AD 1657–1683) in Tokyo, called Edo in ancient times. The output data obtained were analysed using Gene Ontology and label-free quantification. We detected leucocyte-derived proteins, possibly originating from the bone marrow of the rib. Particularly prevalent and relatively high expression of eosinophil peroxidase suggests the influence of infectious diseases. This scenario is plausible, considering the overcrowding and unhygienic living conditions of the Edo city described in the historical literature. We also observed age-dependent differences in proteome profiles, particularly for proteins involved in developmental processes. Among them, alpha-2-HS-glycoprotein demonstrated a strong negative correlation with age. These results suggest that analysis of ancient proteins could provide a useful indicator of stress, disease, starvation, obesity and other kinds of physiological and pathological information.

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Section: Discussionmentioning

confidence: 98%

“…Owing to high concentrations of AHSG in fetal serum, multiple functions related to development have been suggested [72,73]. Following collagen, AHSG is one of the most abundant proteins in bone and its ability to bind calcium and other minerals supports the notion that it is essential for osteogenesis [74,75].…”

Section: Discussionmentioning

confidence: 99%

Proteomic profiling of archaeological human bone

et al. 2017

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“…These include, for example, a lack of reference values, inconsistent values from various commercial enzyme-linked immunosorbent assays (ELISA), and the unknown effect of post-translational modifications (PTMs) on hFet clinical measurements. 13 One source of confusion may also originate from some in vitro studies, where recombinant human fetuin was used. 14 , 15 Serum hFet is predominantly synthesized in the liver, where its N-glycosylation pattern originates.…”

Section: Introductionmentioning

confidence: 99%

Similar Albeit Not the Same: In-Depth Analysis of Proteoforms of Human Serum, Bovine Serum, and Recombinant Human Fetuin

2018

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Fetuin, also known as alpha-2-Heremans Schmid glycoprotein (AHSG), belongs to some of the most abundant glycoproteins secreted into the bloodstream. In blood, fetuins exhibit functions as carriers of metals and small molecules. Bovine fetuin, which harbors 3 N-glycosylation sites and a suggested half dozen O-glycosylation sites, has been used often as a model glycoprotein to test novel analytical workflows in glycoproteomics. Here we characterize and compare fetuin in depth, using protein from three different biological sources: human serum, bovine serum, and recombinant human fetuin expressed in HEK-293 cells, with the aim to elucidate similarities and differences between these proteins and the post-translational modifications they harbor. Combining data from high-resolution native mass spectrometry and glycopeptide centric LC-MS analysis, we qualitatively and quantitatively gather information on fetuin protein maturation, N-glycosylation, O-glycosylation, and phosphorylation. We provide direct experimental evidence that both the human serum and part of the recombinant proteins are processed into two chains (A and B) connected by a single interchain disulfide bridge, whereas bovine fetuin remains a single-chain protein. Although two N-glycosylation sites, one O-glycosylation site, and a phosphorylation site are conserved from bovine to human, the stoichiometry of the modifications and the specific glycoforms they harbor are quite distinct. Comparing serum and recombinant human fetuin, we observe that the serum protein harbors a much simpler proteoform profile, indicating that the recombinant protein is not ideally engineered to mimic human serum fetuin. Comparing the proteoform profile and post-translational modifications of human and bovine serum fetuin, we observe that, although the gene structures of these two proteins are alike, they represent quite distinct proteins when their glycoproteoform profile is also taken into consideration.

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“…It is known to have various biological functions, including the prevention of tissue calcification and maintenance of calcium-phosphorus balance [1011]. Data obtained in recent experimental studies showed that elevated levels of fetuin-A lead to IR by disturbing insulin receptor signalling [11].…”

Section: Introductionmentioning

confidence: 99%

Associations of serum fetuin-A and oxidative stress parameters with polycystic ovary syndrome

Sak

Uyanıkoğlu

Incebiyik

et al. 2018

Clin Exp Reprod Med

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ObjectiveThe aim of this study was to compare serum fetuin-A levels and oxidative stress markers, as indicators of insulin resistance, in women with polycystic ovary syndrome (PCOS) and in healthy controls.MethodsThis prospective case-control study included 46 patients with PCOS and 48 age- and body mass index–matched control women. Levels of serum hormones, fetuin-A, and oxidative stress markers were measured in blood samples taken during the early follicular period from each participant.ResultsFollicle-stimulating hormone (FSH), luteinising hormone (LH), total testosterone levels, and the LH/FSH ratio were found to be significantly higher in women with PCOS than in controls. Serum total antioxidant status, total oxidant status, and oxidative stress index parameters all indicated significantly higher levels of oxidative stress in PCOS patients than in controls. Serum fetuin-A levels, which were analyzed as an indicator of insulin resistance, were higher in the PCOS group than in the control group (210.26±65.06 µg/mL and 182.68±51.20 µg/mL, respectively; p=0.024).ConclusionThe data obtained from the present study suggest that higher levels of both serum fetuin-A and oxidative stress markers might be related with PCOS.

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From infancy to aging: Biological and behavioral modifiers of Fetuin-A

Cited by 33 publications

References 101 publications

Proteomic profiling of archaeological human bone

Proteomic profiling of archaeological human bone

Similar Albeit Not the Same: In-Depth Analysis of Proteoforms of Human Serum, Bovine Serum, and Recombinant Human Fetuin

Associations of serum fetuin-A and oxidative stress parameters with polycystic ovary syndrome

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