Increased serotransferrin and ceruloplasmin turnover in diet-controlled patients with type 2 diabetes

Golizeh, Makan; Lee, Kwang Won; Ilchenko, Serguei; Ösme, Abdullah; Bena, James; Sadygov, Rovshan G.; Kashyap, Sangeeta R.; Kasumov, Takhar

doi:10.1016/j.freeradbiomed.2017.10.373

Cited by 48 publications

(44 citation statements)

References 55 publications

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“…These changes were associated with lower levels of adiponectin, an adipose-tissue-derived peptide that was negatively related to CETP activity. The study extends upon our prior research [28,33] and demonstrates that mild hyperglycemia alters HDL dynamics in the early stages of diabetes.…”

Section: Discussionsupporting

confidence: 78%

“…Non-enzymatic modification (glycation) has been shown to reduce protein stability [53,61] via protein cross-linking and changes in peptide charge, HDL protein conformation, is altered [62]. Recently, we demonstrated that increased degradations of two HDL proteins, ApoA-I and transferrin in normolipidemic diet-controlled subjects with T2D are related to their post-translational glycation [28,33]. Additionally, small lipid-poor HDL particles may be prone to cleavage and degradation as a result of glycation [61,63].…”

Section: Discussionmentioning

confidence: 99%

“…Recently, we demonstrated that despite no changes in ApoA-I, ceruloplasmin and transferrin levels, the FCR of these proteins were significantly altered in diet-controlled T2D patients [28,33], indicating that the kinetic measurements were more sensitive than static snapshots of proteins levels. Consistent with these results, we found that the kinetics of several other HDL proteins were also perturbed in the subjects with T2D as compared to the controls (Table 3).…”

Section: Hdl Proteome Composition and Dynamicsmentioning

confidence: 98%

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Temporal Dynamics of High-Density Lipoprotein Proteome in Diet-Controlled Subjects with Type 2 Diabetes

et al. 2020

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We examined the effect of mild hyperglycemia on high-density lipoprotein (HDL) metabolism and kinetics in diet-controlled subjects with type 2 diabetes (T2D). 2H2O-labeling coupled with mass spectrometry was applied to quantify HDL cholesterol turnover and HDL proteome dynamics in subjects with T2D (n = 9) and age- and BMI-matched healthy controls (n = 8). The activities of lecithin–cholesterol acyltransferase (LCAT), cholesterol ester transfer protein (CETP), and the proinflammatory index of HDL were quantified. Plasma adiponectin levels were reduced in subjects with T2D, which was directly associated with suppressed ABCA1-dependent cholesterol efflux capacity of HDL. The fractional catabolic rates of HDL cholesterol, apolipoprotein A-II (ApoA-II), ApoJ, ApoA-IV, transthyretin, complement C3, and vitamin D-binding protein (all p < 0.05) were increased in subjects with T2D. Despite increased HDL flux of acute-phase HDL proteins, there was no change in the proinflammatory index of HDL. Although LCAT and CETP activities were not affected in subjects with T2D, LCAT was inversely associated with blood glucose and CETP was inversely associated with plasma adiponectin. The degradation rates of ApoA-II and ApoA-IV were correlated with hemoglobin A1c. In conclusion, there were in vivo impairments in HDL proteome dynamics and HDL metabolism in diet-controlled patients with T2D.

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Section: Discussionsupporting

confidence: 78%

Section: Discussionmentioning

confidence: 99%

Section: Hdl Proteome Composition and Dynamicsmentioning

confidence: 98%

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Temporal Dynamics of High-Density Lipoprotein Proteome in Diet-Controlled Subjects with Type 2 Diabetes

et al. 2020

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“…27 The gel was stained with Coomassie blue and the five most abundant bands including one at the molecular weight of 130 kD (expected to be for TRAPPC9, MW 128 233.2 Da) Total protein (100 µg) was combined with 10 µg of TRAPPC9 antibody with protein A/G magnetic beads.…”

Section: Mass Spectrometrymentioning

confidence: 99%

A novel regulatory role of TRAPPC9 in L‐plastin‐mediated osteoclast actin ring formation

Hussein

Mbimba

Al-Adlaan

et al. 2019

J of Cellular Biochemistry

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Trafficking protein particle complex 9 (TRAPPC9) is a major subunit of the TRAPPII complex. TRAPPC9 has been reported to bind nuclear factor κB kinase subunit β (IKKβ) and NF‐kB‐inducing kinase (NIK) where it plays a role in the canonical and noncanonical of nuclear factor‐κB (NF‐kB) signaling pathways, receptively. The role of TRAPPC9 in protein trafficking and cytoskeleton organization in osteoclast (OC) has not been studied yet. In this study, we examined the mRNA expression of TRAPPC9 during OC differentiation. Next, we examined the colocalization of TRAPPC9 with cathepsin‐K, known to mediate OC resorption suggesting that TRAPPC9 mediates the trafficking pathway within OC. To identify TRAPPC9 protein partners important for OC‐mediated cytoskeleton re‐organization, we conducted immunoprecipitation of TRAPPC9 in mature OCs followed by mass spectrometry analysis. Our data showed that TRAPPC9 binds various protein partners. One protein with high recovery rate is L‐plastin (LPL). LPL localizes at the podosomes and reported to play a crucial role in actin aggregation thereby actin ring formation and OC function. Although the role of LPL in OC‐mediated bone resorption has not fully reported in detail. Here, first, we confirmed the binding of LPL to TRAPPC9 and, then, we investigated the potential regulatory role of TRAPPC9 in LPL‐mediated OC cytoskeleton reorganization. We assessed the localization of TRAPPC9 and LPL in OC and found that TRAPPC9 is colocalized with LPL at the periphery of OC. Next, we determined the effect of TRAPPC9 overexpression on LPL recruitment to the actin ring using a viral system. Interestingly, our data showed that TRAPPC9 overexpression promotes the recruitment of LPL to the actin ring when compared with control cultures. In addition, we observed that TRAPPC9 overexpression reorganizes actin clusters/aggregates and regulates vinculin recruitment into the OC periphery to initiate podosome formation.

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“…Although Cp does not form a stable complex with transferrin (Tf) [8], its physiological function is acceleration of loading into Tf of ferric ions produced during Cp-catalyzed ferroxidase reaction [9]. Recently the glycation sites in both Cp and Tf were identified in T2D patients [10,11]. However, no significant correlations between HbA1c and serum iron, as well as between HbA1c and TIBC were found in T2D [12].…”

Section: Introductionmentioning

confidence: 99%

The specific activity of proteins involved in iron metabolism depends on compensation of type 2 diabetes mellitus

Voynova

Витальевна²,

Kostevich

et al. 2019

Medical academic journal

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Objective. We aimed to analyze the alterations of activity of iron metabolism members i.e. ceruloplasmin (Cp) and transferrin (Tf), in relation to the percentage of glycated hemoglobin. The latter is one of biochemical criteria of chronic hyperglycemia compensation in case of type 2 diabetes mellitus. Materials and methods. Concentration and activity of Cp and Tf, concentration of iron, copper and lipoprotein cholesterol were measured by biochemical methods in blood serum samples obtained from healthy donors and patients with type 2 diabetes mellitus divided in three groups according to glycated hemoglobin level. Results. The significant decrease in serum copper, ferroxidase activity of Cp and iron-binding capacity of Tf, as well as an increase of Tf concentration, in groups with compensated and uncompensated type 2 diabetes mellitus was found. Conclusion. Our data demonstrate a statistical link between the degree of type 2 diabetes mellitus compensation and alteration of iron metabolism members’ activity. Thus, an increase of hyperglycemia is associated with a decrease of both Cp ferroxidase activity and the degree of Tf saturation with iron. These alterations may explain the efficiency of treatment with iron chelators of such type 2 diabetes mellitus complications as trophic ulcers. The said disease condition is directly connected with the changes in iron efflux.

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Increased serotransferrin and ceruloplasmin turnover in diet-controlled patients with type 2 diabetes

Cited by 48 publications

References 55 publications

Temporal Dynamics of High-Density Lipoprotein Proteome in Diet-Controlled Subjects with Type 2 Diabetes

Temporal Dynamics of High-Density Lipoprotein Proteome in Diet-Controlled Subjects with Type 2 Diabetes

A novel regulatory role of TRAPPC9 in L‐plastin‐mediated osteoclast actin ring formation

The specific activity of proteins involved in iron metabolism depends on compensation of type 2 diabetes mellitus

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