Proteomic analysis of mature adipo cytes from obese patients in relation to aging

Alfadda, Assim A.; Benabdelkamel, Hicham; Masood, Afshan; Moustafa, Amr Soliman; Sallam, Reem M.; Bassas, Abdulelah F.; Duncan, M. H.

doi:10.1016/j.exger.2013.07.008

Cited by 70 publications

(112 citation statements)

References 48 publications

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“…This mouse model of PHB overexpression confirmed an important role of PHB in the regulation of adipose tissue homeostasis at the systemic level in mice, and revealed a sex-dimorphic role of PHB in adipose tissue function. Furthermore, PHB has been found to be upregulated in dietinduced obese mouse models [26], as well as in the adipose tissue of patients with obesity [39]. Of note, the PHB gene has been mapped to the chromosome locus 17q12-q21 in humans [40], a region that in a genome-wide scan was identified among chromosomal regions harboring genes that influence the propensity to store fat in the abdominal area [41].…”

mentioning

confidence: 99%

Prohibitin in Adipose and Immune Functions

Ande

Nguyen

Nyomba

et al. 2016

Trends in Endocrinology & Metabolism

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mentioning

confidence: 99%

Prohibitin in Adipose and Immune Functions

Ande

Nguyen

Nyomba

et al. 2016

Trends in Endocrinology & Metabolism

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“…The spots from Coomassie-stained gels were excised manually, washed, and digested according to a previously published protocol [43]. The mixture of tryptic peptides (1 µL), derived from each protein, was spotted onto a MALDI (Matrix-assisted laser desorption/ionization) target (384 anchorchip MTP 800 µm Anchorchip; Bruker Daltonics, Bremen, Germany) together with 0.8 μL of matrix (10 mg α-cyano-4-hydroxycinnamic acid (CHCA) in 1 μL of 30% CH 3 CN and 0.1% aqueous CF 3 COOH) and then left to dry (RT) before MS analysis.…”

Section: Methodsmentioning

confidence: 99%

Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins

Benabdelkamel

Alanazi

Alzahrani

et al. 2017

IJMS

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Camel milk is consumed in the Middle East because of its high nutritional value. Traditional heating methods and the duration of heating affect the protein content and nutritional quality of the milk. We examined the denaturation of whey proteins in camel milk by assessing the effects of temperature on the whey protein profile at room temperature (RT), moderate heating at 63 °C, and at 98 °C, for 1 h. The qualitative and quantitative variations in the whey proteins before and after heat treatments were determined using quantitative 2D-difference in gel electrophoresis (DIGE)-mass spectrometry. Qualitative gel image analysis revealed a similar spot distribution between samples at RT and those heated at 63 °C, while the spot distribution between RT and samples heated at 98 °C differed. One hundred sixteen protein spots were determined to be significantly different (p < 0.05 and a fold change of ≥1.2) between the non-heated and heated milk samples. Eighty protein spots were decreased in common in both the heat-treated samples and an additional 25 spots were further decreased in the 98 °C sample. The proteins with decreased abundance included serum albumin, lactadherin, fibrinogen β and γ chain, lactotransferrin, active receptor type-2A, arginase-1, glutathione peroxidase-1 and, thiopurine S, etc. Eight protein spots were increased in common to both the samples when compared to RT and included α-lactalbumin, a glycosylation-dependent cell adhesion molecule. Whey proteins present in camel milk were less affected by heating at 63 °C than at 98 °C. This experimental study showed that denaturation increased significantly as the temperature increased from 63 to 98 °C.

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“…The aging process has repeatedly been shown to be associated with the pronounced decrease of the expression [19,28] and activities [19] of ACL and FAS in rat adipose tissue. In our study we demonstrated that not only were ACL and FAS activities in WAT decreased in the old rats, but also that depot-specific differences in the enzymatic response to refeeding were largely abolished in the old as compared to the young animals.…”

Section: Discussionmentioning

confidence: 99%

“…A recent study employing proteome analysis of subcutaneous WAT biopsies from young and old obese female patients did not report any differences in protein levels of lipogenic enzymes [28]. Another study compared the gene expression of two isoforms of a crucial lipogenic enzyme: ACCα (mostly found in heart and skeletal muscle) and ACCβ (characteristic for liver and WAT), in subcutaneous abdominal and gluteal fat of premenopausal and postmenopausal women, showing decreased ACCα expression in the abdominal depot, but increased ACCβ expression in the gluteal depot [37].…”

Section: Discussionmentioning

confidence: 99%

White Adipose Tissue Depot-Specific Activity of Lipogenic Enzymes in Response to Fasting and Refeeding in Young and Old Rats

et al. 2015

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Background: Although the heterogeneity of white adipose tissue (WAT) in different anatomical sites is a well-known phenomenon, there are scarce data on aging-associated metabolic alterations in various WAT depots. Objective: We used the model of fasting and refeeding to analyze the effect of aging on the activity of key lipogenic enzymes in retroperitoneal (rWAT), epididymal (eWAT), and subcutaneous (sWAT) adipose tissue depots. Methods: 5- and 24-month-old male Wistar rats were fasted for 48 h or were fasted for 2 days and subsequently refed for 2 or 4 days. Control animals had ad libitum access to chow. Samples obtained from three WAT deposits were analyzed for the enzymatic activities of ATP citrate lyase (ACL), fatty acid synthase (FAS), and glucose-6-phosphate dehydrogenase (G6PD). Concentrations of lipids and proteins were measured in the blood serum. Results: Fasting for 2 days decreased the concentration of free fatty acids only in the young rats. The basal activities of ACL and FAS were lower in eWAT than in rWAT and sWAT of the young rats. In the young rats, fasting did not change ACL and FAS activities in any of the studied depots. Refeeding increased these activities more quickly in rWAT than in eWAT, while in sWAT no induction was observed. ACL and FAS activities were manifold lower in all WAT depots of the old than in those of the young rats. In the old animals fasting had no effect on ACL activity in any depot and decreased FAS activity only in sWAT. After 4 days of refeeding, FAS activity increased in rWAT and sWAT, but no change in ACL activity occurred. G6PD activity in the young rats was lower by 40% in eWAT than in rWAT. The induction of the enzyme by refeeding occurred faster in rWAT than in eWAT, while in sWAT no change in G6PD activity was observed. G6PD activity did not change with aging. Fasting of the old rats decreased G6PD activity in rWAT and sWAT. Refeeding failed to induce the enzyme in these depots, whereas in eWAT G6PD activity increased by 76% after 4 days of refeeding. Conclusion: Fasting and refeeding revealed WAT depot-specific, age-related changes of the activities of lipogenic enzymes.

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Proteomic analysis of mature adipo cytes from obese patients in relation to aging

Cited by 70 publications

References 48 publications

Prohibitin in Adipose and Immune Functions

Prohibitin in Adipose and Immune Functions

Proteomic Profiling Comparing the Effects of Different Heat Treatments on Camel (Camelus dromedarius) Milk Whey Proteins

White Adipose Tissue Depot-Specific Activity of Lipogenic Enzymes in Response to Fasting and Refeeding in Young and Old Rats

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