Role of Intrahelical Arginine Residues in Functional Properties of Uncoupling Protein (UCP1)†

Biochemistry ◽  
2001 ◽  
Vol 40 (17) ◽  
pp. 5243-5248 ◽  
Author(s):  
Karim S. Echtay ◽  
Martin Bienengraeber ◽  
Martin Klingenberg
Keyword(s):  
Functional Properties ◽  
Uncoupling Protein ◽  
Arginine Residues

scholarly journals Mr 46,000 mannose 6-phosphate receptor. The role of histidine and arginine residues for binding of ligand.

1991 ◽  
Vol 266 (5) ◽  
pp. 2917-2923 ◽  
Author(s):  
M Wendland ◽  
A Waheed ◽  
K von Figura ◽  
R Pohlmann
Keyword(s):  
Arginine Residues ◽  
Mannose 6 Phosphate

Role of correlated disorder on structural stability and functional properties in Na,Ba(Nb,Ti)O3

2021 ◽  
Vol 866 ◽  
pp. 158982
Author(s):  
Sourabh Wajhal ◽  
S.K. Mishra ◽  
A.B. Shinde ◽  
P.S.R. Krishna ◽  
R. Mittal
Keyword(s):  
Structural Stability ◽  
Functional Properties

Irisin exerts dual effects on browning and adipogenesis of human white adipocytes

2016 ◽  
Vol 311 (2) ◽  
pp. E530-E541 ◽  
Author(s):  
Yuan Zhang ◽  
Chao Xie ◽  
Hai Wang ◽  
Robin M. Foss ◽  
Morgan Clare ◽  
...  
Keyword(s):  
Adipose Tissue ◽  
Uncoupling Protein ◽  
Adipogenic Differentiation ◽  
Mapk Signaling ◽  
Cellular Energy ◽  
Subcutaneous White Adipose Tissue ◽  
Basal Expression ◽  
White Adipocytes ◽  
Ucp1 Expression

To better understand the role of irisin in humans, we examined the effects of irisin in human primary adipocytes and fresh human subcutaneous white adipose tissue (scWAT). Human primary adipocytes derived from 28 female donors' fresh scWAT were used to examine the effects of irisin on browning and mitochondrial respiration, and preadipocytes were used to examine the effects of irisin on adipogenesis and osteogenesis. Cultured fragments of scWAT and perirenal brown fat were used for investigating signal transduction pathways that mediate irisin's browning effect by Western blotting to detect phosphorylated forms of p38, ERK, and STAT3 as well as uncoupling protein 1 (UCP1). Individual responses to irisin in scWAT were correlated with basal expression levels of brown/beige genes. Irisin upregulated the expression of browning-associated genes and UCP1 protein in both cultured primary mature adipocytes and fresh adipose tissues. It also significantly increased thermogenesis at 5 nmol/l by elevating cellular energy metabolism (OCR and ECAR). Treating human scWAT with irisin increased UCP1 expression by activating the ERK and p38 MAPK signaling. Blocking either pathway with specific inhibitors abolished irisin-induced UCP1 upregulation. However, our results showed that UCP1 in human perirenal adipose tissue was insensitive to irisin. Basal levels of brown/beige and FNDC5 genes correlated positively with the browning response of scWAT to irisin. In addition, irisin significantly inhibited adipogenic differentiation but promoted osteogenic differentiation. We conclude that irisin promotes “browning” of mature white adipocytes by increasing cellular thermogenesis, whereas it inhibits adipogenesis and promotes osteogenesis during lineage-specific differentiation. Our findings provide a rationale for further exploring the therapeutic use of irisin in obesity and exercise-associated bone formation.

scholarly journals Characterization of the Drosophila protein arginine methyltransferases DART1 and DART4

2004 ◽  
Vol 379 (2) ◽  
pp. 283-289 ◽  
Author(s):  
Marie-Chloé BOULANGER ◽  
Tina Branscombe MIRANDA ◽  
Steven CLARKE ◽  
Marco di FRUSCIO ◽  
Beat SUTER ◽  
...  
Keyword(s):  
Rna Binding ◽  
Developmental Stages ◽  
Rna Binding Proteins ◽  
Genetic System ◽  
Arginine Methylation ◽  
Type I ◽  
Protein Arginine Methyltransferases ◽  
Arginine Residues ◽  
Drosophila Protein

The role of arginine methylation in Drosophila melanogaster is unknown. We identified a family of nine PRMTs (protein arginine methyltransferases) by sequence homology with mammalian arginine methyltransferases, which we have named DART1 to DART9 (Drosophilaarginine methyltransferases 1–9). In keeping with the mammalian PRMT nomenclature, DART1, DART4, DART5 and DART7 are the putative homologues of PRMT1, PRMT4, PRMT5 and PRMT7. Other DART family members have a closer resemblance to PRMT1, but do not have identifiable homologues. All nine genes are expressed in Drosophila at various developmental stages. DART1 and DART4 have arginine methyltransferase activity towards substrates, including histones and RNA-binding proteins. Amino acid analysis of the methylated arginine residues confirmed that both DART1 and DART4 catalyse the formation of asymmetrical dimethylated arginine residues and they are type I arginine methyltransferases. The presence of PRMTs in D. melanogaster suggest that flies are a suitable genetic system to study arginine methylation.

Role of active site arginine residues in substrate recognition by PPM1A

2021 ◽  
Author(s):  
Itsumi Tani ◽  
Shogo Ito ◽  
Yukiko Shirahata ◽  
Yutaka Matsuyama ◽  
James G. Omichinski ◽  
...  
Keyword(s):  
Active Site ◽  
Substrate Recognition ◽  
Arginine Residues

The Role of Interface on the Toughening and Failure Mechanisms of Thermoplastic Nanocomposites Reinforced with Nanofibrillated Rubber

Nanoscale ◽  
2021 ◽  
Author(s):  
Mahdi Zeidi ◽  
Chun Il Kim ◽  
Chul B B. Park
Keyword(s):  
Polymer Nanocomposites ◽  
Functional Properties ◽  
Crucial Role ◽  
Failure Mechanisms

Interface plays a crucial role on the physical and functional properties of polymer nanocomposites, yet its effects have not been fully recognized in the setting of classical continuum-based modeling. In...

scholarly journals Effects of modifications of α-crystallin on its chaperone and other properties

2002 ◽  
Vol 364 (3) ◽  
pp. 711-717 ◽  
Author(s):  
Barry K. DERHAM ◽  
John J. HARDING
Keyword(s):  
Congenital Cataract ◽  
Point Mutations ◽  
Small Heat Shock Protein ◽  
High Molecular Mass ◽  
Lens Crystallins ◽  
Post Translational Modifications ◽  
Chaperone Function ◽  
Arginine Residues

The role of α-crystallin, a small heat-shock protein and chaperone, may explain how the lens stays transparent for so long. α-Crystallin prevents the aggregation of other lens crystallins and proteins that have become unfolded by ‘trapping’ the protein in a high-molecular-mass complex. However, during aging, the chaperone function of α-crystallin becomes compromised, allowing the formation of light-scattering aggregates that can proceed to form cataracts. Within the central part of the lens there is no turnover of damaged protein, and therefore post-translational modifications of α-crystallin accumulate that can reduce chaperone function; this is compounded in cataract lenses. Extensive in vitro glycation, carbamylation and oxidation all decrease chaperone ability. In the present study, we report the effect of the modifiers malondialdehyde, acetaldehyde and methylglyoxal, all of which are pertinent to cataract. Also modification by aspirin, which is known to delay cataract and other diseases, has been investigated. Recently, two point mutations of arginine residues were shown to cause congenital cataract. 1,2-Cyclohexanedione modifies arginine residues, and the extent of modification needed for a change in chaperone function was investigated. Only methylglyoxal and extensive modification by 1,2-cyclohexanedione caused a decrease in chaperone function. This highlights the robust nature of α-crystallin.

scholarly journals The role of Tb-doping on the structural and functional properties of Bi4−xTbxTi3O12 ferroelectric phases with the Aurivillius type structure

2016 ◽  
Vol 28 (6) ◽  
pp. 4914-4924 ◽  
Author(s):  
Tapati Sarkar ◽  
Sergey A. Ivanov ◽  
Elena A. Fortalnova ◽  
Ekaterina D. Politova ◽  
Marina G. Safronenko ◽  
...  
Keyword(s):  
Functional Properties ◽  
Type Structure ◽  
Structural And Functional Properties
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