DsbA-L is a versatile player in adiponectin secretion

Wang, Zhao V.; Scherer, Philipp E.

doi:10.1073/pnas.0810027105

Cited by 50 publications

(57 citation statements)

References 15 publications

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“…Therefore, adiponectin is considered a promising candidate in the development of drugs to treat obesity, insulin resistance, T 2 DM, and other metabolic diseases (Wang, Scherer, 2008;Ouchi et al, 2011).…”

Section: Adiponectinmentioning

confidence: 99%

Obesity, inflammation, and insulin resistance

Martins

Oliveira

Cruz

et al. 2014

Braz. J. Pharm. Sci.

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White adipose tissue (WAT) is considered an endocrine organ. When present in excess, WAT can influence metabolism via biologically active molecules. Following unregulated production of such molecules, adipose tissue dysfunction results, contributing to complications associated with obesity. Previous studies have implicated pro-and anti-inflammatory substances in the regulation of inflammatory response and in the development of insulin resistance. In obese individuals, pro-inflammatory molecules produced by adipose tissue contribute to the development of insulin resistance and increased risk of cardiovascular disease. On the other hand, the molecules with anti-inflammatory action, that have been associated with the improvement of insulin sensitivity, have your decreased production. Imbalance of these substances contributes significantly to metabolic disorders found in obese individuals. The current review aims to provide updated information regarding the activity of biomolecules produced by WAT.Uniterms: Obesity. Inflammation. Adipose tissue. Adipokines. Insulin resistance.O tecido adiposo branco (WAT) é considerado um órgão endócrino, que, em excesso, é capaz de controlar o metabolismo, pela ação de moléculas biologicamente ativas. A produção desregulada destas substâncias pela disfunção do tecido adiposo pode contribuir para as complicações presentes na obesidade. As pesquisas atuais têm esclarecido fatores e mecanismos envolvidos na atuação de substâncias pró e anti-inflamatórias na modulação da inflamação e da resistência à insulina. Em indivíduos obesos, as moléculas pró-inflamatórias produzidas pelo tecido adiposo têm sido implicadas como fator contribuinte para o desenvolvimento da resistência à insulina e aumento do risco de doença cardiovascular. Por outro lado, as moléculas com ação anti-inflamatória, que atuam na melhora da sensibilidade à insulina, têm sua produção reduzida. O desequilíbrio entre essas substâncias contribui de forma significativa para as desordens metabólicas presente em indivíduos obesos. Assim, esta revisão visa a trazer informações atualizadas sobre a atuação de moléculas secretadas pelo tecido adiposo. Unitermos:Obesidade. Inflamação. Tecido adiposo. Adipocinas. Resistência à insulina.

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Section: Adiponectinmentioning

confidence: 99%

Obesity, inflammation, and insulin resistance

Martins

Oliveira

Cruz

et al. 2014

Braz. J. Pharm. Sci.

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“…Because the peptide contains a tryptophan (corresponding to Trp 42 in adiponectin), this residue can be used as probe for fluorescence quenching experiments. However, Trp 28 in ERp44, located next to Cys 29 , also contributes to the fluorescence signal albeit at a much smaller level. Despite this "background" signal, a significant decrease in fluorescence was still observed, giving evidence of binding (Fig.…”

Section: Erp44 Binds Lmw and Mmw But Not The Hmw Form Ofmentioning

confidence: 99%

“…For instance, the Cys 160 /Cys 212 pair has been implicated in the regulation of binding to the IP3R1 channel (38), whereas the biological roles of the Cys 289 /Cys 272 pair and that of residue Cys 63 have not yet been assigned. Cys 29 was shown to be responsible for thiolmediated retention and release of ERp44 substrates such as IgM antibodies and oxidoreductase Ero1-␣ and also suggested to be implicated in a similar process with adiponectin (34,36,37). Binding and release of ERp44 substrates is believed to be pH-dependent occurring in the following manner.…”

mentioning

confidence: 99%

“…Binding and release of ERp44 substrates is believed to be pH-dependent occurring in the following manner. A flexible tail at the C terminus of ERp44 shields Cys 29 contained in the CRFS motif at the binding site in the a domain. At higher pH in the ER (pH 7.2), the buried Cys 29 is then deprotonated, and in addition, an RDEL motif facilitates the transport of ERp44 substrates from the Golgi back to the ER upon binding to the KDEL receptors, making the active site inaccessible.…”

mentioning

confidence: 99%

“…A flexible tail at the C terminus of ERp44 shields Cys 29 contained in the CRFS motif at the binding site in the a domain. At higher pH in the ER (pH 7.2), the buried Cys 29 is then deprotonated, and in addition, an RDEL motif facilitates the transport of ERp44 substrates from the Golgi back to the ER upon binding to the KDEL receptors, making the active site inaccessible. It is believed that at lower pH in cis-Golgi (pH 6.7) Cys 29 becomes protonated, a state that exhibits higher affinity to target Cys residues of ERp44 substrates, and the C-terminal tail rearranges to make the active site accessible.…”

mentioning

confidence: 99%

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Regulation and Quality Control of Adiponectin Assembly by Endoplasmic Reticulum Chaperone ERp44

Hampe

Radjainia

et al. 2015

Journal of Biological Chemistry

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Background: ERp44 tightly controls adiponectin assembly in the early secretory compartment. Results: ERp44 exclusively recognizes and converts assembly-trapped adiponectin intermediates back to precursors of the biologically potent high molecular weight form. Conclusion: ERp44 enhances the population of adiponectin intermediates with appropriate oxidative state for HMW assembly. Significance: Our findings provide a mechanism for the regulation of adiponectin assembly and shed light on ERp44 function.

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A Dimension Reduction Approach for Energy Landscape: Identifying Intermediate States in Metabolism‐EMT Network

Kang

2021

Advanced Science

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Dimension reduction is a challenging problem in complex dynamical systems. Here, a dimension reduction approach of landscape (DRL) for complex dynamical systems is proposed, by mapping a high-dimensional system on a low-dimensional energy landscape. The DRL approach is applied to three biological networks, which validates that new reduced dimensions preserve the major information of stability and transition of original high-dimensional systems. The consistency of barrier heights calculated from the low-dimensional landscape and transition actions calculated from the high-dimensional system further shows that the landscape after dimension reduction can quantify the global stability of the system. The epithelial-mesenchymal transition (EMT) and abnormal metabolism are two hallmarks of cancer. With the DRL approach, a quadrastable landscape for metabolism-EMT network is identified, including epithelial (E), abnormal metabolic (A), hybrid E/M (H), and mesenchymal (M) cell states. The quantified energy landscape and kinetic transition paths suggest that for the EMT process, the cells at E state need to first change their metabolism, then enter the M state. The work proposes a general framework for the dimension reduction of a stochastic dynamical system, and advances the mechanistic understanding of the underlying relationship between EMT and cellular metabolism.

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DsbA-L is a versatile player in adiponectin secretion

Cited by 50 publications

References 15 publications

Obesity, inflammation, and insulin resistance

Obesity, inflammation, and insulin resistance

Regulation and Quality Control of Adiponectin Assembly by Endoplasmic Reticulum Chaperone ERp44

A Dimension Reduction Approach for Energy Landscape: Identifying Intermediate States in Metabolism‐EMT Network

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