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Specific protein has vital role in controlling symptoms of allergic asthma …
News-Medical.net An enzyme that helps maintain immune system function by "throwing away" a specific protein has a vital role in controlling symptoms of allergic asthma, new research in mice suggests. The finding suggests that this enzyme, called Cbl-b, could be a … Researchers find potential target for drug to treat allergic asthma |
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Structural insights into the interaction between a potent anti-inflammatory protein, vCCI, and the human CC chemokine, Eotaxin-1.
J Biol Chem. 2014 Jan 30;
Authors: Kuo NW, Gao YG, Schill MS, Isern N, Dupureur CM, Liwang PJ
Abstract
Chemokines play important roles in the immune system, not only recruiting leukocytes to the site of infection and inflammation but also guiding cell homing and cell development. The soluble poxvirus-encoded protein vCCI, a CC chemokine inhibitor, can bind to human CC chemokines tightly to impair the host immune defense. This protein has no known homologs in eukaryotes, and may represent a potent method to stop inflammation. Previously, our structure of the vCCI:MIP-1? complex indicated that vCCI uses negatively charged residues in ?-sheet II to interact with positively charged residues in the MIP-1? N-terminus,20’s region and 40’s loop. However, the interactions between vCCI and other CC chemokines have not yet been fully explored. Here, we used NMR and fluorescence anisotropy to study the interaction between vCCI and eotaxin-1 (CCL11), a CC chemokine that is an important factor in the asthma response. NMR results reveal that the binding pattern is very similar to the vCCI:MIP-1? complex, and suggest that electrostatic interactions provide a major contribution to binding. Fluorescence anisotropy results on variants of eotaxin-1 further confirm the critical roles of the charged residues in eotaxin. In addition, the binding affinity between vCCI and other wild type CC chemokines, MCP-1, MIP-1? and RANTES, were determined as 1.09 nM, 1.16 nM, and 0.22 nM, respectively. To our knowledge, this is the first work quantitatively measuring the binding affinity between vCCI and different CC chemokines.
PMID: 24482230 [PubMed – as supplied by publisher]
View full post on pubmed: asthma
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Protein explains increased asthma severity in children exposed to diesel …
Science Codex A new study shows that exposure to diesel exhaust particles from traffic pollution leads to increased asthma severity in children. Moreover, the study finds that this is due to increased blood levels of IL-17A, a protein associated with several chronic … |
View full post on asthma – Google News
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Protein explains increased asthma severity in children exposed to diesel …
Medical Xpress A new study shows that exposure to diesel exhaust particles from traffic pollution leads to increased asthma severity in children. Moreover, the study finds that this is due to increased blood levels of IL-17A, a protein associated with several chronic … |
View full post on asthma – Google News
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Protein explains increased asthma severity in children exposed to diesel …
EurekAlert (press release) A new study shows that exposure to diesel exhaust particles from traffic pollution leads to increased asthma severity in children. Moreover, the study finds that this is due to increased blood levels of IL-17A, a protein associated with several chronic … |
View full post on asthma – Google News
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Scientists discover protein that helps trigger allergic asthma
HealthCanal.com The findings, published in the journal Science, could help develop more targeted treatments in the future. Allergic asthma is often marked by the symptoms of difficulty breathing in, wheezing and coughing, and can be trigged by different factors in the … |
View full post on asthma – Google News
The Independent |
Scientists discover protein that helps trigger allergic asthma
The Independent Allergic asthma is often marked by symptoms like difficulty drawing breath, wheezing and coughing, and can be trigged by different factors in the environment such as dust, mold or animals. Co-author David Corry explained that "asthma is part of a … |
View full post on asthma – Google News
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Small protein plays big role in asthma severity
EurekAlert (press release) Bethesda, MD—A new culprit has been identified that likely plays a big role in the severity of asthma—a small protein chemokine called CCL26. These findings were published in the Journal of Leukocyte Biology and represent the first demonstration that … |
View full post on asthma – Google News
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Small protein plays big role in asthma severity
Science Codex Bethesda, MD—A new culprit has been identified that likely plays a big role in the severity of asthma—a small protein chemokine called CCL26. These findings were published in the Journal of Leukocyte Biology and represent the first demonstration that … |
View full post on asthma – Google News
Exchange Protein Directly Activated by cAMP (epac): A Multidomain cAMP Mediator in the Regulation of Diverse Biological Functions.
Pharmacol Rev. 2013;65(2):670-709
Authors: Schmidt M, Dekker FJ, Maarsingh H
Abstract
Since the discovery nearly 60 years ago, cAMP is envisioned as one of the most universal and versatile second messengers. The tremendous feature of cAMP to tightly control highly diverse physiologic processes, including calcium homeostasis, metabolism, secretion, muscle contraction, cell fate, and gene transcription, is reflected by the award of five Nobel prizes. The discovery of Epac (exchange protein directly activated by cAMP) has ignited a new surge of cAMP-related research and has depicted novel cAMP properties independent of protein kinase A and cyclic nucleotide-gated channels. The multidomain architecture of Epac determines its activity state and allows cell-type specific protein-protein and protein-lipid interactions that control fine-tuning of pivotal biologic responses through the “old” second messenger cAMP. Compartmentalization of cAMP in space and time, maintained by A-kinase anchoring proteins, phosphodiesterases, and ?-arrestins, contributes to the Epac signalosome of small GTPases, phospholipases, mitogen- and lipid-activated kinases, and transcription factors. These novel cAMP sensors seem to implement certain unexpected signaling properties of cAMP and thereby to permit delicate adaptations of biologic responses. Agonists and antagonists selective for Epac are developed and will support further studies on the biologic net outcome of the activation of Epac. This will increase our current knowledge on the pathophysiology of devastating diseases, such as diabetes, cognitive impairment, renal and heart failure, (pulmonary) hypertension, asthma, and chronic obstructive pulmonary disease. Further insights into the cAMP dynamics executed by the Epac signalosome will help to optimize the pharmacological treatment of these diseases.
PMID: 23447132 [PubMed – as supplied by publisher]
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