Solution Structure and Dynamics of Myeloid Progenitor Inhibitory Factor-1 (MPIF-1), A Novel Monomeric CC Chemokine

Rajarathnam, Krishna; Li, Yuling; Rohrer, Thomas E.; Gentz, Reiner

doi:10.1074/jbc.m005085200

Cited by 28 publications

(28 citation statements)

References 64 publications

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“…For human CCL15 and CCL23, chemokines that share ϳ64% identity, the extra disulfide seems to have a negligible effect on structure. The extra disulfide in these two chemokines links a 3 10 -helical turn just before the first ␤-strand to the C-terminal ␣-helix and does not disrupt the conserved chemokine fold (17,19). In addition, mutational studies with CCL15 have shown that disruption of the extra disulfide has a minimal effect on protein structure (17).…”

Section: Discussionmentioning

confidence: 99%

Structure-Function Analysis of CCL28 in the Development of Post-viral Asthma

Thomas

Buelow

Nevins

et al. 2015

Journal of Biological Chemistry

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Background: CCL28 is associated with the pathogenesis of acute post-viral asthma. Results: In the absence of viral infection, natively folded CCL28 can induce asthma pathology, whereas unfolded CCL28 cannot. Conclusion:The structure of CCL28 is critical for its role in asthma pathogenesis. Significance: Inhibition of CCL28 presents a novel therapeutic option for the prevention of post-viral asthma.

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Section: Discussionmentioning

confidence: 99%

Structure-Function Analysis of CCL28 in the Development of Post-viral Asthma

Thomas

Buelow

Nevins

et al. 2015

Journal of Biological Chemistry

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“…Chemokines have also been involved in angiogenesis, Th1/Th2 development, and the release of cytokines (46,47). Two CCR1 ligands, CCL3 and CCL23, have been associated respectively with recruitment of monocytes and T cells (12), specific inhibition of myeloid progenitor cells, and activation of monocytes and eosinophils (48). Interestingly, in a CCR1 Ϫ/Ϫ model of chronic allergic asthma, the features of airway remodeling were greatly reduced in CCR1-deficient animals, suggesting an association between CCR1 and the development of airway remodeling (14).…”

Section: Discussionmentioning

confidence: 99%

Expression and Regulation of CCR1 by Airway Smooth Muscle Cells in Asthma

Joubert

Lajoie-Kadoch

Welman

et al. 2008

The Journal of Immunology

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C-C chemokines such as CCL11, CCL5, and CCL3 are central mediators in the pathogenesis of asthma. They are mainly associated with the recruitment and the activation of specific inflammatory cells, such as eosinophils, lymphocytes, and neutrophils. It has recently been shown that they can also activate structural cells, such as airway smooth muscle and epithelial cells. The aims of this study were to examine the expression of the CCL3 receptor, CCR1, on human airway smooth muscle cells (ASMC) and to document the regulation of this receptor by cytokines involved in asthma pathogenesis. We first demonstrated that CCR1 mRNA is increased in the airways of asthmatic vs control subjects and showed for the first time that ASMC express CCR1 mRNA and protein, both in vitro and in vivo. Calcium mobilization by CCR1 ligands confirmed its functionality on ASMC. Stimulation of ASMC with TNF-α and, to a lesser extent, IFN-γ resulted in an up-regulation of CCR1 expression, which was totally suppressed by both dexamethasone or mithramycin. Taken together, our data suggest that CCR1 might be involved in the pathogenesis of asthma, through the activation of ASMC by its ligands.

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“…Many chemokines form homodimers or oligomers at high nanomolar to micromolar concentrations (36-39) whereas others exist strictly as monomers (40)(41)(42)(43)(44). For IL-8, MCP-1, MCP-2, and I-309, the monomeric form predominates in solution at physiological (nM) concentrations (32,44,45).…”

Section: Vv-35kda Protein Monomer Binds Monomeric Mcp-1mentioning

confidence: 99%

Molecular determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor

Seet

Singh

Paavola

et al. 2001

Proc. Natl. Acad. Sci. U.S.A.

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Poxviruses express a family of secreted proteins that bind with high affinity to chemokines and antagonize the interaction with their cognate G protein-coupled receptors (GPCRs). These viral inhibitors are novel in structure and, unlike cellular chemokine receptors, are able to specifically interact with most, if not all, CC-chemokines. We therefore sought to define the structural features of CC-chemokines that facilitate this broad-spectrum interaction. Here, we identify the residues present on human monocyte chemoattractant protein-1 (MCP-1) that are required for highaffinity interaction with the vaccinia virus 35-kDa CC-chemokine binding protein (VV-35kDa). Not only do these residues correspond to those required for interaction with the cognate receptor CCR2b but they are also conserved among many CC-chemokines. Thus, the results provide a structural basis for the ability of VV-35kDa to promiscuously recognize CC-chemokines and block binding to their receptors.CCR2b ͉ chemokine binding protein ͉ monocyte chemoattractant protein-1 ͉ mutagenesis ͉ surface plasmon resonance

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Solution Structure and Dynamics of Myeloid Progenitor Inhibitory Factor-1 (MPIF-1), A Novel Monomeric CC Chemokine

Cited by 28 publications

References 64 publications

Structure-Function Analysis of CCL28 in the Development of Post-viral Asthma

Structure-Function Analysis of CCL28 in the Development of Post-viral Asthma

Expression and Regulation of CCR1 by Airway Smooth Muscle Cells in Asthma

Molecular determinants for CC-chemokine recognition by a poxvirus CC-chemokine inhibitor

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