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Mammalian allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2020
Tuomas Virtanen, Marja Rytkönen-Nissinen
Fel d 1 is a glycoprotein with a molecular mass of 38 kDa [63]. It is a tetramer composed of two noncovalently linked heterodimers, each with a molecular mass of about 19 kDa. These dimers are composed of an 8-kDa chain 1 (α-chain) and 10-kDa chain 2 (β-chain), which are linked together covalently by three disulfide bonds. Chain 1 contains 70 amino acids, and the dominant forms of chain 2 contain 90 or 92 amino acids [64,65]. Chain 1 has a 29% amino acid identity with human uteroglobin, an anti-inflammatory protein (BLAST). Chain 2 has an amino acid identity of 39% with a putative human protein in a segment of 41 amino acids (BLAST). Both chains are classified as members of the secretoglobin (uteroglobin) family. Fel d 1 exists in several isoforms [63] and can be produced in a recombinant form. The three-dimensional structure of Fel d 1 is strikingly similar to that of uteroglobin and contains two cavities with potential for ligand binding [66].
Mammalian Allergens
Published in Richard F. Lockey, Dennis K. Ledford, Allergens and Allergen Immunotherapy, 2014
Tuomas Virtanen, Tuure Kinnunen, Marja Rytkönen-Nissinen
Fel d 1 is a glycoprotein with a molecular mass of 38 kDa.42 It is a tetramer composed of two noncovalently linked heterodimers each with a molecular mass of about 19 kDa. These dimers comprise an 8 kDa chain 1 (α-chain) and 10 kDa chain 2 (β-chain), which are linked together covalently by three disulfide bonds. Chain 1 contains 70 and chain 2 contains 90–92 amino acids.43,44 Chain 1 exhibits a 28% amino acid identity with human uteroglobin, an anti-inflammatory protein (SBNS). Chain 2 shows an amino acid identity of 39% with a human protein in a segment of 41 amino acids (SBNS). Both chains are classified as members of the secretoglobin (uteroglobin) family. Fel d 1 exists in several isoforms.42 It can be produced in a recombinant form. The three-dimensional structure of Fel d 1 is strikingly similar to that of uteroglobin.45
Club cell 10-kDa protein (CC10) as a surrogate for identifying type 2 asthma phenotypes
Published in Journal of Asthma, 2023
Meijia Wang, Kun Tang, Pengfei Gao, Yanjiao Lu, Shanshan Wang, Xiaojie Wu, Jianping Zhao, Jungang Xie
Club cell 10-kDa protein (CC10) belongs to the secretoglobin family, and is primarily produced by nonciliated club cells in the distal airway and in nasal epithelial cells, and can be detected in the circulation (10,11). It is reported that CC10 inhibits inflammation through the suppression of phospholipase A2 activity (12), downregulation of Th2 cell differentiation (13), and inhibition of inflammatory cytokine production (14). Previous studies suggest that adeno-associated virus (AAV)2/9-CC10 vector virus significantly reduces airway hyperresponsiveness, Th2 cytokines expression, and eosinophilia in the lungs of OVA-sensitized mice (15). Serum CC10 level in patients with asthma is significantly lower than in control subjects (16), but whether the expression of CC10 differs between T2-high asthma and T2-low asthma is still unknown. Therefore, in this study, we sought to examine the ability of serum CC10 to predict type 2 asthmatic phenotypes.
Reaction products of hexamethylene diisocyanate vapors with “self” molecules in the airways of rabbits exposed via tracheostomy
Published in Xenobiotica, 2018
Adam V. Wisnewski, Jean Kanyo, Jennifer Asher, James A. Goodrich, Grace Barnett, Lyn Patrylak, Jian Liu, Carrie A. Redlich, Ala F. Nassar
Uteroglobin as a reaction target for inhaled HDI vapor is a novel finding of the present study. Rabbit uteroglobin is the homolog of human secretoglobin family 1 A member 1 (SCGB1A1) and is commonly referred to by a variety of different names (Clara or club cell protein, CC10, CC16, blastokinin or polychlorinated biphenyl-binding protein) depending upon species/tissue source (Mantile et al., 1993; Mukherjee et al., 2007; Wolf et al., 1992). SCGB1A1 is relatively abundant in the airways, where it is secreted by nonciliated cells that specialize in chemical metabolism (Mukherjee et al., 2007). Polymorphism in human SCGB1A1 is associated with reduced levels of protein and increased likelihood of developing asthma (Candelaria et al., 2005; Ku et al., 2011; Laing et al., 2000; Taniguchi et al., 2013). Of particular relevance to the present study are findings (Kultz et al., 2015) demonstrating uteroglobin as a reaction target for naphthalene, a xenobiotic metabolically activated within Clara cells. Kultz et al suggest chemical modification of proteins such as uteroglobin, which normally exhibit anti-inflammatory activity (Miele et al., 1987; Mukherjee et al., 2007; Ray et al., 2006; Shijubo et al., 2003; Vasanthakumar et al., 1988), may be key to the pathophysiology associated with certain xenobiotic exposures (Kultz et al., 2015). Further investigation, beyond the scope of this study, will be needed to determine if human uteroglobin is also susceptible to HDI modification in vivo, and if so, its potential relevance to occupational exposure and/or disease pathogenesis.
Therapeutic targets for inflammation-mediated airway remodeling in chronic lung disease
Published in Expert Review of Respiratory Medicine, 2018
A previously unresolved problem has been identification of the initial innate sentinel cells, e.g. those responsible for triggering innate inflammation. Candidates include alveolar macrophages, intraepithelial lymphocytes, natural killer cells, and the epithelium itself. Recent advances using tissue-specific knockouts have provided new major insights into the identity of airway sentinels in response to luminal virus. An interesting epithelial population found in the bronchiolar alveolar junction expresses both secretoglobin (Scgb1a1) and surfactant; these cells function as progenitor cells responsible for populating the distal bronchioles in response to injury [55]. Recent work using small animal models selectively depleting NFκB/RelA in these bronchiolar stem cells by Cre recombinase [55] have provided definitive proof that derivatives of these cells [55,56], are the major functionally important innate sensors of viral infection (Figure 1). Mice with deletion of NFκB/RelA in the Scgb1a1 progenitor-derived population have significantly reduced inflammation and remodeling in response to RSV infection [56]. Similarly, TLR3-driven viral inflammation is also mediated by the same bronchiolar-derived epithelial cells. Like that of RSV, deletion of NFκB/RelA in the Scgb1a1+ progenitors mice respond to TLR3 agonism with reduced neutrophilia, epithelial dependent chemokine expression and myofibroblast expansion [57]. It is important to note that poly(I:C) mimics acute aspects of RNA virus infections [58], producing inflammatory signatures characteristic of COPD and airway hyper reactivity [59].