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Description

Uteroglobin (UniProt: P17559, also known as Clara cell phospholipid-binding protein, CCPBP, Clara cells 10 kDa secretory protein, CC10, PCB-binding protein, Secretoglobin family 1A member 1, Blastokinin) is encoded by the Scgb1a1 (also known as Cc10, Ugb, Utg) gene (Gene ID: 25575) in rat. Uteroglobin, is a member of the Secretoglobin superfamily that serves as a multifunctional protein and can exert anti-inflammatory and anti-tumorigenic effects by binding small hydrophobic molecules. Uteroglobin is synthesized with a signal peptide of 19 amino acids and consists of a disulfide-linked dimer of two identical polypeptides, each polypeptide being composed of four helices. Uteroglobin derives its name from its high levels of expression in pre-implantation embryos, where it exhibits growth stimulatory effects. It is produced and secreted by the non-ciliated, non-mucous Clara cells predominant in the epithelial surfaces of pulmonary airways. It plays a role in sequestering pro-inflammatory mediators and carcinogens and has been implicated in the inhibition of cell migration and invasion. It inhibits soluble phospholipase A2 activity and binds and perhaps sequesters hydrophobic ligands such as progesterone, phospholipids, prostaglandins, and retinols. Uteroglobin positive (Scgb1a1+) cells in different regions of the lung differ in their role as progenitors in vivo. For example, in the bronchioles, these cells can both self-renew and generate ciliated cells during postnatal growth and adult homeostasis. On the other hand, in the trachea, the majority of uteroglobin positive cells constitute a transient amplifying population during postnatal growth and steady state, and their capacity for self-renewal and multi-lineage differentiation increases in response to injury. (Ref.: Mukherjee, AB et al. (2007). Endocrine Rev. 28(7): 707-725).