Uteroglobin is a small, non-glycosylated secreted protein of the secretoglobin superfamily. It is produced by the non-ciliated, non-mucous secretory cells that predominate in lung bronchioles (Clara cells), and other non-ciliated epithelia that communicate with the external environment. Expression is induced by steroid hormones such as estrogen, and enhanced by the non-steroid hormone prolactin. Human Uteroglobin cDNA encodes a 21 amino acid (aa) signal sequence and a 70 aa mature protein. The mature protein forms a disulfide-linked head-to-tail homodimer of 16 kDa. This homodimer is thought to form a binding pocket that binds hydrophobic ligands such as phospholipids, progesterone and retinols. Binding of fibronectin to Uteroglobin in the kidney is thought to protect against nephropathy, while binding of the lipocalin-1 receptor has been reported to suppress cancer cell motility and invasion.
CD5L, also known as CD5 antigen-like, is a soluble protein belonging to group B of the scavenger receptor cysteine-rich (SRCR) superfamily and contains three SRCR domains. It is a secreted glycoprotein and expressed by macrophages presentin lymphoid tissues (spleen, lymph node, thymus, and bone marrow). It binds to myelomonocytic and lymphoid cells and may play an important role in the regulation of the innate and adaptive immune systems. CD5L functions as a pattern recognition molecule by binding both lipoteichoic acid (LTA) on Gram positive and lipopolysaccharide (LPS) on Gram negative bacteria. and the SRCR domain 1 of CD5L retains both the LPS and LTA binding activities. In addtion, it is revealed that CD5L seems to play a role as an inhibitor of apoptosis.
Coiled-coil domain-containing protein 134(CCDC134), which is short for Coiled-coil domain-containing protein 134, belongs to the UPF0388 family. Human CCDC134 cDNA encodes a 229 amino acid (aa) precursor that contains a 22 aa signal peptide and a 207 aa with coiled-coil domain protein. Coiled-coil domain is a motif in which alpha-helix are coiled together. This protein is usually expressed in extracellular region. CCDC134 is also considered as a novel human MAPK-regulating protein that can inhibit the MAPK pathway.
CCDC47 gene is expressed at high level. The gene contains 16 distinct gt-ag introns. Transcription produces 9 different mRNAs, 6 alternatively spliced variants and 3 unspliced forms. There are 3 probable alternative promotors, 3 non overlapping alternative last exons and 8 validated alternative polyadenylation sites. The mRNAs appear to differ by truncation of the 5' end, truncation of the 3' end, presence or absence of a cassette exon, overlapping exons with different boundaries. Functionally, CCDC47 gene has been proposed to participate in processes such as calcium ion homeostasis, embryo development, ER overload response and post-embryonic development. CCDC47 are expected to have molecular function (calcium ion binding) and to localize in various compartments (membrane, endoplasmic reticulum, integral to membrane, microsome).
C-C Motif Chemokine 11 (CCL11) is a secreted protein that belongs to the intercrine beta (chemokine CC) family. In response to the presence of allergens, CCL11 selectively recruits eosinophils, a prominent feature of allergic inflammatory reactions. The effects of CCL11 are mediated by its binding to a G-protein-linked receptor known as a chemokine receptor. Chemokine receptors for CCL11 include CCR2, CCR3 and CCR5. However, it has been found that CCL11 has high degree selectivity for its receptor, such that they are inactive on neutrophils and monocytes, which do not express CCR3.
Monocyte Chemoattractant Proteins 4 (MCP-4/CCL13) is a member of a distinct, structurally-related subclass of CC chemokines mainly involved in recruitment of eosinphils to inflammatory sites. CCL13/MCP-4, is a CC family chemokine that is chemoattractant for eosinophils, basophils, monocytes, macrophages, immature dendritic cells, and T cells, and its capable of inducing crucial immuno-modulatory responses through its effects on epithelial, muscular and endothelial cells. Similar to other CC chemokines, CCL13 binds to several chemokine receptors (CCR1, CCR2 and CCR3), allowing it to elicit different effects on its target cells. A number of studies have shown that CCL13 is involved in many chronic inflammatory diseases, in which it functions as a pivotal molecule involved in the selective recruitment of cell lineages to the inflamed tissues and their subsequent activation. MCP-4/CCL13 is secreted from chondrocytes and activates the proliferation of rheumatoid synovial cells, thereby leading to joint destruction in RA. The interferon-gamma in combination with interleukin-1beta/tumor necrosis factor-alpha activates the production of MCP-4/CCL13 from chondrocytes in RA joints, and that secreted MCP-4/CCL13 enhances fibroblast-like synoviocyte proliferation by activating the extracellular signal-regulated kinase mitogen-activated protein kinase cascade. CCL13 may have some role in the pathogenesis of systemic sclerosis (SSc).
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