Podocalyxin (PODXL), also known as Podocalyxin-like protein 1 (PCLP-1), is a heavily glycosylated transmembrane sialoprotein in the CD34 and Endoglycan family.Podocalyxin is expressed on glomerular and vascular endothelial cells, neurons, hematopoietic, mesenchymal, and cardiac stem cells, and metastatic carcinoma and glioblastoma tumor cells. A soluble form of Podocalyxin can be released into the urine of women with pre-eclampsia. Podocalyxin promotes platelet activation, neurite outgrowth, branching, and synaptogenesis, homing of hematopoietic progenitor cells to the bone marrow and spleen, and engraftment of mesenchymal and cardiac stem cells into ischemic heart and kidney. Its interactions with L-Selectin and E-Selectin mediate the tethering of lymphocytes and metastatic tumor cells to the vascular endothelium.
Polyubiquitin-B(UBB) is one of Ubiquitins. Ubiquitin is one of the most conserved proteins known in eukaryotic organisms. Ubiquitin is required for ATP-dependent, non-lysosomal intracellular protein degradation of abnormal proteins and normal proteins with a rapid turnover. Ubiquitin is covalently bound to proteins to be degraded, and presumably labels these proteins for degradation.
Protein O-Linked-Mannose β-1 2-N-Acetylglucosaminyltransferase 1 (POMGNT1) belongs to the Glycosyltransferase 13 family. Amino acid residues between 299-311 are important for both protein expression and enzymatic activity. The minimal catalytic domain is located between positions 299-651. It is suggested that the stem domain of the soluble form is unnecessary for activity, but that some amino acids play a crucial role in the membrane-bound form. Defects in POMGNT1 are the cause of muscular dystrophy-dystroglycanopathy congenital with brain and eye anomalies type A3 (MDDGA3).
KIR2DL4, also known as CD158d, is a member of the killer cell Ig-like receptor (KIR) family. KIRs are transmembrane glycoproteins expressed by natural killer cells and subsets of T cells. The KIR genes are polymorphic and highly homologous. KIR2DL4 is expressed in all NK cells and some T cells. KIR2DL4 activates the cytotoxicity of NK cells, despite the presence of an immunoreceptor tyrosine-based inhibition motif (ITIM) in its cytoplasmic tail. The ITIM was not necessary for activation of lysis by KIR2DL4. The activation signal of KIR2DL4 was sensitive to inhibition by another ITIM-containing receptor. The activation-deficient mutant of KIR2DL4 inhibited the signal delivered by the activating receptor CD16.
Periostin ( POSTN ), also known as OSF2 (osteoblast specific factor 2), is a heterofunctional secreted extracellular matrix (ECM) protein comprised of four fasciclin domains that promotes cellular adhesion and movement, as well as collagen fibrillogenesis. Postn is expressed in unique growth centers during embryonic development where it facilitates epithelial-mesenchymal transition (EMT) of select cell populations undergoing reorganization. In the adult, Postn expression is specifically induced in areas of tissue injury or areas with ongoing cellular re-organization. In the adult heart Postn is induced in the ventricles following myocardial infarction, pressure overload stimulation, or generalized cardiomyopathy. Although the detailed function of Postn is still unclear, Postn-integrin interaction is thought to be involved in tumor development. Postn is frequently overexpressed in various types of human cancers, stimulating metastatic growth by promoting cancer cell survival, invasion and angiogenesis, and can be a useful marker to predict the behavior of cancer.
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