Cyclophilin C is an enzyme (EC 5.2.1.8) found in both prokaryotes and eukaryotes that interconverts the cis and trans isomers of peptide bonds with the amino acid proline. Proline has an unusually conformationally restrained peptide bond due to its cyclic structure with its side chain bonded to its secondary amine nitrogen. Most amino acids have a strong energetic preference for the trans peptide bond conformation due to steric hindrance, but prolines unusual structure stabilizes the cis form so that both isomers are populated under biologically relevant conditions. Proteins with prolyl isomerase activity include cyclophilin, FKBPs, and parvulin, although larger proteins can also contain prolyl isomerase domains.
Peptidyl-Prolyl Cis-Trans Isomerase D (PPID) belongs to the cyclophilin-type PPIase family and PPIase D subfamily. PPID is widely expressed and it contains one PPIase cyclophilin-type domain and three TPR repeats. PPID catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides and accelerates the folding of proteins. PPID can bind to the immunosuppressant cyclosporine A and is known that its overexpression suppresses the apoptosis in cancer cells.
Peptidyl-prolyl cis-trans isomerase E, also known as Cyclophilin E, Cyclophilin-33, Rotamase E, CYP33, PPIE, is an enzyme which belongs to the cyclophilin-type PPIase family of PPIase E subfamily. PPIE found in all the examined tissues including heart, brain, placenta, lung, liver, skeletal muscle, kidney and pancreas. PPIE contains one PPIase cyclophilin-type domain and one RRM (RNA recognition motif) domain. PPIE accelerates the folding of proteins. It catalyzes the cis-trans isomerization of proline imidic peptide bonds in oligopeptides. PPIE combines RNA-binding and PPIase activities. It may be involved in muscle- and brain-specific processes and pre-mRNA splici
Electron carrier protein. The oxidized form of the cytochrome c heme group can accept an electron from the heme group of the cytochrome c1 subunit of cytochrome reductase. Cytochrome c then transfers this electron to the cytochrome oxidase complex, the final protein carrier in the mitochondrial electron-transport chain.; Plays a role in apoptosis. Suppression of the anti-apoptotic members or activation of the pro-apoptotic members of the Bcl-2 family leads to altered mitochondrial membrane permeability resulting in release of cytochrome c into the cytosol. Binding of cytochrome c to Apaf-1 triggers the activation of caspase-9, which then accelerates apoptosis by activating other caspases.
Proto-oncogene tyrosine-protein kinase Yes, also known as Proto-oncogene c-Yes, p61-Yes and YES1, is a cytoplasm protein which belongs to theprotein kinase superfamily, Tyr protein kinase family and SRC subfamily. YES1 / c-Yes contains oneprotein kinase domain, oneSH2 domain and oneSH3 domain. It is thought that the subcellular distribution of Src-family tyrosine kinases, including c-Yes binding to the cellular membrane, is membranous and/or cytoplasmic. YES1 / c-Yes protein tyrosine kinase is known to be related to malignant transformation. YES1 / c-Yes and c-Src are the two most closely related members of the Src family of nonreceptor tyrosine kinases. Although there is much evidence to support redundancy in signaling between these two kinases. YES1 / c-Yes promotes formation of the tight junction by phosphorylating occludin, while c-Src signaling downregulates occludin formation in a Raf-1 dependent manner. YES1 / c-Yes has tyrosine kinase activity. It promotes infectivity of Neisseria gonorrhoeae in epithelial cells by phosphorylating MCP / CD46.
T-cell-specific surface glycoprotein CD28(CD28) is a single-pass typeI membrane protein which contains one Ig-likeV-type (immunoglobulin-like) domain. It belongs to the immunoglobulin(Ig) superfamily. CD28 is one of the molecules expressed on T cells that provide co-stimulatory signals, which are required for T cell activation.CD28 co-stimulation is necessary for CD4 positive T-cell proliferation and survival, interleukin-2 production, and T-helper type-2 development. Human post-thymic regulatory T cells require CD28 co-stimulation to expand and maintain potent suppressive function in vivo. Apoptosis plays a key role in the age-related decline of CD28 expression and in immunosenescence. CD28 is the receptor for CD80 (B7.1) and CD86 (B7.2). When activated by Toll-like receptor ligands, the CD80 expression is upregulated in antigen presenting cells (APCs). The CD86 expression on antigen presenting cells is constitutive. CD28 is the only B7 receptor constitutively expressed on naive T cells.
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