DPEP2 (MBD-2) belongs to the membrane-bound dipeptidase family. There are three members of this family as membrane-bound dipeptidase-1 (MBD-1),membrane-bound dipeptidase-2 (MBD-2) and membrane-bound dipeptidase-3 (MBD-3).MBD-2 is expressed at highest levels in lung, heart, and testis and at some what lower levels in spleen.MBD-2 is membrane-bound through a glycosylphosphatidyl-inositol linkage and probably is a metalloprotease which hydrolyzes leukotriene D4 (LTD4) into leukotriene E4 (LTE4).It is generally recognized that rapid cleavage of LTD4 is important in inactivating the broncho-and vaso-constrictive effects of cysteinyl LTs in asthmatic and inflammatory processes.
Inactive dipeptidyl peptidase 10, also known as Dipeptidyl peptidase IV-related protein 3, Dipeptidyl peptidase X, Dipeptidyl peptidase-like protein 2, DPRP-3, DPL2 and DPP10, is a single-pass type II membrane protein which belongs to thepeptidase S9B family.DPPIV subfamily. It may modulate cell surface expression and activity of the potassium channels KCND1 and KCND2. DPP10 / DPRP3 has no detectable protease activity, most likely due to the absence of the conserved serine residue normally present in the catalytic domain of serine proteases. However, it does bind specific voltage-gated potassium channels and alters their expression and biophysical properties. Genetic variations in DPP10 are associated with susceptibility to asthma (ASTHMA). The most common chronic disease affecting children and young adults. It is a complex genetic disorder with a heterogeneous phenotype, largely attributed to the interactions among many genes and between these genes and the environment. It is characterized by recurrent attacks of paroxysmal dyspnea, with weezing due to spasmodic contraction of the bronchi.
Dipeptidyl peptidase 3(DPP3), is a member of the S9B family in clan SC of the serine proteases. DPP3 has post-proline dipeptidyl aminopeptidase activity, cleaving Xaa-Pro dipeptides from the N-termini of proteins. This cytoplasmic protein binds a single zinc ion with its zinc-binding motif (HELLGH). It releases an N-terminal dipeptide from a peptide comprising four or more residues, with broad specificity and also acts on dipeptidyl 2-naphthylamides.Increased activity of this protein has a relationship with endometrial and ovarian cancers.
Dipeptidyl peptidase-4 (DPP4) or adenosine deaminase complexing protein 2 (ADCP 2) or T-cell activation antigen CD26 is a serine exopeptidase belonging to the S9B protein family that cleaves X-proline dipeptides from the N-terminus of polypeptides, such as chemokines, neuropeptides, and peptide hormones. The enzyme is a type II transmembrane glycoprotein, expressed on the surface of many cell types. It is also present in serum and other body fluids in a truncated form (sCD26/DPPIV). The soluble CD26 (sCD26) as a tumour marker for the detection of colorectal cancer (CRC) and advanced adenomas. As both a regulatory enzyme and a signalling factor, DPP4 has been evaluated and described in many studies. DPP4 inhibition results in increased blood concentration of the incretin hormones glucagon-like peptide-1 (GLP-1) and gastric inhibitory polypeptide (GIP). This causes an increase in glucose-dependent stimulation, resulting in a lowering of blood glucose levels. Recent studies have shown that DPP4 inhibitors can induce a significant reduction in glycosylated haemoglobin (HbA(1c)) levels, either as monotherapy or as a combination with other antidiabetic agents. Research has also demonstrated that DPP4 inhibitors portray a very low risk of hypoglycaemia development, and are a new pharmacological class of drugs for treating Type 2 diabetes.
CD26 is a signal-anchor for type II membrane protein that belongs to the peptidase S9B family. CD26 is expressed specifically in lymphatic vessels but not in blood vessels in the skin; small intestine; esophagus; ovary; breast and prostate glands. It acts as a positive regulator of T-cell coactivation; by binding at least ADA; CAV1; IGF2R; and PTPRC. It’s binding to CAV1 and CARD11 induces T-cell proliferation and NF-kappa-B activation in a T-cell receptor/CD3-dependent manner. Its interaction with ADA also regulates lymphocyte-epithelial cell adhesion. In association with FAP is involved in the pericellular proteolysis of the extracellular matrix (ECM); the migration and invasion of endothelial cells into the ECM. It may be involved in the promotion of lymphatic endothelial cells adhesion; migration and tube formation. When overexpressed; it enhanced cell proliferation; a process inhibited by GPC3. It acts also as a serine exopeptidase with a dipeptidyl peptidase activity that regulates various physiological processes by cleaving peptides in the circulation; including many chemokines; mitogenic growth factors; neuropeptides and peptide hormones.
The protein encoded by this gene is identical to adenosine deaminase complexing protein-2, and to the T-cell activation antigen CD26. It is an intrinsic membrane glycoprotein and a serine exopeptidase that cleaves X-proline dipeptides from the N-terminus of polypeptides.
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