Corticosteroid-binding globulin (CBG), also known as SerpinA6, is a non-inhibitory member of the serine proteinase inhibitor (serpin) superfamily. It is the high-affinity transport protein for glucocorticoids in vertebrate blood. CBG is specifically cleaved by this protease at a precise site close to its carboxy-terminus. This induces a conformation change and disrupts the binding between glucocorticoids and CBG, and promotes a significant and local release of glucocorticoids (over 90% of them are bound to CBG in human plasma). In this context, CBG directs glucocorticoids to sites of inflammation, and plays in consequence a crucial role in efficient glucocorticoid action in physiology. The SerpinA6 protein is mainly secreted by the liver. This negative acute phase protein regulates free cortisol levels in the blood and distributes cortisol to its target tissues. SerpinA6 deficiency is an extremely rare hereditary disorder characterized by reduced corticosteroid-binding capacity with normal or low plasma corticosteroid-binding globulin concentration, and normal or low basal cortisol levels associated with hypo-/hypertension and muscle fatigue. There are three heritable, human CBG gene mutations that can reduce CBG-cortisol binding affinity and/or reduce circulating CBG levels.
Serpin A7 is a secreted protein which belongs to the Serpin family. As a 54 kDa protein, Serpin A7 is synthesized primarily in the liver and secreted in plasma. Genomically, Serpin A7 is a serpin, although it has no inhibitory function like many other members of this class of proteins. Serpin A7 binds thyroid hormone in circulation. It is one of three proteins (along with transthyretin and albumin) responsible for carrying the thyroid hormones thyroxine (T4) and 3,5,3’-triiodothyronine (T3) in the bloodstream. Of these three proteins, Serpin A7 has the highest affinity for T4 and T3, but is present in the lowest concentration. Despite its low concentration, Serpin A7 carries the majority of T4 in serum. Due to the very low serum concentration of T4 and T3 in the blood, Serpin A7 is rarely more than 25% saturated with its ligand. Unlike transthyretin and albumin, Serpin A7 has a single binding site for T4/T3. Serpin A7 tests are sometimes used in finding the reason for elevated or diminished levels of thyroid hormone, and defects in Serpin A7 are a cause of Serpin A7 deficiency.
Thyroxine-binding globulin, also known as T4-binding globulin, Serpin A7 and TBG, is a secreted protein which belongs to theserpin family. TBG is synthesized primarily in theliveras a 54 kDa protein.TBG is genomically aserpin, although it has no inhibitory function like many other members of this class of proteins. TBG binds thyroid hormone in circulation. It is one of three proteins(along with transthyretin and albumin) responsible for carrying thethyroidhormones thyroxine(T4) and 3,5,3’-triiodothyronine (T3) in the bloodstream. Of these three proteins, TBG has the highest affinity for T4 and T3, but is present in the lowest concentration. Despite its low concentration, TBG carries the majority of T4 inserum. Due to the very low serum concentration of T4 and T3, TBG is rarely more than 25% saturated with itsligand. Unlike transthyretin and albumin, TBG has a single binding site for T4/T3. TBG tests are sometimes used in finding the reason for elevated or diminished levels of thyroid hormone.
Serpin B12 is a member of the serpin family. Serpins are the largest and most diverse family of serine protease inhibitors. Most serpins are secreted and attain physiologic concentrations in the blood and extracellular fluids. Serpin B12 is expressed in many tissues, including brain, bone marrow, lymph node, heart, lung, liver, pancreas, testis, ovary, and intestine. Serpins are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. SerpinB12 inhibits trypsin and plasmin, but not thrombin, coagulation factor Xa, or urokinase-type plasminogen activator.
SerpinB1 is an endogenous inhibitor of serine proteases recognized for its anti-inflammatory and host-protective properties. Serum SerpinB1 levels are elevated in patients with type 2 diabetes compared with that in healthy subjects and are negatively correlated with serum LDL-C. serpinB1 as an endogenous protein that can potentially be harnessed to enhance functional beta cell mass in patients with diabetes.
SERPINB1 is a member of the serpin family and Ov-serpin subfamily. As protease inhibitors; serpins have an array of functions including regulating blood coagulation; fibrinolysis; the complement pathway; angiogenesis; inflammation; tumor suppression; extracellular matrix remodeling; and cell motility. SERPINB1 regulates the activity of the neutrophil proteases elastase; cathepsin G; proteinase-3; chymase; chymotrypsin; and kallikrein-3. Reactive bond 1 of SerpinB1 is specific for reaction with chymotrypsin-like protease such as cathepsin G; chymotrypsin or chymase. Reactive bond 2 of SerpinB1 is specific for reaction with elastase-like protease such as neutrophyl elastase; proteinase-3; pancreatic elastase or PSA. In addition; SERPINB1 also functions as a potent intracellular inhibitor of granzyme H.
Serpins are the largest and most diverse family of serine protease inhibitors which are involved in a number of fundamental biological processes such as blood coagulation, complement activation, fibrinolysis, angiogenesis, inflammation and tumor suppression and are expressed in a cell-specific manner. SerpinB2, also known as Plasminogen activator inhibitor 2, Placental plasminogen activator inhibitor, Monocyte Arg-serpin, Urokinase inhibitor and PAI2, is a cytoplasm protein which belongs to theserpin family and Ov-serpin subfamily. SerpinB2 is a major product of activated monocytes and macrophages and is substantially induced during most inflammatory processes. Distinct from its widely described extracellular role as an inhibitor of urokinase plasminogen activator. SerpinB2 has been shown to have an intracellular role as a retinoblastoma protein (Rb)-binding protein that inhibits Rb degradation. SerpinB2 is widely described as an inhibitor of urokinase plasminogen activator. SerpinB2 inhibits urokinase-type plasminogen activator. The monocyte derived SerpinB2 is distinct from the endothelial cell-derived PAI-1. SerpinB2 is a potentially important inducible host factor that significantly promotes HIV-1 replication.
Serpin B3, also known as squamous cell carcinoma antigen-1 (SCCA-1), is a member of the serpin superfamily of serine protease inhibitors. Serpin B3 belongs to the subgroup ovalbumin-related serpins which are involved in the regulation of apoptosis, inflammation, angiogenesis and embryogenesis. It may act as a papain-like cysteine protease inhibitor to modulate the host immune response against tumor cells. It also functions as an inhibitor of UV-induced apoptosis via suppression of the activity of c-Jun NH(2)-terminal kinase (JNK1).
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