SerpinF2, also known as alpha-2 antiplasmin (alpha-2 AP), is a member of the Serpin superfamily. SerpinF2 is the principal physiological inhibitor of serine protease plasmin, and as well as, an efficient inhibitor of trypsin and chymotrypsin. This protease is produced mainly by liver and kidney, and also expressed in muscle, intestine, central nervous system, and placenta also express this protein at a moderate level. It is indicated that Serpin F2 is a key regulator of plasmin-mediated proteolysis in these tissues. Alpha-2 AP is an unusual serpin in that it contains extensive N- and C-terminal sequences flanking the serpin domain. The N-terminal sequence is crosslinked to fibrin by factor XIIIa, whereas the C-terminal region mediates the initial interaction with plasmin. SerpinF2 is one of the inhibitors of fibrinolysis, which acts as the primary inhibitor of plasmin(ogen). It is a specific plasmin inhibitor, and is important in modulating the effectiveness and persistence of fibrin with respect to its susceptibility to digestion and removal by plasmin. Alpha-2 AP plays the dominant role in inhibiting both plasma clot lysis and thrombus lysis, and accordingly, the congenital deficiency of Alpha-2 antiplasmin causes a rare bleeding disorder because of increased fibrinolysis. Thus, it may be a useful target for developing more effective treatment of thrombotic diseases.
SERPIN G1 is a member of the serpin family, The C-terminal serpin domain is similar to other serpins, and this part of C1-INH provides the inhibitory activity. SERPIN G1 is involved in the inhibition of the complement system to prevent spontaneous activation. SERPIN G1 may play a potentially crucial role in regulating important physiological pathways including complement activation, blood coagulation, fibrinolysis and the generation of kinins. SERPIN G1 prevents the proteolytic cleavage of later complement components C4 and C2 by C1 and MBL. SERPIN G1 is a very efficient physiological inhibitor of FXIIa, plasma kallikrein and fXIa, and could inhibit chymotrypsin and kallikrein. It forms a proteolytically inactive stoichiometric complex with the C1r or C1s proteases in the C1 complex of classical pathway of complement. Activation of the C1 complex is under control of the C1-inhibitor.
Neuroserpin, also known as Protease inhibitor 12 and SERPINI1, is a secreted protein which belongs to the serpin family. Neuroserpin is a serine protease inhibitor that inhibits plasminogen activators and plasmin but not thrombin. Serine protease inhibitors of the serpin superfamily are involved in many cellular processes. Neuroserpin was first identified as a protein secreted from the axons of dorsal root ganglion neurons. Neuroserpin is predominantly expressed in the brain, and is expressed in the late stages of neurogenesis during the process of synapse formation. Overexpression of neuroserpin in an anterior pituitary corticotroph cell line results in the extension of neurite-like processes, suggesting that neuroserpin may play a role in cell communication, cell adhesion, and/or cell migration. Neuroserpin may be involved in the formation or reorganization of synaptic connections, as well as synaptic plasticity in the adult nervous system. Neuroserpin may also protect neurons from cell damage by tissue-type plasminogen activator. Defects of neuroserpin are the cause of familial encephalopathy with neuroserpin inclusion bodies (FEN1B).
The Secreted frizzled-related protein (SFRP) family consists of five secreted glycoproteins in humans (SFRP1~5)that act as extracellular signaling ligands. Each SFRP is approximately 300 amino acids in length and contains a cysteine-rich domain (CRD) that shares 30-50% sequence homology with the CRD ofFrizzled(Fz) receptors, a putative signal sequence, and a conserved hydrophilic carboxy-terminal domain.SFRPs are able to bindWntproteins and Fz receptors in the extracellular compartment. The interaction between SFRPs and Wnt proteins prevents the latter from binding the Fz receptors. The Wnt pathway plays a key role in embryonic development, cell differentiation and cell proliferation. sFRP2 is a member of the SFRP family acting as soluble modulators of Wnt signaling and contains acysteine-rich domain homologous to the putative Wnt-binding site ofFrizzledproteins called FZ domain and a NTR domain.sFRP2 inhibites hypoxia induced endothelial cell apoptosis and increases endothelial cell migration. It prevents mesoderm specification and maintains the cells in the undifferentiated state. SFRP2 is also a novel stimulator of angiogenesis that stimulates angiogenesis via a calcineurin/NFAT pathway, thus is regarded as a favorable target for the inhibition of angiogenesis in solid tumors. Mouse sFRP2 is highly expressed in the eye and is also detected in heart and lung at low level.
SFRP family consists of five secreted glycoproteins in humansacting as extracellular signaling ligands. Each is approximately 300 amino acids in length and contains a cysteine-rich domain (CRD) that shares 30-50% sequence homology with the CRD ofFrizzled(Fz) receptors, a putative signal sequence, and a conserved hydrophilic carboxy-terminal domain.SFRPs act as soluble modulators of Wnt signaling, counteracting Wnt-induced effects at high concentrations and promoting them at lower concentrations. SFRPs are able to bindWntproteins and Fz receptors in the extracellular compartment. The interaction between SFRPs and Wnt proteins prevents the latter from binding the Fz receptors. The Wnt pathway plays a key role in embryonic development, cell differentiation and cell proliferation. SFRP4 is a member of the SFRP family that contains acysteine-rich domain homologous to the putative Wnt-binding site ofFrizzledproteins called FZ domain and a NTR domain . Mouse SFRP4 is highly expressed in the ovary, and is localized to granulosa cells of periovulatory follicles and corpora lutea. It plays a critical role in placental development and implantation, and is also an important factor in the development of the decidual fibrinoid zone, and in trophoblast apoptosis.
Surfactant pulmonary-associated protein D, also known as SFTPD and SP-D, is a member of the collectin family of C-type lectins that is synthesized in many tissues including respiratory epithelial cells in the lung, and contains one C-type lectin domain and one collagen-like domain. The polymorphic variation in the N-terminal domain of the SP-D molecule influences oligomerization, function, and the concentration of the molecule in serum. SFTPD is produced primarily by alveolar type II cells and nonciliated bronchiolar cells in the lung and is constitutively secreted into the alveoli where it influences surfactant homeostasis, effector cell functions, and host defense. It is upregulated in a variety of inflammatory and infectious conditions including Pneumocystis pneumonia and asthma. SFTPD is humoral molecules of the innate immune system, and is considered a functional candidate in chronic periodontitis. Besides it is involved in the development of acute and chronic inflammation of the lung. Several human lung diseases are characterized by decreased levels of bronchoalveolar SFTPD. Thus, recombinant SFTPD has been proposed as a therapeutical option for cystic fibrosis, neonatal lung disease and smoking-induced emphysema. Furthermore, SFTPD serum levels can be used as disease activity markers for interstitial lung diseases.
Pulmonary surfactant-associated protein D (SP-D) is a 43 kDa member of the collectin family of innate immune modulators. Mouse SP-D cDNA encodes a 19 aa signal sequence and a 355 aa mature region with a 25 aa N-terminal linking-region, a 177 aa hydroxyproline and hydroxylysine collagen-like domain, a 46 aa coiled-coil segment, and a 106 aa, C-terminal collectin-like C-type lectin domain . SP-D is found in serum, plasma, broncho-alveolar lavage (BAL) fluid, and amniotic fluid. It also binds SIRP alpha and the calreticulin/CD91 complex on macrophages. SP-D contributes to the lung's defense against inhaled microorganisms, organic antigens and toxins. It Interacts with compounds such as bacterial lipopolysaccharides, oligosaccharides and fatty acids and modulates leukocyte action in immune response. It may participate in the extracellular reorganization or turnover of pulmonary surfactant. It binds strongly maltose residues and to a lesser extent other alpha-glucosyl moieties.
Differential screening of mouse skin cDNA libraries identified cDNA encoding a protein containing a Src homologous 3 (SH3) domain, a novel protein containing a SH3 domain at the carboxyl terminus, and reporting gene expression patterns during the hair growth cycle. The protein shows significant homology with an the yeast protein YHRO 16c/Ysc 84 in its amino and carboxyl terminus, suggesting that it may be a mouse homolog of the yeast protein. Therefore, we name it the Sh3 domain YSC-like 1, Sh3yl1.
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