p 144: sunflower mannose binding lectin-associated serine protease inhibitor-1 (sfmi-1) and -2: significant inhibitors of mannose binding lectin pathway which helps in multiple sclerosis treatment
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abstract
one of the important parts of innate immunity is complement system that occurs in three different ways; the classic, the alternative and the lectin pathway. the four pattern recognition molecules that have been identified till now are mannose binding lectin (mbl), a component of lectin pathway, and three ficolins (ficolin1,-2 and -3) which compound to the carbohydrates of the cell surface. mbl associated serine protease1 (masp-1), masp-2 and -3 are three proteases which associate with recognition molecules. also mbl-associated protein 19 and mbl-associated protein 44 are two non-catalytic molecules that their role is association with recognition molecules. masp-1 and masp-2 activate the lectin pathway but function of masp-3 is unclear. although some researches show that masp-3 down regulates activation of two other masps and has a similar role like mbl-association 19 and mbl-association 44 that they inhibit mbl pathway too. researches show that mbl pathway has a critical role in pathogenesis of autoimmune diseases such as multiple sclerosis (ms). researches indicate that levels of mbl pathway activator components (masp-1 and masp-2) are higher in serum plasma of ms patients. inhibiting activators of mbl pathway seems to be useful for ms treatment and reducing its disabilities. sunflower masp inhibitor-1 (sfmi-1) and sunflower masp inhibitor-2 (sfmi-2) are two peptides with 14 amino acids that inhibit masp-1 and masp-2 and block the lectin pathway activation. this article suggests using sfmi-1 and sfmi-2 in drugs to targeted therapy of ms and decreasing its symptoms.
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P 144: Sunflower Mannose binding Lectin-Associated Serine Protease Inhibitor-1 (SFMI-1) and -2: Significant Inhibitors of Mannose binding Lectin Pathway which Helps in Multiple Sclerosis Treatment
One of the important parts of innate immunity is complement system that occurs in three different ways; the classic, the alternative and the lectin pathway. The four pattern recognition molecules that have been identified till now are Mannose binding lectin (MBL), a component of lectin pathway, and three ficolins (ficolin1,-2 and -3) which compound to the carbohydrates of the cell surface. MBL ...
full textMannose-binding lectin (MBL)-associated serine protease (MASP)-1 contributes to activation of the lectin complement pathway.
The complement system plays an important role in innate immunity. In the lectin complement pathway, mannose-binding lectin (MBL) and ficolins act as recognition molecules, and MBL-associated serine protease (MASP) is a key enzyme. It has been suggested that MASP-2 is responsible for the activation of C4. Other serine proteases (MASP-1 and MASP-3) are also associated with MBL or ficolins; howeve...
full textmannose-binding lectin mediated complement pathway in autoimmune neurological disorders
multiple sclerosis (ms) is a complex, demyelinating disease of the central nervous system (cns) with variable phenotypic presentations, while guillain-barre syndrome (gbs) is the prototypic acute inflammatory disorder that affects the peripheral nervous system. myasthenia gravis (mg) is a t cell dependent and antibody mediated autoimmune disease. although it has been shown that complement plays...
full textMannose-binding lectin-associated serine protease-1 is a significant contributor to coagulation in a murine model of occlusive thrombosis.
Bleeding disorders and thrombotic complications constitute a major cause of death and disability worldwide. Although it is known that the complement and coagulation systems interact, no studies have investigated the specific role or mechanisms of lectin-mediated coagulation in vivo. FeCl(3) treatment resulted in intra-arterial occlusive thrombogenesis within 10 min in wild-type (WT) and C2/fact...
full textA true autoactivating enzyme. Structural insight into mannose-binding lectin-associated serine protease-2 activations.
Few reports have described in detail a true autoactivation process, where no extrinsic cleavage factors are required to initiate the autoactivation of a zymogen. Herein, we provide structural and mechanistic insight into the autoactivation of a multidomain serine protease: mannose-binding lectin-associated serine protease-2 (MASP-2), the first enzymatic component in the lectin pathway of comple...
full textSelective inhibition of the lectin pathway of complement with phage display selected peptides against mannose-binding lectin-associated serine protease (MASP)-1 and -2: significant contribution of MASP-1 to lectin pathway activation.
The complement system, an essential part of the innate immune system, can be activated through three distinct routes: the classical, the alternative, and the lectin pathways. The contribution of individual activation pathways to different biological processes can be assessed by using pathway-selective inhibitors. In this paper, we report lectin pathway-specific short peptide inhibitors develope...
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Journal title:
مجله علوم اعصاب شفای خاتمجلد ۵، شماره ۲، صفحات ۱۷۵-۱۷۵
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