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PRG2, BMPG, MBP, MBP1, proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein), proMBP, proteoglycan 2, pro eosinophil major basic protein
Eosinophil major basic protein, often shortened to major basic protein (MBP; also called Proteoglycan 2 (PRG2)) is encoded in humans by the PRG2gene.[5]
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Eosinophils| Eosinophil and its role in immunity | What causes high eosinophil? | Eosinophilia
Protein Structure and Folding
Protein Structure
Protein Synthesis (Updated)
Protein Synthesis | Cells | Biology | FuseSchool
Transcription
Function
The protein encoded by this gene is the predominant constituent of the crystalline core of the eosinophil granule. High levels of the proform of this protein are also present in placenta and pregnancy serum, where it exists as a complex with several other proteins including pregnancy-associated plasma protein A (PAPPA), angiotensinogen (AGT), and C3dg. This protein may be involved in antiparasitic defense mechanisms as a cytotoxin and helmintho-toxin, and in immune hypersensitivity reactions. It is directly implicated in epithelial cell damage, exfoliation, and bronchospasm in allergic diseases.[5]
PRG2 is a 117-residue protein that predominates in eosinophil granules. It is a potent enzyme against helminths and is toxic towards bacteria and mammalian cells in vitro. The eosinophil major basic protein also causes the release of histamine from mast cells and basophils, and activates neutrophils and alveolar macrophages.
Structure
Structurally the major basic protein (MBP) is similar to lectins (sugar-binding proteins), and has a fold similar to that seen in C-type lectins. However, unlike other C-type lectins (those that bind various carbohydrates in the presence of calcium), MBP does not bind either calcium or any of the other carbohydrates that this family recognize.
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Oxvig C, Haaning J, Højrup P, Sottrup-Jensen L (1994). "Location and nature of carbohydrate groups in proform of human major basic protein isolated from pregnancy serum". Biochem. Mol. Biol. Int. 33 (2): 329–36. PMID7524900.
Bonno M, Oxvig C, Kephart GM, Wagner JM, Kristensen T, Sottrup-Jensen L, Gleich GJ (1994). "Localization of pregnancy-associated plasma protein-A and colocalization of pregnancy-associated plasma protein-A messenger ribonucleic acid and eosinophil granule major basic protein messenger ribonucleic acid in placenta". Lab. Invest. 71 (4): 560–6. PMID7526035.
Shikata Y, Hayashi Y, Yoshimatsu K, Ohya Y, Seto T, Fukushima K, Yoshida Y (1993). "Pro-major basic protein has three types of sugar chains at the pro-portion". Biochim. Biophys. Acta. 1163 (3): 243–9. doi:10.1016/0167-4838(93)90158-N. PMID8507662.
Nittoh T, Watanabe M, Okayama H, Misawa S, Isobe Y, Hayashi H, Mue S, Ohuchi K (1996). "Cloning of cDNA for rat eosinophil major basic protein". Biochim. Biophys. Acta. 1264 (3): 261–4. doi:10.1016/0167-4781(95)00183-2. PMID8547309.
This page was last edited on 27 January 2024, at 04:45