Major basic protein

PRG2
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1H8U, 2BRS, 4QXX
Identifiers
Aliases	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
External IDs	OMIM: 605601; MGI: 103294; HomoloGene: 2044; GeneCards: PRG2; OMA:PRG2 - orthologs
Gene location (Human)
Chr.	Chromosome 11 (human)
End	57,390,650 bp
Gene location (Mouse)
Chr.	Chromosome 2 (mouse)
End	84,813,976 bp
RNA expression pattern
	Top expressed in
	placenta; ; bone marrow; ; bone marrow cells; ; right lobe of liver; ; skin of leg; ; subcutaneous adipose tissue; ; spleen; ; skin of abdomen; ; monocyte; ; blood;
	Top expressed in
	tibiofemoral joint; ; granulocyte; ; fetal liver hematopoietic progenitor cell; ; bone marrow; ; embryo; ; embryo; ; ankle joint; ; spleen; ; human fetus; ; vestibular membrane of cochlear duct;
	More reference expression data
	More reference expression data
Gene ontology
Molecular function	heparin binding ; carbohydrate binding ; extracellular matrix structural constituent conferring compression resistance ;
Cellular component	extracellular region ; transport vesicle ; cytoplasmic vesicle ; extracellular exosome ; ficolin-1-rich granule lumen ; collagen-containing extracellular matrix ;
Biological process	defense response to bacterium ; immune system process ; defense response to nematode ; negative regulation of interleukin-10 production ; positive regulation of interleukin-4 production ; immune response ; neutrophil degranulation ;
	Sources:Amigo / QuickGO
Orthologs
	5553
	19074
	ENSG00000186652
	ENSMUSG00000027073
	P13727
	Q61878
	NM_002728 ; NM_001243245 ; NM_001302926 ; NM_001302927
	NM_008920
	NP_001230174 ; NP_001289855 ; NP_001289856 ; NP_002719
	NP_032946
	Wikidata
View/Edit Human	View/Edit Mouse

Last updated October 03, 2024

Eosinophil major basic protein, often shortened to major basic protein (MBP; also called Proteoglycan 2 (PRG2)) is encoded in humans by the PRG2 gene.^[5]

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.

Instead, MBP recognises heparan sulfate proteoglycans. Two crystallographic structures of MBP have been determined.^[6]^[7]

Interactions

Major basic protein has been shown to interact with Pregnancy-associated plasma protein A.^[8]^[9]^[10]

Related Research Articles

Eosinophils, sometimes called eosinophiles or, less commonly, acidophils, are a variety of white blood cells and one of the immune system components responsible for combating multicellular parasites and certain infections in vertebrates. Along with mast cells and basophils, they also control mechanisms associated with allergy and asthma. They are granulocytes that develop during hematopoiesis in the bone marrow before migrating into blood, after which they are terminally differentiated and do not multiply.

α₂-Macroglobulin (α₂M) or alpha-2-macroglobulin is a large plasma protein found in the blood. It is mainly produced by the liver, and also locally synthesized by macrophages, fibroblasts, and adrenocortical cells. In humans it is encoded by the A2M gene.

Myelin basic protein (MBP) is a protein believed to be important in the process of myelination of nerves in the nervous system. The myelin sheath is a multi-layered membrane, unique to the nervous system, that functions as an insulator to greatly increase the velocity of axonal impulse conduction. MBP maintains the correct structure of myelin, interacting with the lipids in the myelin membrane.

<span class="mw-page-title-main">P-selectin</span> Type-1 transmembrane protein

P-selectin is a type-1 transmembrane protein that in humans is encoded by the SELP gene.

Aggrecan (ACAN), also known as cartilage-specific proteoglycan core protein (CSPCP) or chondroitin sulfate proteoglycan 1, is a protein that in humans is encoded by the ACAN gene. This gene is a member of the lectican (chondroitin sulfate proteoglycan) family. The encoded protein is an integral part of the extracellular matrix in cartilagenous tissue and it withstands compression in cartilage.

Pappalysin-1, also known as pregnancy-associated plasma protein A, and insulin-like growth factor binding protein-4 protease is a protein encoded by the PAPPA gene in humans. PAPPA is a secreted protease whose main substrate is insulin-like growth factor binding proteins. Pappalysin-1 is also used in screening tests for Down syndrome.

Eosinophil cationic protein (ECP) also known as ribonuclease 3 is a basic protein located in the eosinophil primary matrix. In humans, the eosinophil cationic protein is encoded by the RNASE3 gene.

Eosinophil-derived neurotoxin is an enzyme that in humans is encoded by the RNASE2 gene.

Syndecan-2 is a protein that in humans is encoded by the SDC2 gene.

Guanine nucleotide-binding protein G(q) subunit alpha is a protein that in humans is encoded by the GNAQ gene. Together with GNA11, it functions as a Gq alpha subunit.

C-C chemokine receptor type 3 is a protein that in humans is encoded by the CCR3 gene.

Protein AMBP is a protein that in humans is encoded by the AMBP gene.

Collagen alpha-2(VI) chain is a protein that in humans is encoded by the COL6A2 gene.

Galectin-10 is an enzyme that in humans is encoded by the CLC gene.

Tetranectin is a protein that in humans is encoded by the CLEC3B gene.

Sialic acid-binding Ig-like lectin 7 is a protein that in humans is encoded by the SIGLEC7 gene. SIGLEC7 has also been designated as CD328.

Pregnancy zone protein (PZP), also known as the pregnancy-associated α₂-glycoprotein, is a protein which in humans is encoded by the PZP gene on chromosome 12. PZP is part of the alpha-2 globulin family of proteins. It is often associated with pregnancy, during which it can be the most abundant among the plasma proteins. PZP is believed to play a role in immune-regulation during pregnancy, however many aspects of its mechanism, function and structure are yet to be determined. Recent research has largely focused on determining how dysregulated PZP levels can act as a markers of various diseases.

Pancreatic secretory granule membrane major glycoprotein GP2 is a protein that in humans is encoded by the GP2 gene.

Ficolin-1, and also commonly termed M-ficolin is a protein that in humans is encoded by the FCN1 gene.

Neurocan core protein is a protein that in humans is encoded by the NCAN gene.

References

1 2 3 GRCh38: Ensembl release 89: ENSG00000186652 – Ensembl, May 2017
1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027073 – Ensembl, May 2017
↑ "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
↑ "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
1 2 "Entrez Gene: PRG2 proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)".
↑ PDB: 1h8u ; Swaminathan GJ, Weaver AJ, Loegering DA, Checkel JL, Leonidas DD, Gleich GJ, Acharya KR (July 2001). "Crystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificity". J. Biol. Chem. 276 (28): 26197–26203. doi: 10.1074/jbc.M100848200 . PMID 11319227.
↑ PDB: 2brs ; Swaminathan GJ, Myszka DG, Katsamba PS, Ohnuki LE, Gleich GJ, Acharya KR (November 2005). "Eosinophil-granule major basic protein, a C-type lectin, binds heparin". Biochemistry. 44 (43): 14152–14158. doi:10.1021/bi051112b. PMID 16245931.
↑ Overgaard MT, Haaning J, Boldt H B, Olsen I M, Laursen L S, Christiansen M, Gleich G J, Sottrup-Jensen L, Conover C A, Oxvig C (October 2000). "Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor". J. Biol. Chem. 275 (40). UNITED STATES: 31128–31133. doi: 10.1074/jbc.M001384200 . ISSN 0021-9258. PMID 10913121.
↑ Overgaard MT, Sorensen ES, Stachowiak D, Boldt HB, Kristensen L, Sottrup-Jensen L, Oxvig C (January 2003). "Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment". J. Biol. Chem. 278 (4). United States: 2106–2117. doi: 10.1074/jbc.M208777200 . ISSN 0021-9258. PMID 12421832.
↑ Oxvig C, Sand O, Kristensen T, Gleich G J, Sottrup-Jensen L (June 1993). "Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein". J. Biol. Chem. 268 (17). UNITED STATES: 12243–6. doi: 10.1016/S0021-9258(18)31378-4 . ISSN 0021-9258. PMID 7685339.

External links

Eosinophil+Major+Basic+Protein at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
Overview of all the structural information available in the PDB for UniProt : P13727 (Bone marrow proteoglycan) at the PDBe-KB .

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[refGRCh38Ensembl-1] 1 2 3 GRCh38: Ensembl release 89: ENSG00000186652 – Ensembl, May 2017

[refGRCm38Ensembl-2] 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000027073 – Ensembl, May 2017

[3] "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[4] "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.

[entrez-5] 1 2 "Entrez Gene: PRG2 proteoglycan 2, bone marrow (natural killer cell activator, eosinophil granule major basic protein)".

[pmid11319227-6] PDB: 1h8u ; Swaminathan GJ, Weaver AJ, Loegering DA, Checkel JL, Leonidas DD, Gleich GJ, Acharya KR (July 2001). "Crystal structure of the eosinophil major basic protein at 1.8 A. An atypical lectin with a paradigm shift in specificity". J. Biol. Chem. 276 (28): 26197–26203. doi: 10.1074/jbc.M100848200 . PMID 11319227.

[pmid16245931-7] PDB: 2brs ; Swaminathan GJ, Myszka DG, Katsamba PS, Ohnuki LE, Gleich GJ, Acharya KR (November 2005). "Eosinophil-granule major basic protein, a C-type lectin, binds heparin". Biochemistry. 44 (43): 14152–14158. doi:10.1021/bi051112b. PMID 16245931.

[pmid10913121-8] Overgaard MT, Haaning J, Boldt H B, Olsen I M, Laursen L S, Christiansen M, Gleich G J, Sottrup-Jensen L, Conover C A, Oxvig C (October 2000). "Expression of recombinant human pregnancy-associated plasma protein-A and identification of the proform of eosinophil major basic protein as its physiological inhibitor". J. Biol. Chem. 275 (40). UNITED STATES: 31128–31133. doi: 10.1074/jbc.M001384200 . ISSN 0021-9258. PMID 10913121.

[pmid12421832-9] Overgaard MT, Sorensen ES, Stachowiak D, Boldt HB, Kristensen L, Sottrup-Jensen L, Oxvig C (January 2003). "Complex of pregnancy-associated plasma protein-A and the proform of eosinophil major basic protein. Disulfide structure and carbohydrate attachment". J. Biol. Chem. 278 (4). United States: 2106–2117. doi: 10.1074/jbc.M208777200 . ISSN 0021-9258. PMID 12421832.

[pmid7685339-10] Oxvig C, Sand O, Kristensen T, Gleich G J, Sottrup-Jensen L (June 1993). "Circulating human pregnancy-associated plasma protein-A is disulfide-bridged to the proform of eosinophil major basic protein". J. Biol. Chem. 268 (17). UNITED STATES: 12243–6. doi: 10.1016/S0021-9258(18)31378-4 . ISSN 0021-9258. PMID 7685339.

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