MASP1 (protein)

Template:PBB Mannan-binding lectin serine protease 1 also known as mannose-associated serine protease 1 (MASP-1) is an enzyme that in humans is encoded by the MASP1 gene.^[1]^[2]^[3]

MASP-1 is involved in the lectin pathway of the complement system and is responsible for cleaving C4 and C2 to form C4b2a, a C3-convertase.^[4]

Function

MASP-1 is a serine protease that functions as a component of the lectin pathway of complement activation. The complement pathway plays an essential role in the innate and adaptive immune response. MASP-1 is synthesized as a zymogen and is activated when it complexes with the pathogen recognition molecules of lectin pathway, the mannose-binding lectin and the ficolins. This protein is not directly involved in complement activation but may play a role as an amplifier of complement activation by cleaving complement C2 or by activating another complement serine protease, MASP-2. MASP-1 is also able to cleave fibrinogen and factor XIII and may be involved in coagulation. A splice variant of this gene which lacks the serine protease domain functions as an inhibitor of the complement pathway.^[3]

References

^ Takada F, Takayama Y, Hatsuse H, Kawakami M (Oct 1993). "A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum". Biochemical and Biophysical Research Communications. 196 (2): 1003–9. doi:10.1006/bbrc.1993.2349. PMID 8240317.
^ Sato T, Endo Y, Matsushita M, Fujita T (Apr 1994). "Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein". International Immunology. 6 (4): 665–9. doi:10.1093/intimm/6.4.665. PMID 8018603.
^ ^a ^b "Entrez Gene: mannan-binding lectin serine peptidase 1 (C4/C2 activating component of Ra-reactive factor)".
^ Matsushita M, Thiel S, Jensenius JC, Terai I, Fujita T (Sep 2000). "Proteolytic activities of two types of mannose-binding lectin-associated serine protease". Journal of Immunology. 165 (5): 2637–42. doi:10.4049/jimmunol.165.5.2637. PMID 10946292.

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Petersen SV, Thiel S, Jensenius JC (Aug 2001). "The mannan-binding lectin pathway of complement activation: biology and disease association". Molecular Immunology. 38 (2–3): 133–49. doi:10.1016/S0161-5890(01)00038-4. PMID 11532276.
Rajaraman P, Brenner AV, Butler MA, Wang SS, Pfeiffer RM, Ruder AM, Linet MS, Yeager M, Wang Z, Orr N, Fine HA, Kwon D, Thomas G, Rothman N, Inskip PD, Chanock SJ (May 2009). "Common variation in genes related to innate immunity and risk of adult glioma". Cancer Epidemiology, Biomarkers & Prevention. 18 (5): 1651–8. doi:10.1158/1055-9965.EPI-08-1041. PMC 2771723. PMID 19423540.
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Skjoedt MO, Hummelshoj T, Palarasah Y, Honore C, Koch C, Skjodt K, Garred P (Mar 2010). "A novel mannose-binding lectin/ficolin-associated protein is highly expressed in heart and skeletal muscle tissues and inhibits complement activation". The Journal of Biological Chemistry. 285 (11): 8234–43. doi:10.1074/jbc.M109.065805. PMC 2832975. PMID 20053996.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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Kocsis A, Kékesi KA, Szász R, Végh BM, Balczer J, Dobó J, Závodszky P, Gál P, Pál G (Oct 2010). "Selective 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". Journal of Immunology. 185 (7): 4169–78. doi:10.4049/jimmunol.1001819. PMID 20817870.
Rooryck C, Diaz-Font A, Osborn DP, Chabchoub E, Hernandez-Hernandez V, Shamseldin H, Kenny J, Waters A, Jenkins D, Kaissi AA, Leal GF, Dallapiccola B, Carnevale F, Bitner-Glindzicz M, Lees M, Hennekam R, Stanier P, Burns AJ, Peeters H, Alkuraya FS, Beales PL (Mar 2011). "Mutations in lectin complement pathway genes COLEC11 and MASP1 cause 3MC syndrome". Nature Genetics. 43 (3): 197–203. doi:10.1038/ng.757. PMC 3045628. PMID 21258343.
Megyeri M, Makó V, Beinrohr L, Doleschall Z, Prohászka Z, Cervenak L, Závodszky P, Gál P (Sep 2009). "Complement protease MASP-1 activates human endothelial cells: PAR4 activation is a link between complement and endothelial function". Journal of Immunology. 183 (5): 3409–16. doi:10.4049/jimmunol.0900879. PMID 19667088.
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Kang JU, Koo SH, Kwon KC, Park JW, Kim JM (2009). "Identification of novel candidate target genes, including EPHB3, MASP1 and SST at 3q26.2-q29 in squamous cell carcinoma of the lung". BMC Cancer. 9: 237. doi:10.1186/1471-2407-9-237. PMC 2716371. PMID 19607727.{{cite journal}}: CS1 maint: unflagged free DOI (link)
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Duus K, Thielens NM, Lacroix M, Tacnet P, Frachet P, Holmskov U, Houen G (Dec 2010). "CD91 interacts with mannan-binding lectin (MBL) through the MBL-associated serine protease-binding site". The FEBS Journal. 277 (23): 4956–64. doi:10.1111/j.1742-4658.2010.07901.x. PMID 21054788.
Degn SE, Jensen L, Gál P, Dobó J, Holmvad SH, Jensenius JC, Thiel S (Sep 2010). "Biological variations of MASP-3 and MAp44, two splice products of the MASP1 gene involved in regulation of the complement system". Journal of Immunological Methods. 361 (1–2): 37–50. doi:10.1016/j.jim.2010.07.006. PMID 20673767.

External links

MASP+Proteases at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.

[pmid8240317-1] Takada F, Takayama Y, Hatsuse H, Kawakami M (Oct 1993). "A new member of the C1s family of complement proteins found in a bactericidal factor, Ra-reactive factor, in human serum". Biochemical and Biophysical Research Communications. 196 (2): 1003–9. doi:10.1006/bbrc.1993.2349. PMID 8240317.

[pmid8018603-2] Sato T, Endo Y, Matsushita M, Fujita T (Apr 1994). "Molecular characterization of a novel serine protease involved in activation of the complement system by mannose-binding protein". International Immunology. 6 (4): 665–9. doi:10.1093/intimm/6.4.665. PMID 8018603.

[entrez-3] "Entrez Gene: mannan-binding lectin serine peptidase 1 (C4/C2 activating component of Ra-reactive factor)".

[pmid10946292-4] Matsushita M, Thiel S, Jensenius JC, Terai I, Fujita T (Sep 2000). "Proteolytic activities of two types of mannose-binding lectin-associated serine protease". Journal of Immunology. 165 (5): 2637–42. doi:10.4049/jimmunol.165.5.2637. PMID 10946292.

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v t e Endopeptidases: serine proteases/serine endopeptidases (EC 3.4.21)
Digestive enzymes	Enteropeptidase Trypsin Chymotrypsin Elastase Neutrophil Pancreatic
Coagulation	factors: Thrombin Factor VIIa Factor IXa Factor Xa Factor XIa Factor XIIa Kallikrein PSA KLK1 KLK2 KLK3 KLK4 KLK5 KLK6 KLK7 KLK8 KLK9 KLK10 KLK11 KLK12 KLK13 KLK14 KLK15 fibrinolysis: Plasmin Plasminogen activator Tissue plasminogen activator Urinary plasminogen activator
Complement system	Factor B Factor D Factor I MASP MASP1 MASP2 C3-convertase
Other immune system	Chymase Granzyme Tryptase Proteinase 3/Myeloblastin
Venombin	Ancrod Batroxobin
Other	Acrosin Prolyl endopeptidase Pronase Proprotein convertases 1 2 Prostasin Reelin Subtilisin/Furin/S1P4 Sedolisin/TPP1 Streptokinase Cathepsin A G

v t e Enzymes
Activity	Active site Binding site Catalytic triad Oxyanion hole Enzyme promiscuity Diffusion-limited enzyme Cofactor Enzyme catalysis
Regulation	Allosteric regulation Cooperativity Enzyme inhibitor Enzyme activator
Classification	EC number Enzyme superfamily Enzyme family List of enzymes
Kinetics	Enzyme kinetics Eadie–Hofstee diagram Hanes–Woolf plot Lineweaver–Burk plot Michaelis–Menten kinetics
Types	EC1 Oxidoreductases (list) EC2 Transferases (list) EC3 Hydrolases (list) EC4 Lyases (list) EC5 Isomerases (list) EC6 Ligases (list) EC7 Translocases (list)

MASP1 (protein)

Function

See also

References

Further reading

External links