Human MPO Instant ELISA

Description: The human MPO Instant ELISA is an enzyme-linked immunosorbent assay for the quantitative detection of human Myeloperoxidase. The human MPO Instant ELISA is for research use only. Not for diagnostic or therapeutic procedures.

Myeloperoxidase is a human enzyme in the azurophilic granules of neutrophils and in the lysosomes of monocytes. Its major role is to aid in microbial killing.

MPO is a dimeric molecule, consisting of a pair of heavy- and light-chain protomers and 2 iron atoms. MPO has only 1 gene; thus, the mature enzyme is synthesized from a single polypeptide product. The synthesis of MPO primarily occurs during the promyelocytic stage of myeloid development, concurrent with development of the azurophilic granules. The MPO gene encodes for a primary translational product, which is glycosylated to yield an enzymatically inactive precursor, apopro-MPO. Heme is then inserted, yielding the enzymatically active precursor, pro-MPO.
MPO is found in the azurophilic granules of neutrophilic polymorphonuclear leukocytes (PMNs) and in the lysosomes of monocytes in humans. MPO is most abundant in the granules of neutrophils. Monocytes contain only about a third of the MPO present in neutrophils.

Normal function of myeloperoxidase:
When neutrophils become activated in conjunction with phagocytosis, they undergo a process referred to as a respiratory burst. This respiratory burst causes production of superoxide, hydrogen peroxide, and other reactive oxygen derivatives, which are all toxic to microbes. During respiratory bursts, granule contents are released into the phagolysosomes and outside the cell, allowing released contents to come into contact with any microbes present. MPO catalyzes the conversion of hydrogen peroxide and chloride ions (Cl) into hypochlorous acid. Hypochlorous acid is 50 times more potent in microbial killing than hydrogen peroxide.
MPO may have a role in atherosclerosis, carcinogenesis, and degenerative neurological diseases. The role of MPO in atherosclerosis is supported by the fact that MPO deficiency may protect against cardiovascular disease.
MPO deficiency is associated with a huge number of disorders.

Citations: Rautelin,H.I.; Oksanen,A.M.; Veijola,L.I.; Sipponen,P.I.; Tervahartiala,T.I.; Sorsa,T.A.; Lauhio,A.. Enhanced systemic matrix metalloproteinase response in Helicobacter pylori gastritis. Ann Med 2009;41:208-215. (Link)

References: Milla,C.; Yang,S.; Cornfield,D.N.; Brennan,M.L.; Hazen,S.L.; Panoskaltsis-Mortari,A.; Blazar,B.R.; Haddad,I.Y.. Myeloperoxidase deficiency enhances inflammation after allogeneic marrow transplantation. Am.J.Physiol Lung Cell Mol.Physiol 2004;287:L706-L714. (Link)

Nauseef,W.M.. Quality control in the endoplasmic reticulum: lessons from hereditary myeloperoxidase deficiency. J.Lab Clin.Med. 1999;134:215-221. (Link)

Marchetti,C.; Patriarca,P.; Solero,G.P.; Baralle,F.E.; Romano,M.. Genetic studies on myeloperoxidase deficiency in Italy. Jpn.J.Infect.Dis. 2004;57:S10-S12. (Link)

Nauseef,W.M.. Insights into myeloperoxidase biosynthesis from its inherited deficiency. J.Mol.Med. 1998;76:661-668. (Link)

Marchetti,C.; Patriarca,P.; Solero,G.P.; Baralle,F.E.; Romano,M.. Genetic characterization of myeloperoxidase deficiency in Italy. Hum.Mutat. 2004;23:496-505. (Link)

Nauseef,W.M.. Myeloperoxidase deficiency. Hematol.Oncol.Clin.North Am. 1988;2:135-158. (Link)

Kutter,D.; Devaquet,P.; Vanderstocken,G.; Paulus,J.M.; Marchal,V.; Gothot,A.. Consequences of total and subtotal myeloperoxidase deficiency: risk or benefit ? 73. Acta Haematol. 2000;104:10-15. (Link)

Nauseef,W.M.; Cogley,M.; Bock,S.; Petrides,P.E.. Pattern of inheritance in hereditary myeloperoxidase deficiency associated with the R569W missense mutation. J.Leukoc.Biol. 1998;63:264-269. (Link)

DeLeo,F.R.; Goedken,M.; McCormick,S.J.; Nauseef,W.M.. A novel form of hereditary myeloperoxidase deficiency linked to endoplasmic reticulum/proteasome degradation. J.Clin.Invest 1998;101:2900-2909. (Link)

Kutter,D.. Prevalence of myeloperoxidase deficiency: population studies using Bayer-Technicon automated hematology. J.Mol.Med. 1998;76:669-675. (Link)