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Myeloblastin (EC 3.4.21.76, leukocyte proteinase 3, leukocyte proteinase 4, proteinase PR-3, proteinase-3, PMNL proteinase) is an enzyme. This enzyme catalyses the following chemical reaction: Hydrolysis of proteins, including elastin, by preferential cleavage: -Ala- > -Val-

This enzyme is present in polymorphonuclear leukocyte granules. Downregulation of myeloblastin in promyelocytic leukemia cells was shown to induce their growth arrest and differentiation.

See also

• Proteinase 3

References

1. Martin KR, Witko-Sarsat V (September 2017). "Proteinase 3: the odd one out that became an autoantigen". Journal of Leukocyte Biology. 102 (3): 689–698. doi:10.1189/jlb.3MR0217-069R. PMID 28546501.
2. Brubaker MJ, Groutas WC, Hoidal JR, Rao NV (November 1992). "Human neutrophil proteinase 3: mapping of the substrate binding site using peptidyl thiobenzyl esters". Biochemical and Biophysical Research Communications. 188 (3): 1318–24. doi:10.1016/0006-291x(92)91375-z. PMID 1445363.
3. Kam CM, Kerrigan JE, Dolman KM, Goldschmeding R, Von dem Borne AE, Powers JC (February 1992). "Substrate and inhibitor studies on proteinase 3". FEBS Letters. 297 (1–2): 119–23. doi:10.1016/0014-5793(92)80340-m. PMID 1551417.
4. Bories D, Raynal MC, Solomon DH, Darzynkiewicz Z, Cayre YE (December 1989). "Down-regulation of a serine protease, myeloblastin, causes growth arrest and differentiation of promyelocytic leukemia cells". Cell. 59 (6): 959–68. doi:10.1016/0092-8674(89)90752-6. PMID 2598267.

External links

• Myeloblastin at the U.S. National Library of Medicine Medical Subject Headings (MeSH)

• Biology

• EC 3.4.21