Purification and characterization of an acid metalloproteinase from human articular cartilage.

Azzo, Walid; Woessner, Jeff

doi:10.1016/s0021-9258(19)57234-9

Cited by 55 publications

(1 citation statement)

References 33 publications

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“…Amino acid residues indicated are NH2-termini identified in various forms of MMP-3. This includes tissue collagenase (MMP-1) (Stricklin et al, 1983), MMP-2 (Murphy et al, 1985), MMP-3 (Okada et al, 1988) , neutrophil collagenase (Mallya & Van Wart, 1989), "gelatinases" from neutrophils (Hibbs et al, 1985;Murphy et al, 1989) and macrophages (Hibbs et al, 1987), acid metalloproteinase from cartilage (Azzo & Woessner, 1986), collagen telopeptidase (Nakano & Scott, 1987), the enzyme that degrades one-quarter and three-quarter fragments of type I collagen (Overall & Sodek, 1987), and a low relative molecular mass metalloproteinase from rat uterus (Woessner & Taplin, 1988). Studies on the activation of procollagenase and proMMP-3 suggest that treatment of the zymogens with APMA initiates a molecular perturbation of the precursor zymogens that results in loss of an approximately 12 000 Mx peptide from the NH2-terminal end (Stricklin et al, 1983;Okada et al, 1988).…”

Section: ~Xe)mentioning

confidence: 99%

Stepwise activation mechanisms of the precursor of matrix metalloproteinase 3 (stromelysin) by proteinases and (4-aminophenyl)mercuric acetate

Nagase

Enghild²,

Suzuki³

et al. 1990

Biochemistry

368

217

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The mechanisms of activation of the precursor of human matrix metalloproteinase 3 (proMMP-3/prostromelysin) by proteinases and (4-aminophenyl)mercuric acetate (APMA) were investigated by kinetic and sequence analyses. Incubation of proMMP-3 with neutrophil elastase, plasma kallikrein, plasmin, or chymotrypsin at 37 degrees C resulted in the formation of MMP-3 of Mr = 45,000 by cleaving of the His82-Phe83 bond. Since this bond is unlikely to be cleaved by these proteinases it was postulated that an initial attack of an activator proteinase on proMMP-3 creates an intermediate form, which is then processed to a more stable form of Mr = 45,000. To test this hypothesis proMMP-3 was incubated with these serine proteinases under conditions that minimize the action of MMP-3. This led to the accumulation of major intermediates of Mr = 53,000 and two minor forms of Mr = 49,000 and 47,000. The 53,000 Mr intermediate generated by human neutrophil elastase resulted from cleavage of the Val35-Arg36 whereas plasma kallikrein cleaved the Arg36-Arg37 and Lys38-Asp39 bonds and chymotrypsin the Phe34-Val35 bond, all of which are located near the middle of the propeptide. Conversion of these intermediates to the fully active 45,000 Mr form of MMP-3 resulted from a bimolecular reaction of the intermediates. A similar short-lived intermediate of Mr = 46,000 generated by APMA was a result of the intramolecular cleavage of the Glu68-Val69 bond, and it was then converted to a stable MMP-3 of Mr = 45,000 by a intermolecular reaction of MMP-3. However, MMP-3 failed to activate proMMP-3.(ABSTRACT TRUNCATED AT 250 WORDS)

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