Reactome | Elastin degradation by elastin-degrading extracellular proteinases

Elastin degradation by elastin-degrading extracellular proteinases

Stable Identifier

R-HSA-1566962

Type

Reaction [transition]

Species

Homo sapiens

Compartment

extracellular region

ReviewStatus

5/5

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Elastin degradation by elastin-degrading extracellular proteinases

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The elastin component of elastic fibres is degraded to soluble fragments by MMP2 (Murphy et al. 1991), MMP7 (Quantin et al. 1989, Murphy et al. 1991), MMP9 (Murphy et al. 1991, Katsuda et al. 1994) and MMP12 (macrophage elastase) (Shapiro et al. 1993, Taddese et al. 2008), and to a limited extent by MMP3 and 10 (Murphy et al. 1991). In addition, elastin is a substrate for neutrophil elastase (Reilly & Travis 1980).
Eighty-nine tropoelastin cleavage sites were identified for MMP-12, whereas MMP-7 and MMP-9 were found to cleave at only 58 and 63 sites, respectively (Heinz et al. 2010).

Literature References

PubMed ID	Title	Journal	Year
1649600	Matrix metalloproteinase degradation of elastin, type IV collagen and proteoglycan. A quantitative comparison of the activities of 95 kDa and 72 kDa gelatinases, stromelysins-1 and -2 and punctuated metalloproteinase (PUMP) Docherty, AJ, Ward, RV, Cockett, MI, Murphy, G	Biochem J	1991
8226919	Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages Kobayashi, DK, Ley, TJ, Shapiro, SD	J Biol Chem	1993