Fibrillin-1 degradation by MMP3, CTSK, CTSL2

Stable Identifier
R-HSA-2514772
Type
Reaction [transition]
Species
Homo sapiens
Compartment
extracellular region
ReviewStatus
5/5
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Fibrillin-1 degradation by MMP3, CTSK, CTSL2
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Fibrillin-1 can be degraded by MMP3 (Ashworth et al. 1999) and cathepsins K and L2 (V) (Kirschner et al. 2011).
Literature References
PubMed ID Title Journal Year
10229672 Fibrillin degradation by matrix metalloproteinases: implications for connective tissue remodelling

Shuttleworth, CA, Murphy, G, Sherratt, MJ, Kielty, CM, Ashworth, JL, Rock, MJ, Shapiro, SD

Biochem. J. 1999
21784848 Classical and neonatal Marfan syndrome mutations in fibrillin-1 cause differential protease susceptibilities and protein function

Brömme, D, Hubmacher, D, Fagotto-Kaufmann, C, Kaur, J, Iyengar, G, Bartels, R, Kirschner, R, Reinhardt, DP

J. Biol. Chem. 2011
Participants
Input
Output
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as an event of
Catalyst Activity

serine-type endopeptidase activity of MMP3, CTSK, CTSL2 [extracellular region]

Physical Entity
MMP3, CTSK, CTSL2 [extracellular region] (Homo sapiens)
Activity
serine-type endopeptidase activity (GO:0004252)
Orthologous Events
Fibrillin-1 degradation by MMP3, CTSK, CTSL2 (Bos taurus)
Fibrillin-1 degradation by MMP3, CTSK, CTSL2 (Canis familiaris)
Fibrillin-1 degradation by MMP3, CTSK, CTSL2 (Danio rerio)
Fibrillin-1 degradation by MMP3, CTSK, CTSL2 (Dictyostelium discoideum)
Fibrillin-1 degradation by MMP3, CTSK, CTSL2 (Gallus gallus)
Fibrillin-1 degradation by MMP3, CTSK, CTSL2 (Mus musculus)
Fibrillin-1 degradation by MMP3, CTSK, CTSL2 (Rattus norvegicus)
Authored
Jupe, S  (2012-08-08)
Reviewed
Ricard-Blum, S  (2013-08-13)
Created
Jupe, S  (2012-10-10)
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