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Literature summary for 3.4.24.7 extracted from

  • Xia, W.; Hammerberg, C.; Li, Y.; He, T.; Quan, T.; Voorhees, J.J.; Fisher, G.J.
    Expression of catalytically active matrix metalloproteinase-1 in dermal fibroblasts induces collagen fragmentation and functional alterations that resemble aged human skin (2013), Aging Cell, 12, 661-671.
    View publication on PubMedView publication on EuropePMC

Application

Application Comment Organism
medicine MMP-1-mediated fragmentation of dermal collagen fibrils alters the morphology and function of dermal fibroblasts, linking collagen fibril fragmentation to age-related decline of fibroblast function Homo sapiens

Cloned(Commentary)

Cloned (Comment) Organism
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Homo sapiens

Protein Variants

Protein Variants Comment Organism
V94G constitutively active MMP-1 mutant. Expression of MMP-1 V94G in young skin in organ culture causes fragmentation and ultrastructural alterations of collagen fibrils similar to those observed in aged human skin in vivo. Expression of MMP-1 V94G in dermal fibroblasts cultured in three-dimensional collagen lattices causes substantial collagen fragmentation, which is markedly reduced by MMP-1 siRNA-mediated knockdown or MMP inhibitor MMI270. Fibroblasts cultured in MMP-1 V94G-fragmented collagen lattices display many alterations observed in fibroblasts in aged human skin, including reduced cytoplasmic area, disassembled actin cytoskeleton, impaired TGF-beta pathway, and reduced collagen production Homo sapiens

Organism

Organism UniProt Comment Textmining
Homo sapiens P03956
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Source Tissue

Source Tissue Comment Organism Textmining
fibroblast dermal fibroblast Homo sapiens
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