MMP1 Gene: Function, Expression, and Role in Disease

MMP1 (matrix metallopeptidase 1) encodes a member of the matrix metalloproteinase (MMP) family of zinc-dependent endopeptidases. The encoded preproprotein is proteolytically processed to generate the mature enzyme, which degrades fibrillar collagens (types I, II, III, VII, VIII, and X) and other extracellular matrix components. MMP1 plays a critical role in tissue remodeling, wound healing, angiogenesis, and tumor invasion. Its expression is induced by various cytokines, growth factors, and cellular stress signals. Dysregulation of MMP1 is implicated in cancer metastasis, arthritis, cardiovascular disease, and fibrotic disorders.

Tissue Expression

Cell Line Expression

Hotspot Mutations

Mutation functional classification

• Matrix Metalloproteinases (MMPs) - REACT_118779

• Degradation of the extracellular matrix - R-HSA-1474228

• Collagen degradation - R-HSA-1442490

• Interleukin-4 and Interleukin-13 signaling - R-HSA-6785807

• TNF signaling pathway - KEGG hsa04668

MMP1 (collagenase-1) is a 52 kDa secreted zinc-dependent endopeptidase composed of a prodomain, a catalytic domain with a zinc-binding motif (HEXXHXXGXXH), and a hemopexin-like C-terminal domain. The prodomain is cleaved by extracellular proteases (e.g., plasmin, trypsin) to yield the active 42 kDa enzyme. MMP1 specifically cleaves triple-helical fibrillar collagens at a single site (Gly775–Ile776 in type I collagen), generating characteristic 3/4 and 1/4 fragments. Its activity is tightly regulated by tissue inhibitors of metalloproteinases (TIMPs). The protein is expressed primarily by fibroblasts, keratinocytes, macrophages, and endothelial cells in response to inflammatory stimuli.