MMP13
GeneName
MMP13
Summary
MMP13, also known as MMP-13, matrix metalloproteinase 13, or collagenase 3, is a 54 kDa secreted enzyme that is primarily localised to the extracellular matrix and extracellular space. It plays a vital role in the degradation of collagen and other components of the extracellular matrix, contributing to processes such as collagen catabolism, bone mineralization, and bone morphogenesis. MMP13 is involved in endochondral ossification and growth plate cartilage development, and its activity is regulated by calcium and zinc ion binding. Additionally, it has been implicated in the response to amyloid-beta, suggesting a potential role in neurodegenerative conditions.
Importance
MMP13 is relevant to: - Tissue remodelling and repair, particularly in bone and cartilage, due to its role in extracellular matrix disassembly and organisation - Osteoarthritis and rheumatoid arthritis, where it contributes to cartilage degradation - Cancer progression, as matrix metalloproteinases can facilitate tumour invasion and metastasis - Neurodegenerative diseases, given its involvement in the response to amyloid-beta, linking it to Alzheimer’s disease pathology
Top Products
For researchers investigating MMP13, we recommend two excellent primary antibodies that cater to various experimental needs. The first is the well-cited polyclonal antibody, Anti-MMP13 antibody (ab39012), which has garnered 690 citations, highlighting its reliability and trust within the scientific community. This antibody is particularly effective for Western blotting (WB) and ELISA applications. Additionally, we offer the recombinant antibody, Anti-MMP13 antibody [EP1263Y] (ab51072), which is validated for use in Western blotting (WB) as well. With 86 citations, this recombinant product provides the batch-to-batch consistency that many researchers seek. Together, these antibodies represent a robust toolkit for studying MMP13 in various contexts. "The Human MMP13 ELISA Kit (ab221839), supported by 2 citations, is an excellent option for researchers looking to accurately measure MMP13 levels in their samples."
Abcam Product Citation Summary
The data indicates a significant focus on the role of MMP13 in various contexts related to cartilage and joint health, particularly in studies of osteoarthritis and intervertebral disc degeneration. The use of multiple species, including human, rat, and mouse, highlights the translational aspect of this research, aiming to understand MMP13's involvement in ECM degradation, chondrocyte behaviour, and fibrogenic processes.
Abcam Product Citation Table
Domain
The conserved cysteine present in the cysteine-switch motif binds the catalytic zinc ion, thus inhibiting the enzyme. The dissociation of the cysteine from the zinc ion upon the activation-peptide release activates the enzyme (By similarity).
The C-terminal region binds to collagen.
Function
Plays a role in the degradation of extracellular matrix proteins including fibrillar collagen, fibronectin, TNC and ACAN. Cleaves triple helical collagens, including type I, type II and type III collagen, but has the highest activity with soluble type II collagen. Can also degrade collagen type IV, type XIV and type X. May also function by activating or degrading key regulatory proteins, such as TGFB1 and CCN2. Plays a role in wound healing, tissue remodeling, cartilage degradation, bone development, bone mineralization and ossification. Required for normal embryonic bone development and ossification. Plays a role in the healing of bone fractures via endochondral ossification. Plays a role in wound healing, probably by a mechanism that involves proteolytic activation of TGFB1 and degradation of CCN2. Plays a role in keratinocyte migration during wound healing. May play a role in cell migration and in tumor cell invasion.
Involvement in disease
Spondyloepimetaphyseal dysplasia, Missouri type
SEMDM
A bone disease characterized by moderate to severe metaphyseal changes, mild epiphyseal involvement, rhizomelic shortening of the lower limbs with bowing of the femora and/or tibiae, coxa vara, genu varum and pear-shaped vertebrae in childhood. Epimetaphyseal changes improve with age.
None
The disease is caused by variants affecting the gene represented in this entry.
Metaphyseal anadysplasia 1
MANDP1
A bone development disorder characterized by skeletal anomalies that resolve spontaneously with age. Clinical characteristics are evident from the first months of life and include slight shortness of stature and a mild varus deformity of the legs. Patients attain a normal stature in adolescence and show improvement or complete resolution of varus deformity of the legs and rhizomelic micromelia.
None
The disease is caused by variants affecting the gene represented in this entry.
Metaphyseal dysplasia, Spahr type
MDST
An autosomal recessive, rare disease characterized by moderate short stature, mild genua vara, and radiographic signs of metaphyseal dysplasia, but no biochemical signs of rickets.
None
The disease is caused by variants affecting the gene represented in this entry.
Post-translational modifications
The proenzyme is activated by removal of the propeptide; this cleavage can be effected by other matrix metalloproteinases, such as MMP2, MMP3 and MMP14 and may involve several cleavage steps. Cleavage can also be autocatalytic, after partial maturation by another protease or after treatment with 4-aminophenylmercuric acetate (APMA) (in vitro).
N-glycosylated.
Tyrosine phosphorylated by PKDCC/VLK.
Sequence Similarities
Belongs to the peptidase M10A family.
Tissue Specificity
Detected in fetal cartilage and calvaria, in chondrocytes of hypertrophic cartilage in vertebrae and in the dorsal end of ribs undergoing ossification, as well as in osteoblasts and periosteal cells below the inner periosteal region of ossified ribs. Detected in chondrocytes from in joint cartilage that have been treated with TNF and IL1B, but not in untreated chondrocytes. Detected in T lymphocytes. Detected in breast carcinoma tissue.
Cellular localization
- Secreted
- Extracellular space
- Extracellular matrix
- Secreted
Alternative names
Collagenase 3, Matrix metalloproteinase-13, MMP-13, MMP13