MMP-13 , luusto ja nivelrusto
https://www.ncbi.nlm.nih.gov/gene/4322
MMP13 matrix metallopeptidase 13 [ Homo sapiens (human)
]
Gene ID: 4322, updated on
31-Dec-2017
- Official
Symbol
- MMP13provided by HGNC
- Official
Full Name
- matrix metallopeptidase 13provided by HGNC
- Primary source
- HGNC:HGNC:7159
- See related
- Ensembl:ENSG00000137745
MIM:600108;
Vega:OTTHUMG00000165850
- Gene type
- protein coding
- RefSeq status
- REVIEWED
- Organism
- Homo sapiens
- Also known as
- CLG3; MDST; MANDP1; MMP-13
- Summary
- This gene encodes a member of the peptidase M10 family of
matrix metalloproteinases (MMPs). Proteins in this family are involved
in the breakdown of extracellular matrix in normal physiological
processes, such as embryonic development, reproduction, and tissue
remodeling, as well as in disease processes, such as arthritis and
metastasis. The encoded preproprotein is proteolytically processed to
generate the mature protease. This protease cleaves type II collagen
more efficiently than types I and III. It may be involved in articular
cartilage turnover and cartilage pathophysiology associated with
osteoarthritis. Mutations in this gene are associated with metaphyseal
anadysplasia. This gene is part of a cluster of MMP genes on chromosome
11. [provided by RefSeq, Jan 2016]
- Expression
- Low expression observed in reference dataset See more
- Orthologs
- mouse
all
- Mitä kirjallisuutta tästä MMP-13.asta on kertynyt?
Related articles in PubMed
-
Matrix
Metalloproteinase-13 - A Potential Biomarker for Detection and
Prognostic Assessment of Patients with Esophageal Squamous Cell
Carcinoma.
Sedighi M, et al. Asian Pac J Cancer Prev, 2016. PMID 27356690
-
Hyaluronic
Acid Suppresses the Expression of Metalloproteinases in Osteoarthritic
Cartilage Stimulated Simultaneously by Interleukin 1β and Mechanical
Load.
Pohlig F, et al. PLoS One, 2016. PMID 26934732, Free PMC Article
-
Induction
of the Matrix Metalloproteinase 13 Gene in Bronchial Epithelial Cells
by Interferon and Identification of its Novel Functional Polymorphism.
Mashimo Y, et al. Inflammation, 2016 Jun. PMID 26635116
-
Function
of sustained released resveratrol on IL-1β-induced hBMSC MMP13
secretion inhibition and chondrogenic differentiation promotion.
Wu G, et al. J Biomater Appl, 2016 Feb. PMID 26526931
-
Modified platelet deposition on matrix metalloproteinase 13 digested collagen I.
Howes JM, et al. J Thromb Haemost, 2015 Dec. PMID 26447617, Free PMC Article
GeneRIFs: Gene References Into FunctionsWhat's a GeneRIF?
-
TGF-beta1
stimulates the phosphorylation of Runx2 at three serine amino acids,
and this event is required for MMP-13 expression in osteoblastic cells.
-
IL-6-stimulated
MMP-13 expression was independent of IL-1beta stimulation and was
blocked by SAHA, suggesting that SAHA inhibits IL-6 signaling in
Osteoarthritis (OA) chondrocytes.
-
High MMP13 expression is associated with intervertebral disc degeneration.
-
data
demonstrate that MMP-13 is critical for the development of osteolytic
lesions in Multiple myeloma and that targeting the MMP-13 protein -
rather than its catalytic activity - constitutes a potential approach to
mitigating bone disease in affected patients.
-
Endoplasmic
reticulum stress participates in the progress of senescence and
apoptosis of osteoarthritic chondrocytes, which manifested in increased
expression of ADAMTS5, MMP13, and decreased COL2A1 expression.
-
Matrix
metalloprotease (MMP) regulation was the top pathway involved in
gingival aging. MMP3, MMP9, MMP12, and MMP13 were upregulated in old
gingival tissues, concomitantly with interleukin-1 beta (IL1B)
expression.
-
these findings support roles for both cFOS (indirect) and ATF3 (direct) in effecting MMP13 transcription in human chondrocytes.
-
Oxytocin prevents cartilage matrix destruction via regulating MMP1 and MMP13.
-
These
studies have uncovered a new, ATP6V1H-mediated pathway that regulates
bone formation, and defines a new mechanism of disease that leads to
bone loss. We propose that MMP9/MMP13 could be therapeutic targets for
patients with this rare genetic disease.
-
To
conclude, Pseudomonas aeruginosa infection induced the expression of
matrix metalloproteinases, and Pseudomonas aer
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