Bioinformatics Database
MMP9: Matrix metallopeptidase 9
Cellular Process
Cap stage of tooth development
Gene Name
MMP9: Matrix metallopeptidase 9
Gene ID
4318
Gene Sequence
General Description
Proteins of the matrix metalloproteinase (MMP) 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. Most MMP's are secreted as inactive proproteins which are activated when cleaved by extracellular proteinases. The enzyme encoded by this gene degrades type IV and V collagens. Studies in rhesus monkeys suggest that the enzyme is involved in IL-8-induced mobilization of hematopoietic progenitor cells from bone marrow, and murine studies suggest a role in tumor-associated tissue remodeling.
Alternative titles; symbols
COLLAGENASE TYPE IV-B; CLG4B COLLAGENASE TYPE IV, 92-KD COLLAGENASE TYPE V GELATINASE, 92-KD GELATINASE B; GELB
Chromosome
Chromosome 20
Cytogenetic location
20q13.12
Encoded Protein
Matrix metalloproteinase-9 preproprotein
Function of the protein in oral and tooth development
To investigate the functional role played by extracellular matrix metalloproteinase inducer (EMMPRIN) in tooth germ development, Xie et al., (2010) used EMMPRIN siRNA interference in cultured mouse mandibles at embryonic day 11. The results showed that EMMPRIN siRNA-treated explants exhibited a marked growth inhibition of tooth germ compared to the control. A significant reduction in MMP-2, MMP-3, MMP-9, MMP-13 and MT2-MMP mRNA expression were also observed in the mouse mandibles. This findings indicate that EMMPRIN is involved in the early stage of tooth germ development and morphogenesis, possibly by regulating the expression of MMP genes (Xie et al., 2010).
Dental and Oral Diseases
Protein Sequence
>NP_004985.2 matrix metalloproteinase-9 preproprotein [Homo sapiens]
MSLWQPLVLVLLVLGCCFAAPRQRQSTLVLFPGDLRTNLTDRQLAEEYLYRYGYTRVAEMRGESKSLGPA
LLLLQKQLSLPETGELDSATLKAMRTPRCGVPDLGRFQTFEGDLKWHHHNITYWIQNYSEDLPRAVIDDA
FARAFALWSAVTPLTFTRVYSRDADIVIQFGVAEHGDGYPFDGKDGLLAHAFPPGPGIQGDAHFDDDELW
SLGKGVVVPTRFGNADGAACHFPFIFEGRSYSACTTDGRSDGLPWCSTTANYDTDDRFGFCPSERLYTQD
GNADGKPCQFPFIFQGQSYSACTTDGRSDGYRWCATTANYDRDKLFGFCPTRADSTVMGGNSAGELCVFP
FTFLGKEYSTCTSEGRGDGRLWCATTSNFDSDKKWGFCPDQGYSLFLVAAHEFGHALGLDHSSVPEALMY
PMYRFTEGPPLHKDDVNGIRHLYGPRPEPEPRPPTTTTPQPTAPPTVCPTGPPTVHPSERPTAGPTGPPS
AGPTGPPTAGPSTATTVPLSPVDDACNVNIFDAIAEIGNQLYLFKDGKYWRFSEGRGSRPQGPFLIADKW
PALPRKLDSVFEERLSKKLFFFSGRQVWVYTGASVLGPRRLDKLGLGADVAQVTGALRSGRGKMLLFSGR
RLWRFDVKAQMVDPRSASEVDRMFPGVPLDTHDVFQYREKAYFCQDRFYWRVSSRSELNQVDQVGYVTYD
ILQCPED
Mutations
Related Literature
Xie et al., (2010). https://doi.org/10.1007/s00418-010-0697-7
