MMP23B
Matrix metallopeptidase 23B | |
---|---|
Identifiers | |
Symbol | ? |
HGNC | 7170 |
OMIM | 605809 |
Other data | |
EC number | 3.4.24.- |
Matrix metallopeptidase 23B (MMP23B) is a member of the matrix metalloproteinase (MMP) family, which is 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.
Structure[edit | edit source]
MMP23B is a unique member of the MMP family due to its distinct structure. Unlike other MMPs, MMP23B lacks a signal peptide and a propeptide domain, which are typically involved in the regulation of MMP activity. Instead, MMP23B contains a type II transmembrane domain, suggesting that it is anchored to the cell membrane. The protein also contains a cysteine array and an immunoglobulin-like domain, which are not found in other MMPs.
Function[edit | edit source]
The precise biological function of MMP23B is not fully understood. However, it is believed to play a role in the regulation of cell proliferation, apoptosis, and differentiation. MMP23B is expressed in a variety of tissues, including the ovary, testis, and placenta, indicating a potential role in reproductive processes.
Clinical Significance[edit | edit source]
Alterations in MMP23B expression have been associated with various pathological conditions. For example, overexpression of MMP23B has been observed in certain types of cancer, suggesting a potential role in tumor progression and metastasis. However, the exact mechanisms by which MMP23B contributes to these processes remain to be elucidated.
Research Directions[edit | edit source]
Current research is focused on understanding the regulatory mechanisms controlling MMP23B expression and activity, as well as its interactions with other proteins and signaling pathways. Studies are also investigating the potential of MMP23B as a therapeutic target in cancer and other diseases.
Also see[edit | edit source]
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Contributors: Prab R. Tumpati, MD