* 618101

MATRIX METALLOPROTEINASE 27; MMP27


HGNC Approved Gene Symbol: MMP27

Cytogenetic location: 11q22.2     Genomic coordinates (GRCh38): 11:102,691,487-102,705,769 (from NCBI)


TEXT

Description

Matrix metalloproteinases (MMPs), such as MMP27, are key enzymes involved in extracellular matrix remodeling. MMP27 is expressed in a subset of endometrial macrophages related to mestruation (Cominelli et al., 2014).


Cloning and Expression

Cominelli et al. (2014) reported that the 513-amino acid human MMP27 protein contains canonical domains shared by most MMPs: an N-terminal signal peptide targeting translocation into the endoplasmic reticulum (ER); a propeptide containing the cysteine-switch motif responsible for zymogen inactivation; a catalytic domain containing the typical metzincin motif; a proline-rich hinge region; and a hemopexin (HPX; 142290)-like domain. In addition, human MMP27 contains a unique C-terminal extension (CTE). Western blot, colocalization, and gradient analyses revealed that MMP27 was not secreted, but was instead retained in the ER.

Cominelli et al. (2014) investigated expression and localization of MMP27 in cycling human endometrium and found that MMP27 was maximally expressed during the menstrual phase. Immunofluorescence analysis revealed that MMP27 was expressed by CD163 (605545)-positive/CD206 (MRC1; 153618)-positive M2 macrophages during menstruation. MMP27 was present in ovarian and peritoneal, but not rectovaginal, endometriosis.


Gene Function

By mutation analysis, Cominelli et al. (2014) demonstrated that the CTE of human MMP27 was responsible and sufficient for localization of MMP27 in the ER. Further analysis showed that the CTE was not a transmembrane domain and did not confer stable membrane anchorage for MMP27.


Mapping

Gross (2018) mapped the MMP27 gene to chromosome 11q22.2 based on an alignment of the MMP27 sequence (GenBank AF195192) with the genomic sequence (GRCh38).


REFERENCES

  1. Cominelli, A., Gaide Chevronnay, H. P., Lemoine, P., Courtoy, P. J., Marbaix, E., Henriet, P. Matrix metalloproteinase-27 is expressed in CD163+/CD206+ M2 macrophages in the cycling human endometrium and in superficial endometriotic lesions. Molec. Hum. Reprod. 20: 767-775, 2014. [PubMed: 24810263, related citations] [Full Text]

  2. Cominelli, A., Halbout, M., N'Kuli, F., Lemoine, P., Courtoy, P. J., Marbaix, E., Tyteca, D., Henriet, P. A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum. Traffic 15: 401-417, 2014. [PubMed: 24548619, related citations] [Full Text]

  3. Gross, M. B. Personal Communication. Baltimore, Md. 8/28/2018.


Contributors:
Matthew B. Gross - updated : 08/28/2018
Creation Date:
Bao Lige : 08/28/2018
Edit History:
mgross : 08/28/2018

* 618101

MATRIX METALLOPROTEINASE 27; MMP27


HGNC Approved Gene Symbol: MMP27

Cytogenetic location: 11q22.2     Genomic coordinates (GRCh38): 11:102,691,487-102,705,769 (from NCBI)


TEXT

Description

Matrix metalloproteinases (MMPs), such as MMP27, are key enzymes involved in extracellular matrix remodeling. MMP27 is expressed in a subset of endometrial macrophages related to mestruation (Cominelli et al., 2014).


Cloning and Expression

Cominelli et al. (2014) reported that the 513-amino acid human MMP27 protein contains canonical domains shared by most MMPs: an N-terminal signal peptide targeting translocation into the endoplasmic reticulum (ER); a propeptide containing the cysteine-switch motif responsible for zymogen inactivation; a catalytic domain containing the typical metzincin motif; a proline-rich hinge region; and a hemopexin (HPX; 142290)-like domain. In addition, human MMP27 contains a unique C-terminal extension (CTE). Western blot, colocalization, and gradient analyses revealed that MMP27 was not secreted, but was instead retained in the ER.

Cominelli et al. (2014) investigated expression and localization of MMP27 in cycling human endometrium and found that MMP27 was maximally expressed during the menstrual phase. Immunofluorescence analysis revealed that MMP27 was expressed by CD163 (605545)-positive/CD206 (MRC1; 153618)-positive M2 macrophages during menstruation. MMP27 was present in ovarian and peritoneal, but not rectovaginal, endometriosis.


Gene Function

By mutation analysis, Cominelli et al. (2014) demonstrated that the CTE of human MMP27 was responsible and sufficient for localization of MMP27 in the ER. Further analysis showed that the CTE was not a transmembrane domain and did not confer stable membrane anchorage for MMP27.


Mapping

Gross (2018) mapped the MMP27 gene to chromosome 11q22.2 based on an alignment of the MMP27 sequence (GenBank AF195192) with the genomic sequence (GRCh38).


REFERENCES

  1. Cominelli, A., Gaide Chevronnay, H. P., Lemoine, P., Courtoy, P. J., Marbaix, E., Henriet, P. Matrix metalloproteinase-27 is expressed in CD163+/CD206+ M2 macrophages in the cycling human endometrium and in superficial endometriotic lesions. Molec. Hum. Reprod. 20: 767-775, 2014. [PubMed: 24810263] [Full Text: https://doi.org/10.1093/molehr/gau034]

  2. Cominelli, A., Halbout, M., N'Kuli, F., Lemoine, P., Courtoy, P. J., Marbaix, E., Tyteca, D., Henriet, P. A unique C-terminal domain allows retention of matrix metalloproteinase-27 in the endoplasmic reticulum. Traffic 15: 401-417, 2014. [PubMed: 24548619] [Full Text: https://doi.org/10.1111/tra.12149]

  3. Gross, M. B. Personal Communication. Baltimore, Md. 8/28/2018.


Contributors:
Matthew B. Gross - updated : 08/28/2018

Creation Date:
Bao Lige : 08/28/2018

Edit History:
mgross : 08/28/2018