* 185261

MATRIX METALLOPROTEINASE 11; MMP11


Alternative titles; symbols

STROMELYSIN III; STMY3


HGNC Approved Gene Symbol: MMP11

Cytogenetic location: 22q11.23     Genomic coordinates (GRCh38): 22:23,772,849-23,784,316 (from NCBI)


TEXT

Description

The family of matrix metalloproteinases appears to be involved in physiologic and pathologic processes associated with extracellular matrix remodeling such as those that occur in embryonic development, tissue repair, and tumor progression (Matrisian, 1990). Stromelysin III is a member of the matrix metalloproteinases gene family (Basset et al., 1990).


Cloning and Expression

Basset et al. (1990) identified the STMY3 gene by differential screening of a human breast cancer cDNA library. STMY3 was overexpressed in the stromal cells of invasive breast carcinomas but not in the stromal cells surrounding benign breast fibroadenomas.


Gene Family

The members of the metalloproteinase (MMP) family can be partitioned into 2 subfamilies, according to their general structure and chromosomal localization. The first group includes the 72-kD (120360) and the 92-kD (120361) type IV collagenases, which are characterized by the presence of a fibronectin-like domain and colocalize on chromosome 16. The second group contains type I collagenase (120355) and stromelysins I and II, which lack the fibronectin-like domain and colocalize on chromosome 11. Based on the comparison of MMP gene structures, the 92-kD type IV collagenase seems to represent the ancient gene from which the other MMP genes evolved by loss of coding sequences (Tryggvason et al., 1990). Because STMY3 is located on chromosome 22, it may be a member of a third MMP subfamily.


Gene Function

Pei and Weiss (1995) identified stromelysin III as the first matrix metalloproteinase that can be processed directly to its enzymatic active form by an obligate intracellular proteolytic event that occurs within the constitutive secretory pathway. Intracellular activation is regulated by an unusual 10-amino acid insert located between the pro- and catalytic-domains of stromelysin III which is encrypted with an arg-X-arg-X-lys-arg recognition motif for the Golgi-associated proteinase, furin (FUR; 136950) (a mammalian homolog of a yeast pheromone convertase). Pei and Weiss (1995) suggested that the furin-stromelysin III processing system could serve as an example of proprotein convertases as potential targets for therapeutic intervention in matrix-destructive disease states.


Mapping

By in situ hybridization, Levy et al. (1992) assigned the STMY3 gene to chromosome 22q. Using a panel of somatic cell hybrids containing different segments of 22q, they demonstrated that the STMY3 gene is in band 22q11.2, in close proximity to the BCR gene (151410). Both STMY1 (185250) and STMY2 (185260) are located on chromosome 11.


Nomenclature

The nomenclature of the matrix metalloproteinases, together with symbols and EC numbers, was provided by Nagase et al. (1992).


REFERENCES

  1. Basset, P., Bellocq, J. P., Wolf, C., Stoll, I., Hutin, P., Limacher, J. M., Podhajcer, O. L., Chenard, M. P., Rio, M. C., Chambon, P. A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. Nature 348: 699-704, 1990. [PubMed: 1701851, related citations] [Full Text]

  2. Levy, A., Zucman, J., Delattre, O., Mattei, M.-G., Rio, M.-C., Basset, P. Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22. Genomics 13: 881-883, 1992. [PubMed: 1639418, related citations] [Full Text]

  3. Matrisian, L. M. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 6: 121-125, 1990. [PubMed: 2132731, related citations] [Full Text]

  4. Nagase, H., Barrett, A. J., Woessner, J. F., Jr. Nomenclature and glossary of the matrix metalloproteinases. Matrix Suppl. 1: 421-424, 1992. [PubMed: 1480083, related citations]

  5. Pei, D., Weiss, S. J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375: 244-247, 1995. [PubMed: 7746327, related citations] [Full Text]

  6. Tryggvason, K., Huhtala, P., Tuuttila, A., Chow, L., Keski-Oja, J., Lohi, J. Structure and expression of type IV collagenase genes. Cell Differ. Dev. 32: 307-312, 1990. [PubMed: 1965956, related citations] [Full Text]


Creation Date:
Victor A. McKusick : 6/29/1992
carol : 06/21/2021
dkim : 10/28/1998
carol : 7/1/1998
psherman : 5/15/1998
mark : 1/5/1996
mark : 6/19/1995
terry : 5/5/1994
carol : 4/11/1994
carol : 4/14/1993
carol : 6/29/1992

* 185261

MATRIX METALLOPROTEINASE 11; MMP11


Alternative titles; symbols

STROMELYSIN III; STMY3


HGNC Approved Gene Symbol: MMP11

Cytogenetic location: 22q11.23     Genomic coordinates (GRCh38): 22:23,772,849-23,784,316 (from NCBI)


TEXT

Description

The family of matrix metalloproteinases appears to be involved in physiologic and pathologic processes associated with extracellular matrix remodeling such as those that occur in embryonic development, tissue repair, and tumor progression (Matrisian, 1990). Stromelysin III is a member of the matrix metalloproteinases gene family (Basset et al., 1990).


Cloning and Expression

Basset et al. (1990) identified the STMY3 gene by differential screening of a human breast cancer cDNA library. STMY3 was overexpressed in the stromal cells of invasive breast carcinomas but not in the stromal cells surrounding benign breast fibroadenomas.


Gene Family

The members of the metalloproteinase (MMP) family can be partitioned into 2 subfamilies, according to their general structure and chromosomal localization. The first group includes the 72-kD (120360) and the 92-kD (120361) type IV collagenases, which are characterized by the presence of a fibronectin-like domain and colocalize on chromosome 16. The second group contains type I collagenase (120355) and stromelysins I and II, which lack the fibronectin-like domain and colocalize on chromosome 11. Based on the comparison of MMP gene structures, the 92-kD type IV collagenase seems to represent the ancient gene from which the other MMP genes evolved by loss of coding sequences (Tryggvason et al., 1990). Because STMY3 is located on chromosome 22, it may be a member of a third MMP subfamily.


Gene Function

Pei and Weiss (1995) identified stromelysin III as the first matrix metalloproteinase that can be processed directly to its enzymatic active form by an obligate intracellular proteolytic event that occurs within the constitutive secretory pathway. Intracellular activation is regulated by an unusual 10-amino acid insert located between the pro- and catalytic-domains of stromelysin III which is encrypted with an arg-X-arg-X-lys-arg recognition motif for the Golgi-associated proteinase, furin (FUR; 136950) (a mammalian homolog of a yeast pheromone convertase). Pei and Weiss (1995) suggested that the furin-stromelysin III processing system could serve as an example of proprotein convertases as potential targets for therapeutic intervention in matrix-destructive disease states.


Mapping

By in situ hybridization, Levy et al. (1992) assigned the STMY3 gene to chromosome 22q. Using a panel of somatic cell hybrids containing different segments of 22q, they demonstrated that the STMY3 gene is in band 22q11.2, in close proximity to the BCR gene (151410). Both STMY1 (185250) and STMY2 (185260) are located on chromosome 11.


Nomenclature

The nomenclature of the matrix metalloproteinases, together with symbols and EC numbers, was provided by Nagase et al. (1992).


REFERENCES

  1. Basset, P., Bellocq, J. P., Wolf, C., Stoll, I., Hutin, P., Limacher, J. M., Podhajcer, O. L., Chenard, M. P., Rio, M. C., Chambon, P. A novel metalloproteinase gene specifically expressed in stromal cells of breast carcinomas. Nature 348: 699-704, 1990. [PubMed: 1701851] [Full Text: https://doi.org/10.1038/348699a0]

  2. Levy, A., Zucman, J., Delattre, O., Mattei, M.-G., Rio, M.-C., Basset, P. Assignment of the human stromelysin 3 (STMY3) gene to the q11.2 region of chromosome 22. Genomics 13: 881-883, 1992. [PubMed: 1639418] [Full Text: https://doi.org/10.1016/0888-7543(92)90175-r]

  3. Matrisian, L. M. Metalloproteinases and their inhibitors in matrix remodeling. Trends Genet. 6: 121-125, 1990. [PubMed: 2132731] [Full Text: https://doi.org/10.1016/0168-9525(90)90126-q]

  4. Nagase, H., Barrett, A. J., Woessner, J. F., Jr. Nomenclature and glossary of the matrix metalloproteinases. Matrix Suppl. 1: 421-424, 1992. [PubMed: 1480083]

  5. Pei, D., Weiss, S. J. Furin-dependent intracellular activation of the human stromelysin-3 zymogen. Nature 375: 244-247, 1995. [PubMed: 7746327] [Full Text: https://doi.org/10.1038/375244a0]

  6. Tryggvason, K., Huhtala, P., Tuuttila, A., Chow, L., Keski-Oja, J., Lohi, J. Structure and expression of type IV collagenase genes. Cell Differ. Dev. 32: 307-312, 1990. [PubMed: 1965956] [Full Text: https://doi.org/10.1016/0922-3371(90)90044-w]


Creation Date:
Victor A. McKusick : 6/29/1992

Edit History:
carol : 06/21/2021
dkim : 10/28/1998
carol : 7/1/1998
psherman : 5/15/1998
mark : 1/5/1996
mark : 6/19/1995
terry : 5/5/1994
carol : 4/11/1994
carol : 4/14/1993
carol : 6/29/1992