Matrix metallopeptidase 12: Difference between revisions

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{{enzyme
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| Name = macrophage elastase
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| EC_number = 3.4.24.65
| require_manual_inspection = no
| CAS_number = 146888-86-0
| update_protein_box = yes
| IUBMB_EC_number = 3/4/24/65
| update_summary = yes
| GO_code = 0004234
| update_citations = yes
| image =
| width =
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{{Infobox_gene}}


<!-- The GNF_Protein_box is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
'''Matrix metalloproteinase-12''' (MMP-12) also known as '''macrophage metalloelastase''' (MME) or '''macrophage elastase''' (ME) is an [[enzyme]] that in humans is encoded by the ''MMP12'' [[gene]].<ref name="entrez"/><ref name="pmid8226919">{{cite journal | vauthors = Shapiro SD, Kobayashi DK, Ley TJ | title = Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages | journal = J. Biol. Chem. | volume = 268 | issue = 32 | pages = 23824–9 |date=November 1993 | pmid = 8226919 | doi = | url =  }}</ref><ref name="pmid7782320">{{cite journal | vauthors = Belaaouaj A, Shipley JM, Kobayashi DK, Zimonjic DB, Popescu N, Silverman GA, Shapiro SD | title = Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression | journal = J. Biol. Chem. | volume = 270 | issue = 24 | pages = 14568–75 |date=June 1995 | pmid = 7782320 | doi = 10.1074/jbc.270.24.14568| url = }}</ref>
{{GNF_Protein_box
 
| image = PBB_Protein_MMP12_image.jpg
== Function ==
| image_source = [[Protein_Data_Bank|PDB]] rendering based on 1jiz.
 
| PDB = {{PDB2|1jiz}}, {{PDB2|1jk3}}, {{PDB2|1os2}}, {{PDB2|1os9}}, {{PDB2|1rmz}}, {{PDB2|1ros}}, {{PDB2|1utt}}, {{PDB2|1utz}}, {{PDB2|1y93}}, {{PDB2|1ycm}}, {{PDB2|1z3j}}, {{PDB2|2hu6}}, {{PDB2|2oxu}}, {{PDB2|2oxw}}, {{PDB2|2oxz}}
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. The prodomain is cleaved by extracellular proteinases when the enzyme is activated. The active enzyme is constituted by two domains, the catalytic domain resposnsible for its enzymatic activity and the hemopexin-like domain that in some MMPs plays a role in substrate recognition and can contribute to increasing catalytic efficiency. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble [[elastin]]. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.<ref name="entrez">{{cite web | title = Entrez Gene: MMP12 matrix metallopeptidase 12 (macrophage elastase)| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4321| accessdate = }}</ref>
| Name = Matrix metallopeptidase 12 (macrophage elastase)
 
| HGNCid = 7158
== Clinical significance ==
| Symbol = MMP12
 
| AltSymbols =; MME; HME; MGC138506
MMP12 may play a role in [[aneurysm]] formation<ref name="pmid9835614">{{cite journal | vauthors = Curci JA, Liao S, Huffman MD, Shapiro SD, Thompson RW | title = Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms | journal = J. Clin. Invest. | volume = 102 | issue = 11 | pages = 1900–10 |date=December 1998 | pmid = 9835614 | pmc = 509141 | doi = 10.1172/JCI2182 | url =  }}</ref> and studies in mice and humans suggest a role in the development of [[emphysema]].<ref name="pmid16166618">{{cite journal | vauthors = Woodruff PG, Koth LL, Yang YH, Rodriguez MW, Favoreto S, Dolganov GM, Paquet AC, Erle DJ | title = A Distinctive Alveolar Macrophage Activation State Induced by Cigarette Smoking | journal = Am. J. Respir. Crit. Care Med. | volume = 172 | issue = 11 | pages = 1383–92 |date=December 2005 | pmid = 16166618 | pmc = 2718436 | doi = 10.1164/rccm.200505-686OC | url =  }}</ref>
| OMIM = 601046
| ECnumber =
| Homologene = 20547
| MGIid = 97005
| GeneAtlas_image1 = PBB_GE_MMP12_204580_at_tn.png
  | Function = {{GNF_GO|id=GO:0004234 |text = macrophage elastase activity}} {{GNF_GO|id=GO:0005509 |text = calcium ion binding}} {{GNF_GO|id=GO:0008270 |text = zinc ion binding}}
| Component = {{GNF_GO|id=GO:0005578 |text = proteinaceous extracellular matrix}}
| Process = {{GNF_GO|id=GO:0000270 |text = peptidoglycan metabolic process}} {{GNF_GO|id=GO:0006508 |text = proteolysis}} {{GNF_GO|id=GO:0006928 |text = cell motility}}  
| Orthologs = {{GNF_Ortholog_box
    | Hs_EntrezGene = 4321
    | Hs_Ensembl = ENSG00000110347
    | Hs_RefseqProtein = NP_002417
    | Hs_RefseqmRNA = NM_002426
    | Hs_GenLoc_db = 
    | Hs_GenLoc_chr = 11
    | Hs_GenLoc_start = 102238686
    | Hs_GenLoc_end = 102250922
    | Hs_Uniprot = P39900
    | Mm_EntrezGene = 17381
    | Mm_Ensembl = ENSMUSG00000049723
    | Mm_RefseqmRNA = NM_008605
    | Mm_RefseqProtein = NP_032631
    | Mm_GenLoc_db = 
    | Mm_GenLoc_chr = 9
    | Mm_GenLoc_start = 7347406
    | Mm_GenLoc_end = 7369499
    | Mm_Uniprot = Q3TB28
  }}
}}
'''Matrix metallopeptidase 12 (macrophage elastase)''', also known as '''MMP12''', is a human [[gene]].<ref name="entrez">{{cite web | title = Entrez Gene: MMP12 matrix metallopeptidase 12 (macrophage elastase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4321| accessdate = }}</ref>


<!-- The PBB_Summary template is automatically maintained by Protein Box Bot.  See Template:PBB_Controls to Stop updates. -->
== References ==
{{PBB_Summary
{{reflist}}
| section_title =  
| summary_text = 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. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. It may play a role in aneurysm formation and studies in mice suggest a role in the development of emphysema. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.<ref name="entrez">{{cite web | title = Entrez Gene: MMP12 matrix metallopeptidase 12 (macrophage elastase)| url = http://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=4321| accessdate = }}</ref>
}}


==References==
== Further reading ==
{{reflist|2}}
==Further reading==
{{refbegin | 2}}
{{refbegin | 2}}
{{PBB_Further_reading  
{{PBB_Further_reading
| citations =  
| citations =
*{{cite journal  | author=Nagase H, Woessner JF |title=Matrix metalloproteinases. |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491-4 |year= 1999 |pmid= 10419448 |doi=  }}
*{{cite journal  | vauthors=Nagase H, Woessner JF |title=Matrix metalloproteinases |journal=J. Biol. Chem. |volume=274 |issue= 31 |pages= 21491–4 |year= 1999 |pmid= 10419448 |doi=10.1074/jbc.274.31.21491 }}
*{{cite journal | author=Belaaouaj A, Shipley JM, Kobayashi DK, ''et al.'' |title=Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression. |journal=J. Biol. Chem. |volume=270 |issue= 24 |pages= 14568-75 |year= 1995 |pmid= 7782320 |doi=  }}
*{{cite journal   |vauthors=Pendás AM, Santamaría I, Alvarez MV |title=Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3 |journal=Genomics |volume=37 |issue= 2 |pages= 266–8 |year= 1997 |pmid= 8921407 |doi=10.1006/geno.1996.0557 }}
*{{cite journal | author=Shapiro SD, Kobayashi DK, Ley TJ |title=Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages. |journal=J. Biol. Chem. |volume=268 |issue= 32 |pages= 23824-9 |year= 1993 |pmid= 8226919 |doi= }}
*{{cite journal   |vauthors=Gronski TJ, Martin RL, Kobayashi DK |title=Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 12189–94 |year= 1997 |pmid= 9115292 |doi=10.1074/jbc.272.18.12189  }}
*{{cite journal  | author=Pendás AM, Santamaría I, Alvarez MV, ''et al.'' |title=Fine physical mapping of the human matrix metalloproteinase genes clustered on chromosome 11q22.3. |journal=Genomics |volume=37 |issue= 2 |pages= 266-8 |year= 1997 |pmid= 8921407 |doi=  }}
*{{cite journal  | vauthors=Edelstein C, Shapiro SD, Klezovitch O, Scanu AM |title=Macrophage metalloelastase, MMP-12, cleaves human apolipoprotein(a) in the linker region between kringles IV-4 and IV-5. Potential relevance to lipoprotein(a) biology |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10019–23 |year= 1999 |pmid= 10187779 |doi=10.1074/jbc.274.15.10019 }}
*{{cite journal | author=Gronski TJ, Martin RL, Kobayashi DK, ''et al.'' |title=Hydrolysis of a broad spectrum of extracellular matrix proteins by human macrophage elastase. |journal=J. Biol. Chem. |volume=272 |issue= 18 |pages= 12189-94 |year= 1997 |pmid= 9115292 |doi= }}
*{{cite journal   |vauthors=Dias Neto E, Correa RG, Verjovski-Almeida S |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491–6 |year= 2000 |pmid= 10737800 |doi=10.1073/pnas.97.7.3491  | pmc=16267  }}
*{{cite journal | author=Edelstein C, Shapiro SD, Klezovitch O, Scanu AM |title=Macrophage metalloelastase, MMP-12, cleaves human apolipoprotein(a) in the linker region between kringles IV-4 and IV-5. Potential relevance to lipoprotein(a) biology. |journal=J. Biol. Chem. |volume=274 |issue= 15 |pages= 10019-23 |year= 1999 |pmid= 10187779 |doi= }}
*{{cite journal   |vauthors=Wert SE, Yoshida M, LeVine AM |title=Increased metalloproteinase activity, oxidant production and emphysema in surfactant protein D gene-inactivated mice |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 11 |pages= 5972–7 |year= 2000 |pmid= 10801980 |doi= 10.1073/pnas.100448997  | pmc=18543 }}
*{{cite journal | author=Dias Neto E, Correa RG, Verjovski-Almeida S, ''et al.'' |title=Shotgun sequencing of the human transcriptome with ORF expressed sequence tags. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 7 |pages= 3491-6 |year= 2000 |pmid= 10737800 |doi= }}
*{{cite journal   |vauthors=Belaaouaj AA, Li A, Wun TC |title=Matrix metalloproteinases cleave tissue factor pathway inhibitor. Effects on coagulation |journal=J. Biol. Chem. |volume=275 |issue= 35 |pages= 27123–8 |year= 2000 |pmid= 10859319 |doi= 10.1074/jbc.M004218200 }}
*{{cite journal | author=Wert SE, Yoshida M, LeVine AM, ''et al.'' |title=Increased metalloproteinase activity, oxidant production, and emphysema in surfactant protein D gene-inactivated mice. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=97 |issue= 11 |pages= 5972-7 |year= 2000 |pmid= 10801980 |doi= 10.1073/pnas.100448997 }}
*{{cite journal   |vauthors=Hiller O, Lichte A, Oberpichler A, etal |title=Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 33008–13 |year= 2000 |pmid= 10930399 |doi= 10.1074/jbc.M001836200 }}
*{{cite journal  | author=Belaaouaj AA, Li A, Wun TC, ''et al.'' |title=Matrix metalloproteinases cleave tissue factor pathway inhibitor. Effects on coagulation. |journal=J. Biol. Chem. |volume=275 |issue= 35 |pages= 27123-8 |year= 2000 |pmid= 10859319 |doi= 10.1074/jbc.M004218200 }}
*{{cite journal  | vauthors =Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933–46 |year= 2000 |pmid= 10949161 |doi= 10.1080/07391102.2000.10506582}}
*{{cite journal  | author=Hiller O, Lichte A, Oberpichler A, ''et al.'' |title=Matrix metalloproteinases collagenase-2, macrophage elastase, collagenase-3, and membrane type 1-matrix metalloproteinase impair clotting by degradation of fibrinogen and factor XII. |journal=J. Biol. Chem. |volume=275 |issue= 42 |pages= 33008-13 |year= 2000 |pmid= 10930399 |doi= 10.1074/jbc.M001836200 }}
*{{cite journal  | vauthors =Agapova OA, Ricard CS, Salvador-Silva M, Hernandez MR |title=Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human optic nerve head astrocytes |journal=Glia |volume=33 |issue= 3 |pages= 205–16 |year= 2001 |pmid= 11241738 |doi=10.1002/1098-1136(200103)33:3<205::AID-GLIA1019>3.0.CO;2-D  }}
*{{cite journal | author=Terp GE, Christensen IT, Jørgensen FS |title=Structural differences of matrix metalloproteinases. Homology modeling and energy minimization of enzyme-substrate complexes. |journal=J. Biomol. Struct. Dyn. |volume=17 |issue= 6 |pages= 933-46 |year= 2000 |pmid= 10949161 |doi= }}
*{{cite journal   |vauthors=Lang R, Kocourek A, Braun M, etal |title=Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure |journal=J. Mol. Biol. |volume=312 |issue= 4 |pages= 731–42 |year= 2001 |pmid= 11575928 |doi= 10.1006/jmbi.2001.4954 }}
*{{cite journal | author=Agapova OA, Ricard CS, Salvador-Silva M, Hernandez MR |title=Expression of matrix metalloproteinases and tissue inhibitors of metalloproteinases in human optic nerve head astrocytes. |journal=Glia |volume=33 |issue= 3 |pages= 205-16 |year= 2001 |pmid= 11241738 |doi= }}
*{{cite journal   |vauthors=Nar H, Werle K, Bauer MM, etal |title=Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor |journal=J. Mol. Biol. |volume=312 |issue= 4 |pages= 743–51 |year= 2001 |pmid= 11575929 |doi= 10.1006/jmbi.2001.4953 }}
*{{cite journal | author=Lang R, Kocourek A, Braun M, ''et al.'' |title=Substrate specificity determinants of human macrophage elastase (MMP-12) based on the 1.1 A crystal structure. |journal=J. Mol. Biol. |volume=312 |issue= 4 |pages= 731-42 |year= 2001 |pmid= 11575928 |doi= 10.1006/jmbi.2001.4954 }}
*{{cite journal   |vauthors=Joos L, He JQ, Shepherdson MB, etal |title=The role of matrix metalloproteinase polymorphisms in the rate of decline in lung function |journal=Hum. Mol. Genet. |volume=11 |issue= 5 |pages= 569–76 |year= 2002 |pmid= 11875051 |doi=10.1093/hmg/11.5.569  }}
*{{cite journal | author=Nar H, Werle K, Bauer MM, ''et al.'' |title=Crystal structure of human macrophage elastase (MMP-12) in complex with a hydroxamic acid inhibitor. |journal=J. Mol. Biol. |volume=312 |issue= 4 |pages= 743-51 |year= 2001 |pmid= 11575929 |doi= 10.1006/jmbi.2001.4953 }}
*{{cite journal   |vauthors=Andolfo A, English WR, Resnati M, etal |title=Metalloproteases cleave the urokinase-type plasminogen activator receptor in the D1-D2 linker region and expose epitopes not present in the intact soluble receptor |journal=Thromb. Haemost. |volume=88 |issue= 2 |pages= 298–306 |year= 2003 |pmid= 12195704 |doi= }}
*{{cite journal | author=Joos L, He JQ, Shepherdson MB, ''et al.'' |title=The role of matrix metalloproteinase polymorphisms in the rate of decline in lung function. |journal=Hum. Mol. Genet. |volume=11 |issue= 5 |pages= 569-76 |year= 2002 |pmid= 11875051 |doi=  }}
*{{cite journal   |vauthors=Strausberg RL, Feingold EA, Grouse LH, etal |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899–903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 | pmc=139241 }}
*{{cite journal | author=Andolfo A, English WR, Resnati M, ''et al.'' |title=Metalloproteases cleave the urokinase-type plasminogen activator receptor in the D1-D2 linker region and expose epitopes not present in the intact soluble receptor. |journal=Thromb. Haemost. |volume=88 |issue= 2 |pages= 298-306 |year= 2003 |pmid= 12195704 |doi= }}
*{{cite journal   |vauthors=Vos CM, van Haastert ES, de Groot CJ, etal |title=Matrix metalloproteinase-12 is expressed in phagocytotic macrophages in active multiple sclerosis lesions |journal=J. Neuroimmunol. |volume=138 |issue= 1–2 |pages= 106–14 |year= 2003 |pmid= 12742660 |doi=10.1016/S0165-5728(03)00036-5  }}
*{{cite journal | author=Strausberg RL, Feingold EA, Grouse LH, ''et al.'' |title=Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences. |journal=Proc. Natl. Acad. Sci. U.S.A. |volume=99 |issue= 26 |pages= 16899-903 |year= 2003 |pmid= 12477932 |doi= 10.1073/pnas.242603899 }}
*{{cite journal   |vauthors=Anghelina M, Schmeisser A, Krishnan P, etal |title=Migration of monocytes/macrophages in vitro and in vivo is accompanied by MMP12-dependent tunnel formation and by neovascularization |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=67 |issue= |pages= 209–15 |year= 2003 |pmid= 12858542 |doi=10.1101/sqb.2002.67.209  }}
*{{cite journal  | author=Vos CM, van Haastert ES, de Groot CJ, ''et al.'' |title=Matrix metalloproteinase-12 is expressed in phagocytotic macrophages in active multiple sclerosis lesions. |journal=J. Neuroimmunol. |volume=138 |issue= 1-2 |pages= 106-14 |year= 2003 |pmid= 12742660 |doi=  }}
*{{cite journal  | author=Anghelina M, Schmeisser A, Krishnan P, ''et al.'' |title=Migration of monocytes/macrophages in vitro and in vivo is accompanied by MMP12-dependent tunnel formation and by neovascularization. |journal=Cold Spring Harb. Symp. Quant. Biol. |volume=67 |issue=  |pages= 209-15 |year= 2003 |pmid= 12858542 |doi= }}
}}
}}
{{refend}}
{{refend}}


{{protein-stub}}
==External links==
{{WikiDoc Sources}}
* The [[MEROPS]] online database for peptidases and their inhibitors: [http://merops.sanger.ac.uk/cgi-bin/merops.cgi?id=M10.009 M10.009]
 
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[[Category:Matrix metalloproteinases]]
[[Category:Human proteins]]
[[Category:EC 3.4.24]]

Latest revision as of 16:38, 4 September 2017

macrophage elastase
Identifiers
EC number3.4.24.65
CAS number146888-86-0
Databases
IntEnzIntEnz view
BRENDABRENDA entry
ExPASyNiceZyme view
KEGGKEGG entry
MetaCycmetabolic pathway
PRIAMprofile
PDB structuresRCSB PDB PDBe PDBsum
Gene OntologyAmiGO / QuickGO
VALUE_ERROR (nil)
Identifiers
Aliases
External IDsGeneCards: [1]
Orthologs
SpeciesHumanMouse
Entrez

n/a

n/a

Ensembl

n/a

n/a

UniProt

n/a

n/a

RefSeq (mRNA)

n/a

n/a

RefSeq (protein)

n/a

n/a

Location (UCSC)n/an/a
PubMed searchn/an/a
Wikidata
View/Edit Human

Matrix metalloproteinase-12 (MMP-12) also known as macrophage metalloelastase (MME) or macrophage elastase (ME) is an enzyme that in humans is encoded by the MMP12 gene.[1][2][3]

Function

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. The prodomain is cleaved by extracellular proteinases when the enzyme is activated. The active enzyme is constituted by two domains, the catalytic domain resposnsible for its enzymatic activity and the hemopexin-like domain that in some MMPs plays a role in substrate recognition and can contribute to increasing catalytic efficiency. It is thought that the protein encoded by this gene is cleaved at both ends to yield the active enzyme, but this processing has not been fully described. The enzyme degrades soluble and insoluble elastin. The gene is part of a cluster of MMP genes which localize to chromosome 11q22.3.[1]

Clinical significance

MMP12 may play a role in aneurysm formation[4] and studies in mice and humans suggest a role in the development of emphysema.[5]

References

  1. ↑ 1.0 1.1 "Entrez Gene: MMP12 matrix metallopeptidase 12 (macrophage elastase)".
  2. ↑ Shapiro SD, Kobayashi DK, Ley TJ (November 1993). "Cloning and characterization of a unique elastolytic metalloproteinase produced by human alveolar macrophages". J. Biol. Chem. 268 (32): 23824–9. PMID 8226919.
  3. ↑ Belaaouaj A, Shipley JM, Kobayashi DK, Zimonjic DB, Popescu N, Silverman GA, Shapiro SD (June 1995). "Human macrophage metalloelastase. Genomic organization, chromosomal location, gene linkage, and tissue-specific expression". J. Biol. Chem. 270 (24): 14568–75. doi:10.1074/jbc.270.24.14568. PMID 7782320.
  4. ↑ Curci JA, Liao S, Huffman MD, Shapiro SD, Thompson RW (December 1998). "Expression and localization of macrophage elastase (matrix metalloproteinase-12) in abdominal aortic aneurysms". J. Clin. Invest. 102 (11): 1900–10. doi:10.1172/JCI2182. PMC 509141. PMID 9835614.
  5. ↑ Woodruff PG, Koth LL, Yang YH, Rodriguez MW, Favoreto S, Dolganov GM, Paquet AC, Erle DJ (December 2005). "A Distinctive Alveolar Macrophage Activation State Induced by Cigarette Smoking". Am. J. Respir. Crit. Care Med. 172 (11): 1383–92. doi:10.1164/rccm.200505-686OC. PMC 2718436. PMID 16166618.

Further reading

External links

  • The MEROPS online database for peptidases and their inhibitors: M10.009

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