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Information on EC 3.4.24.7 - interstitial collagenase and Organism(s) Rattus norvegicus and UniProt Accession P81563
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3.4.24.7 interstitial collagenaseSpecify your search results
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- 3.4.24.7
- metalloproteinases
- mmp-2
- metastasis
- gelatinase
- timp-1
-
zymography
- endothelial
- gelatin
- angiogenesis
- cartilage
- fibrosis
-
basement
- type-1
- stromelysins
-
invasiveness
- arthritis
- dermal
- plasminogen
-
gelatinolytic
- prommp-2
- proteinases
- integrins
- matrigel
- synovial
-
pericellular
- fibrosarcoma
-
mt-mmp
-
fibrillar
- procollagen
- chondrocytes
-
matrix-degrading
- collagenase-3
- progelatinase
- proenzyme
-
invadopodia
- laminin-5
- analysis
-
membrane-tethered
- pharmacology
- drug development
-
triple-helical
- diagnostics
-
photoaging
- medicine
- batimastat
- procollagenase
-
podosomes
- furin
- hemopexin
-
collagen-rich
- reck
- cortactin
-
pro-matrix
- synthesis
- matrilysin
-
emmprin
The taxonomic range for the selected organisms is: Rattus norvegicus
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
The expected taxonomic range for this enzyme is: Eukaryota, Bacteria, Archaea
Reaction Schemes
Cleavage of the triple helix of collagen at about three-quarters of the length of the molecule from the N-terminus, at Gly775-/-Ile in the alpha1(I) chain. Cleaves synthetic substrates and alpha-macroglobulins at bonds where P1' is a hydrophobic residue
Synonyms
mt1-mmp, mmp-14, interstitial collagenase, matrix metalloproteinase 1, collagenase-1, fibroblast collagenase, collagenase 1, vertebrate collagenase, membrane-type 1-mmp, matrix-metalloproteinase-1, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
azocollase
-
-
-
-
collagen peptidase
-
-
-
-
collagen protease
-
-
-
-
collagenase
collagenase A
-
-
-
-
collagenase MMP-1
-
-
-
-
Fibroblast collagenase
-
-
-
-
kollaza
-
-
-
-
matrix metalloproteinase 1
matrix metalloproteinase-1
matrix metalloproteinase-18
-
-
-
-
metallocollagenase
-
-
-
-
metalloproteinase-1
-
-
-
-
MMP-1
Myocardial collagenase
-
-
-
-
nucleolysin
-
-
-
-
soycollagestin
-
-
-
-
TC1
-
-
-
-
vertebrate collagenase
-
-
-
-
collagenase
-
-
-
-
matrix metalloproteinase 1
-
-
-
-
matrix metalloproteinase-1
-
-
-
-
MMP-1
-
-
-
-
CAS REGISTRY NUMBER
COMMENTARY
9001-12-1
-
SUBSTRATE
PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
Reversibility
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
acetyl-Pro-Leu-Gly-Ala-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ala + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Ile-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Ile + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Leu-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Leu + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Phe-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Phe + Leu-Gly-ethyl ester
-
-
-
?
acetyl-Pro-Leu-Gly-Val-Leu-Gly-ethyl ester + H2O
acetyl-Pro-Leu-Gly-Val + Leu-Gly-ethyl ester
-
-
-
?
collagen type IV alpha2 + H2O
?
cleavage at sites L715 and T917
-
-
?
Collagen + H2O
?
-
below 30°C the enzyme catalyzes a small number of cleavages in the native collagen molecule with no loss in tertiary structure. Fragments of 75, 67, and 62% of the molecular length from the A end are formed. At 37°C and neutral pH, the enzyme degrades native collagen fibrils or molecules to peptides most of which are dialyzable
-
-
?
Collagen + H2O
?
natural collagen fascicles (termed extracellular matrix/ECM) from tendons of 6-months-old rats, degradation patterns of natural collagen-rich extracellular matrix by MMP-1 compared to MMP-13. Cleavage sites identified in Col I-rich ECM under proteolytic degradation by MMP-1, overview
-
-
?
additional information
?
-
-
myocardial matrix degradation by MMP-1 induced by thyroid hormone through enzyme activation, enzyme regulation involving suppression of tissue inhibitors of matrix metalloproteinases TIMPs and distribution, overview
-
-
?
additional information
?
-
proteomic analysis of MMP-1 activity using LC-MS/MS analysis
-
-
?
NATURAL SUBSTRATE
NATURAL PRODUCT
REACTION DIAGRAM
ORGANISM
UNIPROT
COMMENTARY
(Substrate)
(Substrate)
LITERATURE
(Substrate)
(Substrate)
COMMENTARY
(Product)
(Product)
LITERATURE
(Product)
(Product)
REVERSIBILITY
r=reversible
ir=irreversible
?=not specified
r=reversible
ir=irreversible
?=not specified
additional information
?
-
-
myocardial matrix degradation by MMP-1 induced by thyroid hormone through enzyme activation, enzyme regulation involving suppression of tissue inhibitors of matrix metalloproteinases TIMPs and distribution, overview
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Ca2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
benzo[a]pyrene
increases the mRNA levels of matrix metalloproteinases MMP-1, MMP-2, MMP-3, and MMP-9 in vascular smooth muscle cells and promotes the migration and invasion of cells
TIMP-1
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
-
additional information
platelet-derived growth factor (PDGF) treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
thyroid hormone
-
thyroid hormone induces myocardial matrix degradation by MMP-1 activation
-
additional information
-
dexamethasone induces myocardial matrix degradation by MMP-1
-
KM VALUE [mM]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
TURNOVER NUMBER [1/s]
SUBSTRATE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH RANGE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
5.8 - 9
-
pH 5.8: about 30% of maximal activity, pH 9.0: about 45% of maximal activity
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
the MMP-1 levels are altered in the left ventricle and serum in case of hypertrophy through hyperthyroid conditions with 3,5,3'-triiodo-L-thyroine or dexamethasone application, tissue distribution, overview
-
from Achilles tendon, immunohistochemic analysis of MMP-1, overview
additional information
detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts
-
expression profile of MMPs/TIMP-1 after myocardial infarction, angiotensin II receptor blockade improves MMPs/TIMP-1 balance, overview
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
metabolism
physiological function
additional information
detection of collagen deposition and MMP-1 secretion in rat-1 fibroblasts, macrorheological properties and morphologies of natural and MMP-degraded ECMs
metabolism
matrix metalloproteinase 1 and collagens play a key role in platelet-derived growth factor (PDGF) and stromal cell-derived factor-1 (SDF-1) promotion of the skin wound repairing effect of bone mesenchymal stem cells. Bone marrow mesenchymal stem cells (BMSCs) are applied to treatment of skin wounds. PDGF treatment recruits BSMCs to injured sites and strengthens the effect of BMSCs on skin wound by suppressing activity of MMP-1. SDF-1 treatment increases the treating effect of BMSCs on skin injury through the deposition of collagen I and collagen III. Phenotypes, overview
metabolism
the expression profiles of multiple and possibly redundant matrix-remodeling proteases (e.g., collagenases) differ strongly in health, disease, and development. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes
physiological function
-
matrix metalloproteinases and the tissue inhibitors of MMPs, TIMPs, play a pivotal role in matrix remodeling following myocardial infarction, the MMPs/TIMP-1 balance is perturbed after myocardial infarction. Oral valsartan, but not PD123319 limits infarct size, normalized MMPs/TIMP-1 balance and restores FN level
physiological function
-
transfection of a plasmid expression of MMP-1 into myocard after infarction increases myocyte shortening and reduces Na+-Ca2+ exchange current, it decreases myocardial fibrosis and improves cardiac remodeling and function
physiological function
the protease drives morphological, biochemical, and viscoelastic changes in the extracellular matrix (ECM) leading to unique ECM-cell crosstalk, complexity and selectivity of collagenase-associated degradation mechanisms during tissue remodeling. Matrix metalloproteinases MMP-1 and MMP-13 cause distinct extracellular matrix (ECM) degradation, bringing about significantly distinct cellular phenotypes. Specific influences of the highly abundant collagenases on fibroblast-ECM crosstalk, overview
UNIPROT
ENTRY NAME
ORGANISM
NO. OF AA
NO. OF TRANSM. HELICES
MOLECULAR WEIGHT[Da]
SOURCE
SEQUENCE
LOCALIZATION PREDICTION
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable).
The reliability class of the localization prediction ranges from 1 (very reliable) to 5 (not reliable). MMP1_RAT
15
0
1787
Swiss-Prot
other Location (Reliability: 1)
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
transfection of rat myocard with a plasmid encoding MMP-1, DNA release and MMP1 expression, effects on myocard remodeling, overview. MMP-1 expression increases myocyte shortening and reduces Na+-Ca2+ exchange current, it decreases myocardial fibrosis and improves cardiac remodeling and function
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
ibuprofen upregulates expressions of matrix metalloproteinase-1, as well as MMP-8, MMP-9, and MMP-13, without affecting expressions of types I and III collagen in tendon cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
-
in ovariectomized rats, during the first 1-4 weeks there is a significant increase in collagen accumulation and an increase MT1-MMP expression. Although active-form matrix metalloproteinase MMP-2 and collagen progressively return to normal levels, the markedly increased collagen deposition appears again at 8 weeks and persists until 12 weeks, followed by induction of MMP-2 and MT1-MMP at 12 weeks
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Seifter, S.; Harper, E.
The collagenases
The Enzymes, 3rd Ed. (Boyer, P. D. , ed. )
3
649-697
1971
Capra hircus, Cavia porcellus, Oryctolagus cuniculus, Homo sapiens, Lithobates catesbeianus, Rattus norvegicus
-
Weingarten, H.; Feder, J.
Cleavage site specificity of vertebrate collagenases
Biochem. Biophys. Res. Commun.
139
1184-1187
1986
Oryctolagus cuniculus, Frog, Homo sapiens, Rattus norvegicus, Sus scrofa
Welgus, H.G.; Stricklin, G.P.; Eisen, A.Z.; Bauer, E.A.; Cooney, R.V.; Jeffrey, J.J.
A specific inhibitor of vertebrate collagenases produced by human skin fibroblasts
J. Biol. Chem.
254
1938-1943
1979
Homo sapiens, Rattus norvegicus
Jeffrey, J.J.; Gross, J.
Collagenase from rat uterus. Isolation and partial characterization
Biochemistry
9
268-273
1970
Rattus norvegicus
Sudbeck, H.D.; Jeffrey, J.J.; Welgus, H.G.; Mecham, R.P.; McCourt, D.; Parks, W.C.
Purification and characterization of bovine interstitial collagenase and tissue inhibitor metalloproteinases
Arch. Biochem. Biophys.
293
370-376
1992
Bos taurus, Homo sapiens, Rattus norvegicus
Ghose Roy, S.; Mishra, S.; Ghosh, G.; Bandyopadhyay, A.
Thyroid hormone induces myocardial matrix degradation by activating matrix metalloproteinase-1
Matrix Biol.
26
269-279
2007
Rattus norvegicus
Lam, K.K.; Cheng, P.Y.; Hsiao, G.; Chen, S.Y.; Shen, H.H.; Yen, M.H.; Lee, Y.M.
Estrogen deficiency-induced alterations of vascular MMP-2, MT1-MMP, and TIMP-2 in ovariectomized rats
Am. J. Hypertens.
22
27-34
2009
Rattus norvegicus
Meng, D.; Lv, D.D.; Zhuang, X.; Sun, H.; Fan, L.; Shi, X.L.; Fang, J.
Benzo[a]pyrene induces expression of matrix metalloproteinases and cell migration and invasion of vascular smooth muscle cells
Toxicol. Lett.
184
44-49
2009
Rattus norvegicus (P81563)
Yang, D.; Ma, S.; Li, D.; Tang, B.; Yang, Y.
Angiotensin II receptor blockade improves matrix metalloproteinases/tissue inhibitor of matrix metalloproteinase-1 balance and restores fibronectin expression in rat infarcted myocardium
Biochem. Biophys. Res. Commun.
388
606-611
2009
Rattus norvegicus
Lin, X.; Jo, H.; Ishii, T.M.; Fujita, M.; Fu, M.; Tambara, K.; Yamamoto, M.; Tabata, Y.; Komeda, M.; Matsuoka, S.
Controlled release of matrix metalloproteinase-1 plasmid DNA prevents left ventricular remodeling in chronic myocardial infarction of rats
Circ. J.
73
2315-2321
2009
Rattus norvegicus
Tsai, W.C.; Hsu, C.C.; Chang, H.N.; Lin, Y.C.; Lin, M.S.; Pang, J.H.
Ibuprofen upregulates expressions of matrix metalloproteinase-1, -8, -9, and -13 without affecting expressions of types I and III collagen in tendon cells
J. Orthop. Res.
28
487-491
2010
Rattus norvegicus
Xu, H.; Zhang, H.; Ding, Y.
Platelet-derived growth factor and stromal cell-derived factor-1 promote the skin wound repairing effect of bone mesenchymal stem cells a key role of matrix metalloproteinase 1 and collagens
Int. J. Clin. Exp. Pathol.
10
8253-8262
2017
Rattus norvegicus (B5DFD5), Rattus norvegicus Sprague-Dawley (B5DFD5)
Solomonov, I.; Zehorai, E.; Talmi-Frank, D.; Wolf, S.G.; Shainskaya, A.; Zhuravlev, A.; Kartvelishvily, E.; Visse, R.; Levin, Y.; Kampf, N.; Jaitin, D.A.; David, E.; Amit, I.; Nagase, H.; Sagi, I.
Distinct biological events generated by ECM proteolysis by two homologous collagenases
Proc. Natl. Acad. Sci. USA
113
10884-10889
2016
Rattus norvegicus (B5DFD5), Homo sapiens (P03956)
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