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Information on EC 3.4.24.B7 - matrix metalloproteinase-26 and Organism(s) Homo sapiens and UniProt Accession Q9NRE1
for references in articles please use BRENDA:EC3.4.24.B7preliminary BRENDA-supplied EC number
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EC Tree
3.4.24.B7 matrix metalloproteinase-26Specify your search results
Word Map
- 3.4.24.B7
- endometrial
- timp-4
- mmp-1
- matrilysins
-
menstrual
- medicine
- pro-mmp-9
-
olomouc
- metalloelastase
-
palacky
-
metalloproteinase-4
- prodomain
- diagnostics
- synthesis
The taxonomic range for the selected organisms is: Homo sapiens
The enzyme appears in selected viruses and cellular organisms
The enzyme appears in selected viruses and cellular organisms
Synonyms
mmp-26, matrilysin-2, matrix metalloproteinase-26, endometase, mmp-26/endometase/matrilysin-2, matrilysin 2, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
MMP-26
-
-
REACTION
REACTION DIAGRAM
COMMENTARY
ORGANISM
UNIPROT
LITERATURE
proteolytic degradation of proteins
consensus cleavage sequence is Pro-Glu-Xaa/Leu-Xaa-Thr-Xaa
proteolytic degradation of proteins
mechanism, His81 plays a significant role in functional modification
-
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY
288381-81-7
-
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
(7-methoxycoumarin-4-yl)acetyl-PLAQAV-Dpa-RSSSR-NH2 + H2O
?
synthetic fluorogenic peptide derived of tumor necrosis factor-alpha converting enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-Pro-Cha-Gly-norvaline-His-Ala-Dpa-NH2 + H2O
?
synthetic fluorogenic substrate
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPVA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide, catalytic domain of the enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPVE-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
progelatinase B + H2O
gelatinase B
substrate becomes activated, both enzymes can act as coordinately as part of a proteolytic cascade
-
?
Vitronectin + H2O
?
complete degradation, cleavage sequence is PPEG134-I135DSR
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Ala-Nva-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Ala + Nva-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2
-
among the fluorescent peptide substrates analyzed, 7-amido-4-methylcoumaryl-Pro-Leu-Ala-Nva-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 displays the highest specificity constant
-
-
?
(7-methoxycoumarin)-4-yl-acetyl-Pro-Leu-Gly-Leu-(N-3-(2,4-dinitrophenyl)-L-2,3-diaminopropionyl)-Ala-Arg-NH2 + H2O
?
-
-
-
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
-
synthetic fluorogenic peptide
-
?
alpha1-proteinase inhibitor + H2O
?
-
MMP-26 cleaves Phe352Leu353 and Pro357Met358 in the reactive loop of alpha1-proteinase inhibitor, probably rendering the substrate inactive
-
-
?
insulin-like growth factor-binding protein-1 + H2O
?
-
cleaves His140Val141 in insulin-like growth factor-binding protein-1, probably rendering the substrate inactive
-
-
?
peptide + H2O
?
-
the optimal cleavage motifs for MMP-26 are Lys-Pro-Ile(Leu)-Ser-/-Leu(Met)-Ile(Thr)-Ser(Ala)-Ser. The strongest preference is observed at the P1' and P2 sites where hydrophobic residues are favored. Proline is preferred at P3, and serine is preferred at P1
-
-
?
(7-methoxycoumarin-4-yl)acetyl-PKPLAL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
(7-methoxycoumarin-4-yl)acetyl-PKPLAL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide, catalytic domain of the enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic substrate
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
(7-methoxycoumarin-4-yl)acetyl-PLGL-Dpa-AR-NH2 + H2O
?
synthetic fluorogenic peptide, derived from the catalytic domain of the enzyme
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPYA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide derived of matrix metalloproteinases
-
?
(7-methoxycoumarin-4-yl)acetyl-RPKPYA-norvaline-WMK-(2,4-dinitrophenyl)-NH2 + H2O
?
synthetic fluorogenic peptide, catalytic domain of the enzyme
-
?
Fibrinogen + H2O
?
complete degradation, cleavage sequenced of the peptide chains, overview
-
?
proteins + H2O
peptides
enzyme might be rsponsible for inactivation of cytokins and serpins
-
?
proteins + H2O
peptides
enzyme plays an important specific role in tumor progression and angiogenesis
-
?
proteins + H2O
peptides
potentially implicated in tumor progression
-
?
alpha1-antitrypsin + H2O
?
-
MMP-26 by cleaving and inactivating the alpha1-antitrypsin serpin, operates as a unique functional link that regulates a coordinated interplay between Ser and metalloproteinases in estrogen-dependent neoplasm. Involvement of MMP-26 in inflammation and malignant progression of estrogen-dependent tumor
-
-
?
alpha1-antitrypsin + H2O
?
-
the enzyme is highly efficient in cleaving the the serpin alpha1-antitrypsin at the positions Gln135-/-Leu136, Glu223-/-Val224, Phe376-/-Leu377, and Pro381-/-Met382
-
-
?
pro-MMP-9 + H2O
MMP-9 + MMP-9 propeptide
-
MMP-26 can activate MMP-9 by cleavage of some sites in pro-MMP-9
-
-
?
additional information
?
-
no activity with collagens, laminin, elastin, beta-casein, plasminogen, soybean trypsin inhibitor, Bowman-Birk inhibitor
-
?
additional information
?
-
-
no activity with collagens, laminin, elastin, beta-casein, plasminogen, soybean trypsin inhibitor, Bowman-Birk inhibitor
-
?
additional information
?
-
-
increased level and activation of MMP-26 in gingival crevicular fluid is associated with an enhanced severity of periodontal inflammation, suggesting that MMP-26 can participate in the progression of periodontal diseases
-
-
?
additional information
?
-
-
the enzyme exhibits an unconventional PH81CGVPD Cys switch motif
-
-
?
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
alpha1-antitrypsin + H2O
?
-
MMP-26 by cleaving and inactivating the alpha1-antitrypsin serpin, operates as a unique functional link that regulates a coordinated interplay between Ser and metalloproteinases in estrogen-dependent neoplasm. Involvement of MMP-26 in inflammation and malignant progression of estrogen-dependent tumor
-
-
?
additional information
?
-
-
increased level and activation of MMP-26 in gingival crevicular fluid is associated with an enhanced severity of periodontal inflammation, suggesting that MMP-26 can participate in the progression of periodontal diseases
-
-
?
proteins + H2O
peptides
enzyme might be rsponsible for inactivation of cytokins and serpins
-
?
proteins + H2O
peptides
enzyme plays an important specific role in tumor progression and angiogenesis
-
?
proteins + H2O
peptides
potentially implicated in tumor progression
-
?
pro-MMP-9 + H2O
MMP-9 + MMP-9 propeptide
-
MMP-26 can activate MMP-9 by cleavage of some sites in pro-MMP-9
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
Zn2+
Ca2+
Zn2+
Zn2+
contains a zinc-binding site, coordination of zinc at the active site
Ca2+
-
MMP-26 has one high-affinity and one low-affinity calcium binding site. High-affinity calcium binding is restored at physiologically low calcium conditions with a calcium-dissociation constant of 63 nM without inducing secondary and tertiary structural changes. Low-affinity calcium binding is restored at relatively high calcium concentrations and shows a low-affinity calcium-dissociation constant value of 0.12 mM, which is accompanied with the recovery of enzymatic activity reversibly and tertiary structural changes, but without secondary structural rearrangements
Zn2+
-
zinc ion in the catalytic domain interacts with the conserved sequence PRCXXPD
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
(3R)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
-
(3S)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
-
Brij-35
-
optimally activating at 0.056 mM, at concentrations above the critical micelle concentration, it inhibits the enzyme noncompetitively at 0.05%, i.e. 0.417 mM
N-[(2R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl]-L-tryptophan
-
i.e. GM6001
SDS
-
optimally activating at 0.0095 mM, at concentrations above the critical micelle concentration
Tetradecyltrimethylammonium bromide
-
optimally activating at 0.0075 mM, at concentrations above the critical micelle concentration
Triton X-100
-
optimally activating at 0.140 mM, at concentrations above the critical micelle concentration
Tween 20
-
optimally activating at 0.079 mM, at concentrations above the critical micelle concentration
additional information
-
the hydrolytic activity of endometase is detergent concentration dependent, exhibiting a bell-shaped curve with its maximum activity near the critical micelle concentration of nonionic detergents tested, overview. Monomer of detergents may activate and stabilize MMPs to enhance catalysis, but micelle of detergents may sequester enzyme and block the substrate binding site to impede catalysis
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Brij-35
-
optimally activating at 0.056 mM, at concentrations above the critical micelle concentration, it inhibits the enzyme noncompetitively at 0.05%, i.e. 0.417 mM
SDS
-
optimally activating at 0.0095 mM, at concentrations above the critical micelle concentration
Tetradecyltrimethylammonium bromide
-
optimally activating at 0.0075 mM, at concentrations above the critical micelle concentration
Triton X-100
-
optimally activating at 0.140 mM, at concentrations above the critical micelle concentration
Tween 20
-
optimally activating at 0.079 mM, at concentrations above the critical micelle concentration
additional information
-
the hydrolytic activity of endometase is detergent concentration dependent, exhibiting a bell-shaped curve with its maximum activity near the critical micelle concentration of nonionic detergents tested, overview. Monomer of detergents may activate and stabilize MMPs to enhance catalysis, but micelle of detergents may sequester enzyme and block the substrate binding site to impede catalysis
-
Ki VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
0.0000015
(3R)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
-
0.00006
(3S)-N-hydroxy-2-[(4-methoxyphenyl)sulfonyl]-1,2,3,4-tetrahydroisoquinoline-3-carboxamide
-
-
0.00000036
N-[(2R)-2-(hydroxamidocarbonylmethyl)-4-methylpentanoyl]-L-tryptophan
-
-
additional information
additional information
-
detergent inhibition kinetics, overview
-
IC50 VALUE [mM]
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
SwissProt
enzyme shares minimal domain organisation and a threonine residue adjacent to the zinc-binding site with matrilysin
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
constitutive expression. Protein is found in both disc cells and in the disc extracellular matrix. MMP-26 is identified in the outer and inner annulus and in the nucleus pulposus. Fewer cells show localization in the inner vs. outer annulus, and localization is sparse in the nucleus
MMP-26 mRNA is evenly distributed in all glandular epithelial cells and luminal epithelial cells but is absent in the stroma. The amount of MMP-26 mRNA is greater in samples at day 5 in an artificial cycle of progesterone addition than at day 7 in an artificial cycle of progesterone addition
-
epithelium and stroma of adenomatoid odontogenic tumors, overview
-
beta-catenin regulates the gene of MMP-26, a novel metalloproteinase expressed both in carcinomas and normal epithelial cells
-
slightly enhanced MMP-26 staining in HIV+ gingival tissue samples in comparison with controls
-
from patients with aggressive periodontitis, with chronic periodontitis, with gingivitis and periodontally healthy subjects. Patients with aggressive periodontitis and patients with chronic periodontitis have elevated MMP-26 levels and degrees of activation compared with the gingivitis and healthy groups. The gingivitis group has higher MMP-26 levels and degree of activation compared to the healthy group
-
elevated MMP-26 expression level
in the outer and inner annulus and in the nucleus pulposus
-
matrilysin-2 (matrix metalloproteinase-26) is upregulated in keratinocytes during wound repair and early skin carcinogenesis. MMP-26 is expressed by laminin-5-positive keratinocytes in the migrating area during wound repair, in benign skin disorders characterized by inflammation and microdisruptions of basement membrane. MMP-26 may be upregulated in basal keratinocytes even without tumorigenesis because of altered cell-matrix interactions and inflammation
-
in the course of further disease progression through stages I to III, the expression of MMP-26 decreases. The expression of MMP-26 in ductal carcinomas correlates with a longer patient survival
-
patients with metastatic lymph nodeshave increased expression of MMP-26 in tumor samples
-
matrix metalloproteinase-26 is associated with macrophages and polymorphonuclear leukocytes
-
from coronary artery or from prostate tissue and associated blood vessels
additional information
-
beta-catenin regulates the gene of MMP-26, a novel metalloproteinase expressed both in carcinomas and normal epithelial cells
-
overexpression in 24 of the 50 esophageal squamous cell carcinoma tissues. Overexpression is significantly correlated with depth of invasion, lymph node metastasis amd an advance in pathological tumor node metastasis stage
-
33 out of 34 of the primary tumors express MMP-26. Most abundant expression concentrates in grade I-II tumors. In normal esophagus, the basal cells are usually negative for MMP-26, except for occasional basal cells at the top of epidermal papillae. MMP-26 is already upregulated in dysplasia. Tumor cells making contact with islets undergoing apoptosis show prominent MMP-26 staining, and inflammation upregulates MMP-26 expression. When the invasive islet escapes through the basement membrane, MMP-26 expression becomes abundant. The pushing border of the tumor only shows dispersed MMP-26 staining, and MMP-26 does not colocalize with proliferation or apoptosis. Neoplastic islands are often positive for MMP-26. In 2 out of 4 lymph nodes, MMP-26 is detected in metastatic tumor cells, where individual cancer cells expressed MMP-26 on the border of apoptotic areas non-neoplastic epithelium
-
matrix metalloproteinase-26 is associated with macrophages and polymorphonuclear leukocytes
-
MMP-26 predominantly accumulates in its proenzyme form in the intracellular milieu of the transfected breast carcinoma MCF-7 cells
-
malignant prostate tumor. Higher MMP-26 expression in high-grade prostatic intraepithelial neoplasia and cancer, compared to non-neoplastic acini. The expression level is highest in high-grade prostatic intraepithelial neoplasia, but declines in invasive cancer in the same tissue. MMP-26 may play an important role in the initial conversion of prostate cancer cells to an invasive phenotype
-
MMP-26 may participate in stromal remodelling and regulation of inflammation in various skin disorders, such as granulomatous diseases or actinic damage
-
MMP-26 is expressed in grade I and II squamous cell cancer. It is not present in dedifferentiated grade III tumors. MMP-26 becomes downregulated during histological dedifferentiation of squamous cell cancer cells
-
MMP-26 is present more frequently in squamous cell carcinomas of immunosuppressed compared with immunocompetent patients. Stromal staining for MMP-26 in elastic fibers and endothelial cells does not differ between the groups
additional information
no expression in testis, heart, brain, lung, liver, thymus, and melanoma G361 cell
additional information
-
no expression in testis, heart, brain, lung, liver, thymus, and melanoma G361 cell
additional information
-
matrilysin-2 mRNA expression is undetectable or only faintly detected in non-tumor tissues
additional information
-
MMP-26 exists in the form of complexes with other extracellular matrix components and/or their tissue inhibitors in control and preeclamptic subjects, overview
additional information
-
MMP-26 immunohistochemic expression analysis and comparison to MMP-7 or matrilysin-1, overview
additional information
-
MMP-26 shows unique but complex expression patterns in normal and abnormal tissue, RT-PCR expression analysis, overview
additional information
-
RT-PCR MMP-26 expression profiling in different human cancer tissues, several cancer tissue show elevated MMP-26 expression compared to benign tissue
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
residues 88-123 function to localize MMP-26 to the endoplasmic reticulum
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
physiological function
malfunction
-
silencing of the MMP-26 gene significantly retardes the invasiveness of A-549 cells
physiological function
additional information
physiological function
MMP26-transfected MCF-7 cells demonstrate increased atypia, including unusual mitotic figures, glucogen pools and special lysosomes in the cytoplasm. The adherence and spreading ability of MMP26-transfected cells are significantly increased compared with cells in the control group. The migration and invasion ability of MMP26-transfected cells is dramatically accelerated compared with the control group, but markedly reduced in the presence of anti-MMP26 antibody. MMP26 also increases the malignant phenotype in vivo. The number of vessel branches and the total length of vessels induced by MMP26-transfected cells are significantly increased compared to those induced by nontransfected cells
physiological function
overexpression of MMP26 in SW-1353 chondrosarcoma cells increases cell invasiveness, while inhibition of MMP26 decreases cell invasiveness. Inhibition of Wnt signaling significantly decreases the effect of MMP26 on cancer cell invasion
physiological function
MMP-26 expression levels in androgen-repressed human prostate cancer cells, transfected with sense or anti-sense MMP-26 cDNA, and in benign, neoplastic, and invasive prostate cancer tissues are directly correlated with those of the pro-apoptotic marker Bax. The MMP-26 protein levels are upregulated in high grade prostate intraepithelial neoplasia and decrease during the course of disease progression
physiological function
-
MMP-26 is implicated in genesis, progression, invasion and metastasis of several types of human cancers
physiological function
-
MMP-26 may possess critical roles in the processes of tumor invasion, angiogenesis, and metastasis
physiological function
-
MMP-26 participates in activation other members of the MMP family
physiological function
-
MMP-26 plays an important role in local invasion, and angiogenesis. MMP-26 contributes to tumor development and to the restoration of tissue injury. The spreading cell ratio of MMP-26 transfected cells is significantly higher than parental U251 cells
physiological function
-
the matrilysins, also known as MMP-7 or matrilysin-1 and MMP-26 or matrilysin-2, are involved in cell proliferation, apoptosis, invasion, and metastasis. Matrilysin-2 plays a role in the process of tissue remodeling and growth in the studied tumors, but it does not relate to the their distinct patterns of aggressiveness
physiological function
-
MMP-26 contributes to A-549 cell invasion and migration in vitro. MMP-26 plays an important role in local through coordination with MMP-9
physiological function
MMP-26 plays an important role of in matrix modulation during disc health and degeneration
additional information
-
MMP-26 and MMP-9 may contribute to the more aggressive behavior of squamous cell carcinomas in organ transplant recipients
additional information
-
under physiological conditions, a lipid or membrane microenvironment may regulate enzymatic activity
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). MMP26_HUMAN
261
0
29708
Swiss-Prot
other Location (Reliability: 1)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
19000
x * 19000, SDS-PAGE of catalytic form, x * 28000, SDS-PAGE of His-tagged proform
28000
28000
x * 19000, SDS-PAGE of catalytic form, x * 28000, SDS-PAGE of His-tagged proform
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
?
x * 19000, SDS-PAGE of catalytic form, x * 28000, SDS-PAGE of His-tagged proform
additional information
-
the prodomain of MMP-26 is necessary for proper folding of the enzyme. Homology-modeling of the structure of the MMP-26 catalytic domain, overview
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
glycoprotein
proteolytic modification
additional information
glycoprotein
two (N64, N221) of the three possible N-glycosylation sites in MMP-26 are N-glycosylated, and N-glycosylation is not required for ER localization
proteolytic modification
-
autoactivation by autocleavage of the proform at sequence Lys-Lys-Gln59-Gln60-Phe-His, His81 plays a significant role in functional modification
proteolytic modification
-
two of the major autolytic sites are Leu49/-Thr50 and Ala75/-Leu76, which still left the cysteine switch sequence intact
additional information
-
no activation of the proform by organomercurial treatment
additional information
-
MMP-26 is only active after treatement with reducing agents
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
D114A
D165A
-
very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26
E191A
-
very low rates of hydrolysis that are less than 5% of that seen for wild-type MMP-26
H81R
-
mutation restores the conventional cysteine-switch in the prodomain but fails to induce the cysteine-swich activation
K189E
V184D
-
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis
additional information
exchanging residues 88-123 of secretory MMP-7 with the same region in MMP-26 causes localization of this MMP-7 construct to the ER
D114A
-
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis
D114A
-
mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively
K189E
-
calcium-independent high invasiveness is observed in the K189E mutant MDA-MB-231 cell line
K189E
-
mutant enzyme shows high rates of fluorescent synthetic peptide hydrolysis
K189E
-
mutation induces enhanced affinity for the Ca2+ ion or an irreversible loss of enzymatic activity triggered by low-affinity calcium binding respectively
TEMPERATURE STABILITY
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
high-affinity calcium binding protects MMP-26 against thermal denaturation
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
recombinant catalytic domain from inclusion bodies expressed in Escherichia coli
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
DNA and amino acid sequence determination and analysis, chromosomal mapping to the short arm of chromosome 11 around 11p15, expression in Escherichia coli as His-tagged protein
DNA and amino acid sequence determination and analysis, chromosome mapping to 11p15.3, expression of the enzymes catalytic domain in Escherichia coli BL21 (DE3)
DNA sequence determination and analysis, expression of the zymogen in Escherichia coli
expression in Escherichia coli. Human breast cancer cell line, MDA-MB-231, transfected with wild-type MMP-26 cDNA shows a calcium-dependent invasive potential when compared with controls that were transfected with an inactive form of MMP-26 (E209A)
-
U251 cells wae transfected with a proMMP-26 cDNA encoding vector, establishment of an MMP-26 overexpressing U251 cell model, overview
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
preeclampsia induces a significant increase in the content and actual activity of MMP-26 in umbilical cord vein and Wharton's jelly
significant downregulation of expression of MMP-26, and significant 9.8fold upregulation of TGF-beta in more degenerated discs versus healthier discs
regulatory effects of gonadotropin-releasing hormone I and gonadotropin-releasing hormone II, GnRH I and GnRH II, on the expression of MMP-26 in human immortalized cytotrophoblast-like cell line, B6Tert-1. The activation of JNK, but not ERK1/2, is required for GnRH I and II-stimulated MMP-26 production in B6Tert-1 cells and primary cytotrophoblasts
-
there is significant downregulation of expression of MMP-26 in more degenerated discs vs. healthier discs
RENATURED/Commentary
ORGANISM
UNIPROT
LITERATURE
recombinant zymogen from inclusion bodies expressed in Escherichia coli, partial activation of th proform during refolding
refolding of recombinant catalytic domain from inclusion bodies expressed in Escherichia coli
refolding of recombinant protein from inclusion bodies expressed in Escherichia coli
solubilization of recombinant proMMP-26 from Escherichia coli inclusion bodies by 8 M urea, followed by dialysis against 4 M urea, 1 mM DTT, and 50 mM HEPES or Tricine at pH 7.5 for at least 1 h, and then folded by dialysis against buffer containing 50 mM Hepes, 0.2 M, NaCl, 10 mM CaCl2, 20 lM ZnSO4, and 0.05% Brij-35 at pH 7.5 for 12 h three times, MMP-26 autoactivates
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
synthesis
use of Brevibacillus choshinensis as the host system for the soluble and active expression of MMP26. The enzyme is secreted in soluble form in the supernatant of cell culture medium. The yields of purified proform of MMP26 and catalytic form of MMP-26 are 12 and 18 mg/L, respectively, with high purity and homogeneity. Both pro- and catalytic form show gelatin zymography activity and the purified catalytic form has high enzymatic activity against DQ-gelatin substrate. Expression using several widely used expression vectors in Escheriochia coli cells results in insoluble expressions or soluble expressions with little catalytic activity
medicine
medicine
matrix metalloproteinase MMP26 level is significantly higher in the resected chondrosarcoma than in the adjacent healthy chondral tissue from patients. Overexpression of MMP26 in SW-1353 cells increases cell invasiveness, while inhibition of MMP26 decreases cell invasiveness. Inhibition of Wnt signaling significantly decreases the effect of MMP26 on cancer cell invasion. A strong correlation is detected between MMP26 levels and the ratio of phosphorylated/total beta-catenin in chondrosarcoma from the patients
medicine
slight, but significant, downregulation of MMP-26 in more degenerated intervertebral discs (Thompson grades III, IV and V) compared to healthier discs, while both TGF-beta and latent transforming growth factor-beta binding protein 2 are significantly and strongly upregulated
medicine
all umbilical cord tissues, both control and preeclamptic, express MMP-26 and issue inhibitor of matrix metalloproteinase TIMP-4 in macromolecular complexes. Preeclampsia induces a significant increase in the content and actual activity of MMP-26 in umbilical cord vein and Wharton's jelly. The content of TIMP-4 in preeclamptic umbilical cord vein and Wharton's jelly is reduced. The content of MMP-26 mRNA is lower in umbilical cord arteries and veins, whereas higher in Wharton's jelly in preeclampsia
medicine
in astrocytic glioma, MMP-26 expression is significantly associated with the World Health Organization grade. MMP-26 expression is an independent factor for evaluating the prognosis of astrocytic glioma patients
medicine
MMP-26 expression levels in androgen-repressed human prostate cancer cells, transfected with sense or anti-sense MMP-26 cDNA, and in benign, neoplastic, and invasive prostate cancer tissues are directly correlated with those of the pro-apoptotic marker Bax. The MMP-26 protein levels are upregulated in high grade prostate intraepithelial neoplasia and decrease during the course of disease progression
medicine
-
expression of matrilysin-2 is significantly correlated with nuclear beta-catenin expression and MMP-9 expression. Patients with matrilysin-2-positive cancer have significantly shorter overall and disease-free survival periods than those with matrilysin-2 negative cancer. Matrilysin-2 expression retains its significant predictive value for overall and disease-free survival in multivariate analysis. Patients with concomitant expression of matrilysin-2 and MMP-9 have the worst prognosis
medicine
-
MMP-26 is a valuable cancer marker, that contributers favorably to the survival of the estrogen receptor alpha/beta-positive cohort of breast cancer patients
medicine
-
MMP-26 may play an integral role during the conversion of HGPIN to invasive cancer and may also serve as marker for early prostate cancer diagnosis
medicine
-
matrix metalloproteinase-26 is a marker of melanomas and estrogen-dependent carcinomas
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JOURNAL
VOL.
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ORGANISM (UNIPROT)
PUBMED ID
SOURCE
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Homo sapiens (Q9NRE1), Homo sapiens
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Homo sapiens (Q9NRE1), Homo sapiens
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Homo sapiens (Q9NRE1), Homo sapiens
Marchenko, N.D.; Marchenko, G.N.; Strongin, A.Y.
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Homo sapiens
Park, H.I.; Turk, B.E.; Gerkema, F.E.; Cantley, L.C.; Sang, Q.X.
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Homo sapiens
Park, H.I.; Jin, Y.; Hurst, D.R.; Monroe, C.C.; Lee, S.; Schwartz, M.A.; Sang, Q.X.
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Homo sapiens
Li, W.; Savinov, A.Y.; Rozanov, D.V.; Golubkov, V.S.; Hedayat, H.; Postnova, T.I.; Golubkova, N.V.; Linli, Y.; Krajewski, S.; Strongin, A.Y.
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Homo sapiens
Savinov, A.Y.; Remacle, A.G.; Golubkov, V.S.; Krajewska, M.; Kennedy, S.; Duffy, M.J.; Rozanov, D.V.; Krajewski, S.; Strongin, A.Y.
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Homo sapiens
Yamamoto, H.; Vinitketkumnuen, A.; Adachi, Y.; Taniguchi, H.; Hirata, T.; Miyamoto, N.; Nosho, K.; Imsumran, A.; Fujita, M.; Hosokawa, M.; Hinoda, Y.; Imai, K.
Association of matrilysin-2 (MMP-26) expression with tumor progression and activation of MMP-9 in esophageal squamous cell carcinoma
Carcinogenesis
25
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2004
Homo sapiens
Marchenko, N.D.; Marchenko, G.N.; Weinreb, R.N.; Lindsey, J.D.; Kyshtoobayeva, A.; Crawford, H.C.; Strongin, A.Y.
beta-Catenin regulates the gene of MMP-26, a novel metalloproteinase expressed both in carcinomas and normal epithelial cells
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Homo sapiens
Ahokas, K.; Skoog, T.; Suomela, S.; Jeskanen, L.; Impola, U.; Isaka, K.; Saarialho-Kere, U.
Matrilysin-2 (matrix metalloproteinase-26) is upregulated in keratinocytes during wound repair and early skin carcinogenesis
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Homo sapiens
Lee, S.; Park, H.I.; Sang, Q.X.
Calcium regulates tertiary structure and enzymatic activity of human endometase/matrilysin-2 and its role in promoting human breast cancer cell invasion
Biochem. J.
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Homo sapiens
Lee, S.; Desai, K.K.; Iczkowski, K.A.; Newcomer, R.G.; Wu, K.J.; Zhao, Y.; Tan, W.W.; Roycik, M.D.; Sang, Q.A.
Coordinated peak expression of MMP-26 and TIMP-4 in preinvasive human prostate tumor
Cell Res.
16
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Homo sapiens
Skoog, T.; Ahokas, K.; Orsmark, C.; Jeskanen, L.; Isaka, K.; Saarialho-Kere, U.
MMP-21 is expressed by macrophages and fibroblasts in vivo and in culture
Exp. Dermatol.
15
775-783
2006
Homo sapiens
Pilka, R.; Oborna, I.; Lichnovsky, V.; Havelka, P.; Fingerova, H.; Eriksson, P.; Hansson, S.; Casslen, B.
Endometrial expression of the estrogen-sensitive genes MMP-26 and TIMP-4 is altered by a substitution protocol without down-regulation in IVF patients
Hum. Reprod.
21
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2006
Homo sapiens (Q9NRE1), Homo sapiens
Mellanen, L.; Lahdevirta, J.; Tervahartiala, T.; Meurman, J.H.; Sorsa, T.
Matrix metalloproteinase-7, -8, -9, -25, and -26 and CD43, -45, and -68 cell-markers in HIV-infected patients saliva and gingival tissue
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Homo sapiens
Emingil, G.; Kuula, H.; Sorsa, T.; Atilla, G.
Gingival crevicular fluid matrix metalloproteinase-25 and -26 levels in periodontal disease
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Homo sapiens
Bister, V.; Skoog, T.; Virolainen, S.; Kiviluoto, T.; Puolakkainen, P.; Saarialho-Kere, U.
Increased expression of matrix metalloproteinases-21 and -26 and TIMP-4 in pancreatic adenocarcinoma
Mod. Pathol.
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Homo sapiens
Ahokas, K.; Karjalainen-Lindsberg, M.L.; Sihvo, E.; Isaka, K.; Salo, J.; Saarialho-Kere, U.
Matrix metalloproteinases 21 and 26 are differentially expressed in esophageal squamous cell cancer
Tumour Biol.
27
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Homo sapiens
Park, H.I.; Lee, S.; Ullah, A.; Cao, Q.; Sang, Q.X.
Effects of detergents on catalytic activity of human endometase/matrilysin 2, a putative cancer biomarker
Anal. Biochem.
396
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Homo sapiens
Galewska, Z.; Romanowicz, L.; Jaworski, S.; Ba?kowski, E.
Matrix metalloproteinases, MMP-7 and MMP-26, in plasma and serum of control and preeclamptic umbilical cord blood
Eur. J. Obstet. Gynecol. Reprod. Biol.
150
152-156
2010
Homo sapiens
Souza Freitas, V.; Ferreira de Araujo, C.R.; Alves, P.M.; de Souza, L.B.; Galvao, H.C.; de Almeida Freitas, R.
Immunohistochemical expression of matrilysins (MMP-7 and MMP-26) in ameloblastomas and adenomatoid odontogenic tumors
Oral Surg. Oral Med. Oral Pathol. Oral Radiol. Endod.
108
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Homo sapiens
Zhao, Y.G.; Xiao, A.Z.; Ni, J.; Man, Y.G.; Sang, Q.X.
Expression of matrix metalloproteinase-26 in multiple human cancer tissues and smooth muscle cells
Ai Zheng
28
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Homo sapiens
Li, L.; Mei, T.H.; Zhou, X.D.; Zhang, X.G.
Expression and clinical significance of matrix metalloproteinase (MMP)-26 protein in non-small cell lung cancer
Ai Zheng
28
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Homo sapiens
Kuivanen, T.; Jeskanen, L.; Kylloenen, L.; Isaka, K.; Saarialho-Kere, U.
Matrix metalloproteinase-26 is present more frequently in squamous cell carcinomas of immunosuppressed compared with immunocompetent patients
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Homo sapiens
Deng, Y.; Li, W.; Li, Y.; Yang, H.; Xu, H.; Liang, S.; Zhang, L.; Li, Y.
Expression of Matrix Metalloproteinase-26 promotes human glioma U251 cell invasion in vitro and in vivo
Oncol. Rep.
23
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Homo sapiens
Liu, J.; Cao, B.; Li, Y.; Wu, X.; Wang, Y.
GnRH I and II up-regulate MMP-26 expression through the JNK pathway in human cytotrophoblasts
Reprod. Biol. Endocrinol.
8
5
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Homo sapiens
Gruber, H.E.; Hoelscher, G.L.; Ingram, J.A.; Hanley, E.N.
Matrix metalloproteinase-26, a novel MMP, is constitutively expressed in the human intervertebral disc in vivo and in vitro
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Homo sapiens, Homo sapiens (Q9NRE1)
Zhang, Y.; Zhao, H.; Wang, Y.; Lin, Y.; Tan, Y.; Fang, X.; Zheng, L.
Non-small cell lung cancer invasion and metastasis promoted by MMP-26
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Homo sapiens
Yang, H.; Wang, Y.; Li, Y.; Zhang, L.; Deng, Y.; Qi, D.; Li, Y.; Li, W.
Roles of matrix metalloproteinase-26 in the growth, invasion and angiogenesis of breast cancer
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Homo sapiens (Q9NRE1)
Mu, T.; Liang, W.; Ju, Y.; Wang, Z.; Wang, Z.; Roycik, M.D.; Sang, Q.X.; Yu, D.; Xiang, H.; Fang, X.
Efficient soluble expression of secreted matrix metalloproteinase 26 in Brevibacillus choshinensis
Protein Expr. Purif.
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Homo sapiens (Q9NRE1)
Xu, X.; Ma, J.; Li, C.; Zhao, W.; Xu, Y.
Regulation of chondrosarcoma invasion by MMP26
Tumour Biol.
36
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Homo sapiens (Q9NRE1), Homo sapiens
Romanowicz, L.; Gogiel, T.; Galewska, Z.; Bruczko, M.; Baczyk, J.; Roszkowska-Jakimiec, W.; Sobolewski, K.
Divergent changes in the content and activity of MMP-26 and TIMP-4 in human umbilical cord tissues associated with preeclampsia
Eur. J. Obstet. Gynecol. Reprod. Biol.
231
48-53
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Homo sapiens (Q9NRE1), Homo sapiens
Khamis, Z.I.; Iczkowski, K.A.; Man, Y.G.; Bou-Dargham, M.J.; Sang, Q.X.
Evidence for a proapoptotic role of matrix metalloproteinase-26 in human prostate cancer cells and tissues
J. Cancer
7
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Homo sapiens (Q9NRE1), Homo sapiens
Guo, J.G.; Guo, C.C.; He, Z.Q.; Cai, X.Y.; Mou, Y.G.
High MMP-26 expression in glioma is correlated with poor clinical outcome of patients
Oncol. Lett.
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Homo sapiens (Q9NRE1), Homo sapiens
Zhang, G.; Zhang, J.; Li, X.; Meng, X.; Fang, X.
Identification of the endoplasmic reticulum localization sequence and N-glycosylation of matrix metalloproteinase 26
RSC Adv.
9
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Homo sapiens (Q9NRE1)
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