Any feedback?
Information on EC 3.4.24.B9 - ADAM9 endopeptidase and Organism(s) Homo sapiens
for references in articles please use BRENDA:EC3.4.24.B9preliminary BRENDA-supplied EC number
Please wait a moment until all data is loaded. This message will disappear when all data is loaded.
EC Tree
3.4.24.B9 ADAM9 endopeptidaseSpecify your search results
Word Map
- 3.4.24.B9
-
adams
- metastasis
- ectodomains
- metalloproteases
- alpha-secretase
- hb-egf
- medicine
-
adam-15
-
non-amyloidogenic
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
adam9, adam-9, adam 9, mdc-9, meltrin gamma, adam metallopeptidase domain 9, mdc9/meltrin-gamma/adam9, meltrin-gamma, a disintegrin and metalloproteinase domain 9, 
more
topSYNONYM 
ORGANISM
UNIPROT
COMMENTARY 
LITERATURE
a disintegrin and metalloproteinase domain 9
ADAM9
M12.209
MDC9
meltrin-gamma
additional information
-
ADAM9 is a widely expressed and particularly polyvalent member of the multifunctional ADAM family of proteins
REACTION TYPE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
hydrolysis of peptide bond
CAS REGISTRY NUMBER
COMMENTARY
252565-22-3
-
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
beta-casein + H2O
?
-
recombinant metalloprotease domain is catalytically active against beta-casein
-
?
Fibronectin + H2O
?
-
recombinant metalloprotease domain is catalytically active against fibronectin
-
?
Gelatin + H2O
?
-
recombinant metalloprotease domain is catalytically active gelatin
-
?
Mca-PLAQAV-Dpa-RSSSR-NH2 + H2O
Mca-PLAQA + V-Dpa-RSSSR-NH2
-
quenched fluorescent substrate
-
?
transmembrane collagen XVII + H2O
soluble collagen ectodomain
-
substrate protein is an endothelial adhesion molecule on the surface of keratinocytes, protein is shed from the cell surface
cells show altered motility
?
amyloid precursor protein + H2O
?
-
enzyme shows alpha-secretase activity
-
?
amyloid precursor protein + H2O
?
enzyme shows alpha-secretase activity
-
?
amyloid precursor protein + H2O
?
-
enzyme shows alpha-secretase activity, the alpha-secretase might be composed of several ADAM enzymes in a complexe
-
?
proteins + H2O
peptides
enzymes of the ADAM family play importants roles in cell-cell fusion, intracellular signaling, and other cellular functions
-
?
additional information
?
-
-
interaction with endophilin I and SH3PX1, a SH3 domain- and phox homolog domain-containing protein, which may have a regulatory role by inhibiting the processing of the enzyme
-
?
additional information
?
-
-
the enzyme interacts in a RGD motif-independent manner with the alphaVbeta5-domain of integrins, e.g. on the surface of myeloma but not lymphoblastoid cells, dependent on cations Ca2+ or Mn2+
-
?
additional information
?
-
-
potential ADAM-9 sheddase substrates include growth factors and cytokines, which have been linked to atherosclerosis
-
-
?
additional information
?
-
-
ADAM-9 is capable of binding to alpha6beta1 and alphanubeta5 integrins
-
-
?
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
amyloid precursor protein + H2O
?
-
enzyme shows alpha-secretase activity, the alpha-secretase might be composed of several ADAM enzymes in a complexe
-
?
transmembrane collagen XVII + H2O
soluble collagen ectodomain
-
substrate protein is an endothelial adhesion molecule on the surface of keratinocytes, protein is shed from the cell surface
cells show altered motility
?
proteins + H2O
peptides
enzymes of the ADAM family play importants roles in cell-cell fusion, intracellular signaling, and other cellular functions
-
?
additional information
?
-
-
interaction with endophilin I and SH3PX1, a SH3 domain- and phox homolog domain-containing protein, which may have a regulatory role by inhibiting the processing of the enzyme
-
?
additional information
?
-
-
the enzyme interacts in a RGD motif-independent manner with the alphaVbeta5-domain of integrins, e.g. on the surface of myeloma but not lymphoblastoid cells, dependent on cations Ca2+ or Mn2+
-
?
additional information
?
-
-
potential ADAM-9 sheddase substrates include growth factors and cytokines, which have been linked to atherosclerosis
-
-
?
METALS and IONS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
interaction of the enzyme with integrins is dependent on Ca2+ or Mn2+
INHIBITOR
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
Hydroxamates
-
metalloprotease inhibitors, derivatives FN-439, BB3103, BB 3241, and IC-3
additional information
-
interaction of the enzyme with integrins is inhibited by antibodies against the alphaVbeta5-domain of integrin
-
additional information
-
no inhibition by the metalloprotease inhibitors TIMP-1, -2, and -4
-
ACTIVATING COMPOUND
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
IMAGE
stanolone
-
upregulation, 1.5fold increase in activity at 0.000001 mM, 1.7fold at 0.00001 mM
SPECIFIC ACTIVITY [µmol/min/mg]
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
pH OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
TEMPERATURE OPTIMUM
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
37
ORGANISM
COMMENTARY
LITERATURE
UNIPROT
SEQUENCE DB
SOURCE
-
644075, 649562, 651308, 651956, 653225, 653737, 668073, 668145, 668152, 668164, 668979, 677587, 680831, 682830, 710800, 710868, 712114, 719607, 719997
-
-
native short form of ADAM9 lacking the transmembrane and the cytoplasmic domains due to a deletion in the EGF-like domain
SwissProt
SOURCE TISSUE
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
SOURCE
-
carotid and femoral arteries, only weak ADAM-9 expression from thyroid artery without atherosclerosis
-
grade 3, CIN lesions are premalignant changes
-
lung cancer cell line, enzyme mRNA levels are significantly higher in highly brain-metastatic sublines than in the parent or highly bone-metastatic sublines
-
synovial membrane-like interface tissue is collected from the proximal bone-cement or bone-stem interfaces around aseptically loosened femoral stems
-
cells secrete a alternatively spliced variant of enzyme promoting carcinoma invasion
expression of full length and short enzyme form, with higher level of the short form than in other tissues
-
in advanced human atherosclerotic plaques of aorta and carotid and femoral arteries, high expression level
-
ADAM-9 is expressed in human melanoma at the tumor-stroma border where direct or indirect interactions between tumor cells and fibroblasts occur
-
stromal liver myofibroblast, enzyme expression particularly by cells localized within the tumor stroma at the invasive front
-
recombinant enzyme promotes a fivefold increase in interleukin IL-6, but not IL-1beta mRNA. Enzyme binds directly to alphabeta5 integrin
-
elevated level of enzyme in malignant compared to benign tissue. Increase in enzyme protein and mRNA upon exposure of prostate cells to stress conditions. Inhibition of stress-induction of enzyme by actinomycin D and cycloheximide
-
in normal epithelium, CIN3 lesions, and squamous cell carcinomas
additional information
-
prostate cancer cell, elevated level of enzyme during the transition of cells from androgen-dependent to androgen-independent and metastatic state. Induction of enzyme is abrogated by the antioxidant ebselen or the enzyme catalase
additional information
-
study on several human skin melanoma and melanoma cell lines. In melanoma, enzyme expression is restricted to the melanoma cells within the invading front. Enzyme is detected in melanoma cells and in peritumoral stromal fibroblasts, but absent in fibroblasts distal to the tumor site. In melanoma cell lines, enzyme is expressed in varying amounts in all cell lines studied. Downregulation of enzyme expression upon culture of cells within 3-dimensional latticies of fibrillar type I collagen, but not in the polysaccharide alginate
additional information
-
ADAM9 expression is low in the squamous epithelium of the cervix, but is increased in CIN3 lesions as well as squamous cell carcinomas, only weak expression of ADAM9 in the normal cervical epithelium
LOCALIZATION
ORGANISM
UNIPROT
COMMENTARY
GeneOntology No.
LITERATURE
SOURCE
GENERAL INFORMATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
malfunction
-
silencing of ADAM-9 in melanoma cells significantly reduces cell adhesion to fibroblasts. Ablation of ADAM-9 in fibroblasts almost completely abolishes these cellular interactions and melanoma cell invasion in vitro
physiological function
additional information
physiological function
-
ADAM-9 interaction with alpha6beta1 integrin regulates fibroblast motility, and alpha6beta1 integrin can induce the mobility of several cell types including macrophages. ADAM-9 is involved in advanced human atherosclerosis and might play roles in the monocyte homing, migration, or proliferation in aorta, carotid, and femoral arteries. ADAM-9 is also involved both in ectodomain shedding and cell interactions through integrin binding. Potential ADAM-9 sheddase substrates include growth factors and cytokines, which are linked to atherosclerosis
physiological function
-
ADAM9 is a member of the ADAM family which is involved in cellular processes like cell adhesion, migration and signalling, involvement of this protease in cervical carcinogenesis, overview
physiological function
-
fibroblasts adhere to the adhesive domains of ADAM-9 in the presence of Mn2+ ions. ADAM-9 expression plays an important role in mediating cell-cell contacts between fibroblasts and melanoma cells. These interactions contribute to proteolytic activities required during invasion of melanoma cells
physiological function
-
the enzyme is implicated in auto and paracrine regulation of invasiveness in A-549 cells
physiological function
aberrant overexpression of ADAM9 is found in both gastric cancer tissues and cell lines. Knockdown of ADAM9 in gastric cancer SGC-7901 cells induces a dramatic suppression of cell proliferation along with the arrest of the cell cycle in the G0/G1 phase. The 3' untranslated region of ADAM9 mRNA may be bound by miR-126, a suppressor in gastric cancer. Overexpression of miR-126 significantly downregulates ADAM9 in the gastric cancer cells
physiological function
ADAM9 enhances the expression of the pro-migratory protein CDCP1 to promote lung metastasis. Endogenous miR-218, which is abundant in normal lung tissue but suppressed in lung tumors, is regulated during the process of ADAM9-mediated CDCP1 expression. Suppression of miR-218 is associated with high migration ability in lung cancer cells
physiological function
cells lacking ADAM9 show a significant reduction in infection efficiency by encephalomyocarditis virus EMCV. Pharmacological inhibition of the metalloproteinase activity of ADAM9 does not affect virus infection. Reconstitution of inactive ADAM9 in knockout cells restores susceptibility to EMCV. ADAM9 facilitates attachment of EMCV to the cell surface
additional information
-
ADAM9 is a widely expressed and particularly polyvalent member of the multifunctional ADAM family of proteins
additional information
-
promoter polymorphisms, which regulate ADAM9 transcription, are protective against sporadic Alzheimer's disease
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). ADAM9_HUMAN
819
0
90556
Swiss-Prot
other Location (Reliability: 2)
MOLECULAR WEIGHT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
110000
-
x * 79000, processed mature enzyme, SDS-PAGE, x * 110000, enzyme proform, SDS-PAGE
79000
-
x * 79000, processed mature enzyme, SDS-PAGE, x * 110000, enzyme proform, SDS-PAGE
80000
SUBUNIT
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
-
enzyme binds directly to alpha6beta4 and alpha2beta1 integrins through the disintegrin domain
?
-
x * 79000, processed mature enzyme, SDS-PAGE, x * 110000, enzyme proform, SDS-PAGE
POSTTRANSLATIONAL MODIFICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
proteolytic modification
proteolytic modification
-
cleavage by furin-like endopeptidase, also the recombinant enzyme is cleaved in Pichia pastoris
proteolytic modification
-
cleavage of prodomain by furin, interaction with endophilin I and SH3PX1, a SH3 domain- and phox homolog domain-containing protein, which may have a regulatory role by inhibiting the processing of the enzyme
PROTEIN VARIANTS
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
additional information
additional information
-
construction of a GST-enzyme disintegrin domain fusion protein
additional information
-
enzyme expression in tumor cell lines induces a highly invasive phenotype, protease activity of enzyme is required for invasion
additional information
-
identification of null mutations in the ADAM metallopeptidase domain 9, ADAM9, gene in four consanguineous families with recessively inherited early-onset cone-rod dystrophy, a group of genetically and phenotypically heterogenous retinal disorders, which is an inherited progressive retinal dystrophy affecting the function of cone and rod photoreceptors, phenotype, overview
additional information
-
screening of the ADAM9 gene promoter region identifies four polymorphisms: -542C/T (rs10105311), -600A/C (rs7840270), -963A/G (rs6991968) and -1314T/C (rs7006414), genotyping and phenotyping, overview. Both -963G/-1314C and -963A/-1314C have 1.5-1.8fold and 1.4-1.7fold higher transcriptional activity, respectively, than -963A/-1314T
PURIFICATION (Commentary)
ORGANISM
UNIPROT
LITERATURE
CLONED (Commentary)
ORGANISM
UNIPROT
LITERATURE
ADAM9 gene, DNA and amino acid sequence determination and analysis, screening and analysis of the promoter region, expression of mutants iin SH-SY5Y and HeLa cells
-
DNA sequence determination and analysis, expression of the short enzyme form, lacking the transmembrane and the cytoplasmic domains due to a deletion in the EGF-like domain, in COS cells, coexpression of amyloid precursor protein
expression of GST-enzyme disintegrin domain fusion protein Escherichia coli strain BL21
-
expression of GST-fusion cytoplasmic enzyme domain in a two-hybrid system in Saccharomyces cerevisiae strain HF7c
-
expression of the metalloprotease domain in Pichia pastoris, processing and secretion to the medium
-
EXPRESSION
ORGANISM
UNIPROT
LITERATURE
3 h exposure to 1 mM H2O2 induces ADAM9 expression and ADAM-specific metalloprotease activity in A549 cells
-
APPLICATION
ORGANISM
UNIPROT
COMMENTARY
LITERATURE
medicine
medicine
-
all three enzymes ADAM9, ADAM12, and ADAM15 are significantly upregulated in gastric cancer compared to non-neoplastic foveolar epithelium. Anti-ADAM9 and anti-ADAM15 antibodies inhibit cell growth
medicine
-
elevated level of enzyme in malignant compared to benign prostate tissue. Increase in enzyme protein and mRNA upon exposure of prostate cells to stress conditions. Inhibition of stress-induction of enzyme by actinomycin D and cycloheximide. Decrease of enzyme expression results in apoptotic cell death in prostate cancer cells
medicine
-
in melanoma, enzyme expression is restricted to the melanoma cells within the invading front. Enzyme is detected in melanoma cells and in peritumoral stromal fibroblasts, but absent in fibroblasts distal to the tumor site. In melanoma cell lines, enzyme is expressed in varying amounts in all cell lines studied. Downregulation of enzyme expression upon culture of cells within 3-dimensional latticies of fibrillar type I collagen, but not in the polysaccharide alginate
medicine
-
lung cancer cell line EBC-1, enzyme mRNA levels are significantly higher in highly brain-metastatic sublines than in the parent or highly bone-metastatic sublines
medicine
-
secreted form of enzyme promotes carcinoma invasion through tumor-stromal interactions
medicine
-
significantly higher level of enzyme expression in malignant plasma cells than in other cell populations present in bone marrow
medicine
aberrant overexpression of ADAM9 is found in both gastric cancer tissues and cell lines. The expression of ADAM9 is significantly correlated with patient clinicopathological features including tumor size, local invasion, lymph node metastasis and tumor-node-metastasis stage. Knockdown of ADAM9 in gastric cancer SGC-7901 cells, which present the highest ADAM9 expression among the cell lines, induces a dramatic suppression of cell proliferation along with the arrest of the cell cycle in the G0/G1 phase. The 3' untranslated region of ADAM9 mRNA may be bound by miR-126, a suppressor in gastric cancer. Overexpression of miR-126 significantly downregulates ADAM9 in the gastric cancer cells
medicine
ADAM9 enhances the expression of the pro-migratory protein CDCP1 to promote lung metastasis. Endogenous miR-218, which is abundant in normal lung tissue but suppressed in lung tumors, is regulated during the process of ADAM9-mediated CDCP1 expression. Suppression of miR-218 is associated with high migration ability in lung cancer cells
medicine
ADAM9 staining is increased in lung epithelial cells and macrophages in smokers and even more so in patients with chronic obstructive pulmonary disease COPD. ADAM9 staining correlates directly with pack-year smoking history and inversely with airflow obstruction and/or FEV1 percent predicted. Bronchial epithelial cell ADAM9 mRNA levels are higher in patients with COPD than control subjects and correlate directly with pack-year smoking history
medicine
cells lacking ADAM9 show a significant reduction in infection efficiency by encephalomyocarditis virus EMCV. Pharmacological inhibition of the metalloproteinase activity of ADAM9 does not affect virus infection. Reconstitution of inactive ADAM9 in knockout cells restores susceptibility to EMCV. ADAM9 facilitates attachment of EMCV to the cell surface
REF.
AUTHORS
TITLE
JOURNAL
VOL.
PAGES
YEAR
ORGANISM (UNIPROT)
PUBMED ID
SOURCE
Boeckmann, B.; Bairoch, A.; Apweiler, R.; Blatter, M.C.; Estreicher, A.; Gasteiger, E.; Martin M.J.; Michoud, K.; O'Donovan, C.; Phan, I.; Pilbout, S.; Schneider, M.
The SWISS-PROT protein knowledgebase and its supplement TrEMBL
Nucleic Acids Res.
31
365-370
2003
Homo sapiens (Q13443), Mus musculus (Q61072)
Asai, M.; Hattori, C.; Szabo, B.; Sasagawa, N.; Maruyama, K.; Tanuma, S.I.; Ishiura, S.
Putative function of ADAM9, ADAM10, and ADAM17 as APP alpha-secretase
Biochem. Biophys. Res. Commun.
301
231-235
2003
Homo sapiens
Zhou, M.; Graham, R.; Russell, G.; Croucher, P.I.
MDC-9 (ADAM-9/Meltrin gamma) functions as an adhesion molecule by binding the alpha(v)beta(5) integrin
Biochem. Biophys. Res. Commun.
280
574-580
2001
Homo sapiens
Hotoda, N.; Koike, H.; Sasagawa, N.; Ishiura, S.
A secreted form of human ADAM9 has an alpha-secretase activity for APP
Biochem. Biophys. Res. Commun.
293
800-805
2002
Homo sapiens (Q13443), Homo sapiens
Amour, A.; Knight, C.G.; English, W.R.; Webster, A.; Slocombe, P.M.; Knauper, V.; Docherty, A.J.; Becherer, J.D.; Blobel, C.P.; Murphy, G.
The enzymatic activity of ADAM8 and ADAM9 is not regulated by TIMPs
FEBS Lett.
524
154-158
2002
Homo sapiens
Howard, L.; Nelson, K.K.; Maciewicz, R.A.; Blobel, C.P.
Interaction of the metalloprotease disintegrins MDC9 and MDC15 with two SH3 domain-containing proteins, endophilin I and SH3PX1
J. Biol. Chem.
274
31693-31699
1999
Homo sapiens, Mus musculus
McCulloch, D.R.; Harvey, M.; Herington, A.C.
The expression of the ADAMs proteases in prostate cancer cell lines and their regulation by dihydrotestosterone
Mol. Cell. Endocrinol.
167
11-21
2000
Homo sapiens
Schwettmann, L.; Tschesche, H.
Cloning and expression in Pichia pastoris of metalloprotease domain of ADAM 9 catalytically active against fibronectin
Protein Expr. Purif.
21
65-70
2001
Homo sapiens
Karadag, A.; Zhou, M.; Croucher, P.I.
ADAM-9 (MDC-9/meltrin-gamma), a member of the a disintegrin and metalloproteinase family, regulates myeloma-cell-induced interleukin-6 production in osteoblasts by direct interaction with the alpha(v)beta5 integrin
Blood
107
3271-3278
2006
Homo sapiens
Shintani, Y.; Higashiyama, S.; Ohta, M.; Hirabayashi, H.; Yamamoto, S.; Yoshimasu, T.; Matsuda, H.; Matsuura, N.
Overexpression of ADAM9 in non-small cell lung cancer correlates with brain metastasis
Cancer Res.
64
4190-4196
2004
Homo sapiens, Mus musculus
Mazzocca, A.; Coppari, R.; De Franco, R.; Cho, J.; Libermann, T.A.; Pinzani, M.; Toker, A.
A secreted form of ADAM9 promotes carcinoma invasion through tumor-stromal interactions
Cancer Res.
65
4728-4738
2005
Homo sapiens
Sung, S.; Kubo, H.; Shigemura, K.; Arnold, R.S.; Logani, S.; Wang, R.; Konaka, H.; Nakagawa, M.; Mousses, S.; Amin, M.; Anderson, C.; Johnstone, P.; Petros, J.A.; Marshall, F.F.; Zhau, H.E.; Chung, L.W.
Oxidative stress induces ADAM9 protein expression in human prostate cancer cells
Cancer Res.
66
9519-9526
2006
Homo sapiens
Zigrino, P.; Mauch, C.; Fox, J.W.; Nischt, R.
Adam-9 expression and regulation in human skin melanoma and melanoma cell lines
Int. J. Cancer
116
853-859
2005
Homo sapiens
Carl-McGrath, S.; Lendeckel, U.; Ebert, M.; Roessner, A.; Roecken, C.
The disintegrin-metalloproteinases ADAM9, ADAM12, and ADAM15 are upregulated in gastric cancer
Int. J. Oncol.
26
17-24
2005
Homo sapiens
Yamada, D.; Ohuchida, K.; Mizumoto, K.; Ohhashi, S.; Yu, J.; Egami, T.; Fujita, H.; Nagai, E.; Tanaka, M.
Increased expression of ADAM 9 and ADAM 15 mRNA in pancreatic cancer
Anticancer Res.
27
793-799
2007
Homo sapiens
Zigrino, P.; Steiger, J.; Fox, J.W.; Loeffek, S.; Schild, A.; Nischt, R.; Mauch, C.
Role of ADAM-9 disintegrin-cysteine-rich domains in human keratinocyte migration
J. Biol. Chem.
282
30785-30793
2007
Homo sapiens
Ma, G.F.; Liljestroem, M.; Ainola, M.; Chen, T.; Tiainen, V.M.; Lappalainen, R.; Konttinen, Y.T.; Salo, J.
Expression of ADAM9 (meltrin-gamma) around aseptically loosened total hip replacement implants
Rheumatology
45
808-814
2006
Homo sapiens
Parry, D.A.; Toomes, C.; Bida, L.; Danciger, M.; Towns, K.V.; McKibbin, M.; Jacobson, S.G.; Logan, C.V.; Ali, M.; Bond, J.; Chance, R.; Swendeman, S.; Daniele, L.L.; Springell, K.; Adams, M.; Johnson, C.A.; Booth, A.P.; Jafri, H.; Rashid, Y.; Banin, E.; Strom, T.M.; Farber, D.B.; Sharon, D.; Blobel, C.P.; Pugh, E.
Loss of the metalloprotease ADAM9 leads to cone-rod dystrophy in humans and retinal degeneration in mice
Am. J. Hum. Genet.
84
683-691
2009
Homo sapiens, Mus musculus
Oksala, N.; Levula, M.; Airla, N.; Pelto-Huikko, M.; Ortiz, R.M.; Jaervinen, O.; Salenius, J.P.; Ozsait, B.; Komurcu-Bayrak, E.; Erginel-Unaltuna, N.; Huovila, A.P.; Kytoemaeki, L.; Soini, J.T.; Kaehoenen, M.; Karhunen, P.J.; Laaksonen, R.; Lehtimaeki, T.
ADAM-9, ADAM-15, and ADAM-17 are upregulated in macrophages in advanced human atherosclerotic plaques in aorta and carotid and femoral arteries--Tampere vascular study
Ann. Med.
41
279-290
2009
Homo sapiens
Zubel, A.; Flechtenmacher, C.; Edler, L.; Alonso, A.
Expression of ADAM9 in CIN3 lesions and squamous cell carcinomas of the cervix
Gynecol. Oncol.
114
332-336
2009
Homo sapiens
Cong, L.; Jia, J.
Promoter polymorphisms which regulate ADAM9 transcription are protective against sporadic Alzheimers disease
Neurobiol. Aging
32
54-62
2009
Homo sapiens
Mongaret, C.; Alexandre, J.; Thomas-Schoemann, A.; Bermudez, E.; Chereau, C.; Nicco, C.; Goldwasser, F.; Weill, B.; Batteux, F.; Lemare, F.
Tumor invasion induced by oxidative stress is dependent on membrane ADAM 9 protein and its secreted form
Int. J. Cancer
129
791-798
2011
Homo sapiens
Zigrino, P.; Nischt, R.; Mauch, C.
The disintegrin-like and cysteine-rich domains of ADAM-9 mediate interactions between melanoma cells and fibroblasts
J. Biol. Chem.
286
6801-6807
2011
Homo sapiens
Wang, X.; Polverino, F.; Rojas-Quintero, J.; Zhang, D.; Sánchez, J.; Yambayev, I.; Lindqvist, E.; Virtala, R.; Djukanovic, R.; Davies, D.; Wilson, S.; ODonnell, R.; Cunoosamy, D.; Hazon, P.; Higham, A.; Singh, D.; Olsson, H.; Owen, C.
A disintegrin and metalloproteinase domain-9 A novel proteinase culprit with multifarious contributions to chronic obstructive pulmonary disease
Am. J. Respir. Crit. Care Med.
198
1500-1518
2018
Mus musculus, Homo sapiens (Q13443)
-
Baggen, J.; Jan Thibaut, H.; Hurdiss, D.; Wahedi, M.; Van Vliet, A.; Van Kuppeveld, F.
Identification of the cell-surface protease adam9 as an entry factor for encephalomyocarditis virus
mBio
10
e1780
2019
Homo sapiens (Q13443), Homo sapiens
Wang, J.; Zhou, Y.; Fei, X.; Chen, X.; Yan, J.; Liu, B.; Zhu, Z.
ADAM9 functions as a promoter of gastric cancer growth which is negatively and post-transcriptionally regulated by miR-126
Oncol. Rep.
37
2033-2040
2017
Homo sapiens (Q13443)
EXTERNAL LINKS (specific for EC-Number 3.4.24.B9)
Use of this online version of BRENDA is free under the CC BY 4.0 license. See terms of use for full details.
Release 2023.1 (January 2023)
Legal
Curated at
Member of
