Home
Drugs
Targets
Pathways
Ontologies
Cyp450s
Adv.search
Help/FAQ

Drug-Target Interaction

Drug

show drug details
PubChem ID:5362422
Structure:
Synonyms:
(2S,3R)-5-Methyl-3-(((alphaS)-alpha-(methylcarbamoyl)phenethyl)carbamoyl)-2-((2-thienylthio)methyl)hexanohydroxamic acid
(4-(N-hydroxyamino)-2-isobutyl-3-(thiophen-2-ylthiomethyl)succinyl)phenylalanine-N-methylamide
130370-60-4
1rm8
2j83
4-(N-HYDROXYAMINO)-2R-ISOBUTYL-2S-(2-THIENYLTHIOMETHYL)SUCCINYL-L-PHENYLALANINE-N-METHYLAMIDE
AIDS-043101
AIDS043101
BAT
BATIMASTAT
Batimastat (USAN/INN)
Batimastat [USAN:BAN:INN]
BB 94
BB-94
BB-99
BB94
BB94, BB-94
Butanediamide,
Butanediamide, N(sup 4)-hydroxy-N(sup 1)-(2-(methylamino)-2-oxo-1-(phenylmethyl)ethyl)-2-(2-methylpropyl)-3-((2-thienylthio)methyl)-, (2R-(1(S*),2R*,3S*))-
Butanediamide, N4-hydroxy-N1-(2-(methylamino)-2-oxo-1-(phenylmethyl)ethyl)-2-(2-methylpropyl)-3-((2-thienylthio)methyl)-, (2R-(1(S*),2R*,3S*))-
C23H31N3O4S2
D03061
DSX
ISV-120
ISV-615
LS-45637

Target

show target details
Uniprot ID:MMP14_HUMAN
Synonyms:
Matrix metalloproteinase-14
Membrane-type matrix metalloproteinase 1
Membrane-type-1 matrix metalloproteinase
MMP-14
MMP-X1
MT-MMP 1
MT1-MMP
MT1MMP
MTMMP1
EC-Numbers:3.4.24.80
Organism:Homo sapiens
Human
PDB IDs:1BQQ 1BUV 3C7X
Structure:
3C7X

Binding Affinities:

Ki: Kd:Ic 50:Ec50/Ic50:
----
--2.9-
--3-
--4.6-

References:

10686978
Neutrophil-derived serine proteinases enhance membrane type-1 matrix metalloproteinase-dependent tumor cell invasion.. P Shamamian; B J Pocock; J D Schwartz; S Monea; N Chuang; D Whiting; S G Marcus; A C Galloway; P Mignatti (2000) Surgery display abstract
BACKGROUND: Matrix metalloproteinase-2 degrades a variety of basement membrane components and is essential for tumor invasion. We have previously reported that membrane type-1 matrix metalloproteinase (MT1-MMP) cooperates with neutrophil-derived serine proteinases (NDPs; elastase, cathepsin G, protease-3) to activate matrix metalloproteinase-2. We therefore hypothesized that NDPs enhance tumor-cell invasion. METHODS: Clones of human HT1080 fibrosarcoma cells transfected with MT1-MMP sense (HT-SE) or antisense CDNA (HT-AS) were used. These cells express either high (HT-SE) or extremely low levels (HT-AS) of MT1-MMP relative to nontransfected HT1080 cells (HT-WT). The cells were incubated in the presence or absence of purified NDP, with or without alpha 1-antitrypsin or the MMP inhibitor batimastat. Cell invasion was measured with the use of Boyden chambers with polycarbonate membranes coated with a reconstituted extracellular matrix. RESULTS: Under control conditions HT-WT and HT-SE cells were 4-fold more invasive than HT-AS cells. The addition of NDP increased HT-WT and HT-SE cell invasion 60% to 100% but had no effect on HT-AS cells. alpha 1-antitrypsin or batimastat did not decrease the baseline invasiveness of HT-WT and HT-SE cells; however, they abrogated the stimulatory effect of NDP. CONCLUSIONS: HT1080 cell invasion depends on MT1-MMP expression. MT1-MMP overexpression does not increase invasiveness by itself. NDPs increase invasion by MT1-MMP expressing cells by activating matrix metalloproteinase-2.