Search results for MMP9

Showing 16 results out of 49

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Species

Types

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Protein (4 results from a total of 8)

Identifier: R-HSA-6800973
Species: Homo sapiens
Compartment: ficolin-1-rich granule lumen
Primary external reference: UniProt: MMP9: P14780
Identifier: R-HSA-6800181
Species: Homo sapiens
Compartment: tertiary granule lumen
Primary external reference: UniProt: P14780
Identifier: R-HSA-1604726
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP9: P14780
Identifier: R-HSA-668812
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP9: P14780

Interactor (1 results from a total of 1)

Identifier: EBI-2677274
Species: Homo sapiens
Primary external reference: IntAct: EBI-2677274

DNA Sequence (1 results from a total of 1)

Identifier: R-HSA-8948369
Species: Homo sapiens
Compartment: nucleoplasm
Primary external reference: ENSEMBL: ENSG00000100985

Set (4 results from a total of 5)

Identifier: R-HSA-3928502
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2559546
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-3827999
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2533968
Species: Homo sapiens
Compartment: extracellular region

Reaction (4 results from a total of 32)

Identifier: R-HSA-8943959
Species: Homo sapiens
Compartment: plasma membrane
Signal peptide-CUB-EGF-like domain-containing protein 3 (SCUBE3) is a secreted glycoprotein that is highly expressed in osteoblasts. It can form homooligomers and heterooligomers with SCUBE1, which stably associate with the peripheral cell surface. In normal lung it is mainly expressed in bronchial epithelial cells. Its expression is upregulated in some lung cancer tumors and correlates with invasive ability in a lung cancer cell line model (Wu et al. 2004, 2011). SCUBE3 knockdown is associated with lower tumor vascular permeability, inhibiting the metastatic potential of Non-small-cell lung carcinoma (Chou et al. 2013).

SCUBE3 can be cleaved by the gelatinases Matrix metalloprotease-2 (MMP2) and MMP9, releasing two major fragments. The C-terminal fragment contains a complement proteins C1r/C1s, Uegf and Bmp1 (CUB) domain. The secreted SCUBE3 protein and the C-terminal CUB domain fragment can bind the Transforming growth factor beta type II receptor (TGFBR2) and activate signaling (Wu et al. 2011). SCUBE3 may act as an FGF co-receptor, augmenting FGF8 signaling (Tu et al. 2014) . Overexpressesion of Scube3 has been linked to significant murine cardiac hypertrophy (Yang et al. 2007). The C-terminal portion of SCUBE3 can physically interact with Transforming growth factor beta-1 (TGFB1) and promote TGFB1-mediated transcriptional activation in vitro (Yang et al. 2007). Consistent with this, the phosphorylated and total protein levels of Smad2, a well-known TGFB1 downstream signaling molecule, are elevated in Scube3 transgenic mouse heart under pressure overload. SCUBE3 may be a component of the regulatory mechanisms for active TGFB1 bioavailability, either systemically or locally in cardiac tissues, under baseline conditions and during pathological stresses. A Scube3 mutant mouse line (carrying a missense mutation in exon 8) has phenotypic alterations that suggest a role of Scube3 in bone metabolism and morphology, hearing, and renal function. The observed morphological abnormalities of the skeleton, impaired bone metabolism and hearing impairments are comparable with the rare metabolic bone disorder Paget disease, which is associated with the chromosomal region that includes SCUBE3 (Fuchs et al. 2016).
Identifier: R-HSA-1604690
Species: Homo sapiens
Compartment: extracellular region
The intermediate form of MMP9 is activated by cleavage of the Arg106-Phe107 peptide bond producing the fullly active 82-kDa MMP-9 species (Ogata et al. 1992, Fridman et al. 1995).
Identifier: R-HSA-1454791
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
Certain normally extracellular MMPs can transiently localize at the cell periphery in association with adhesion receptors or proteoglycans. ProMMP9, MMP9, MMP2 and MMP7 (Ahmed et al. 2002, Samanna et al. 2006, Yu et al. 2002) localize at the cell membrane with the single-pass transmembrane glycoprotein CD44, known to be involved in hyaluronan-cell interactions, lymphocyte homing and cell adhesion (Toole 1990). Membrane-associated MMP7 can bring about the shedding of several membrane proteins such as epidermal growth factor (EGF), soluble Fas ligand (FasL), E-cadherin and TNF-alpha from their membrane-bound precursors, thereby promoting cancer progression (Li et al. 2006). MMP9 is able to cleave CD44, inhibiting cell migration and reducing the malignant potential of tumour cells (Chetty et al. 2012).
Identifier: R-HSA-2168982
Species: Homo sapiens
Compartment: extracellular region
Type XVI collagen is a member of the FACIT collagen family (fibril-associated collagens with interrupted helices). During early mouse development, it occurs in many tissues and is co-distributed with the major fibrillar collagens (Lai & Chu 1996). In skin, collagen XVI preferentially occurs in narrow zones near basement membranes at the dermo-epidermal junction (DEJ) of blood vessels (Grässel et al., 1999). In papillary dermis, the protein unexpectedly does not occur in banded collagen fibrils, but is a component of specialized fibrillin-1-containing microfibrils. However, in cartilage matrix it does not aggregate with fibrillin-1, rather it exists as a discrete population of thin, weakly banded collagen fibrils in association with collagens II and XI (Kassner et al. 2003, 2004). Collagen XVI induces the recruitment of integrins alpha1 beta1 and alpha1 beta 2 into focal adhesion plaques, a principal step in integrin signaling (Eble et al. 2006), allowing cells to affect the architecture of the ECM networks by binding and moving ECM proteins.

Collagen type XVI is cleaved by MMP9 (Sires et al. 1995).

Complex (1 results from a total of 1)

Identifier: R-HSA-2559499
Species: Homo sapiens
Compartment: plasma membrane

Pathway (1 results from a total of 1)

Identifier: R-HSA-5687128
Species: Homo sapiens
MAPK6 and MAPK4 (also known as ERK3 and ERK4) are vertebrate-specific atypical MAP kinases. Atypical MAPK are less well characterized than their conventional counterparts, and are generally classified as such based on their lack of activation by MAPKK family members. Unlike the conventional MAPK proteins, which contain a Thr-X-Tyr motif in the activation loop, MAPK6 and 4 have a single Ser-Glu-Gly phospho-acceptor motif (reviewed in Coulombe and Meloche, 2007; Cargnello et al, 2011). MAPK6 is also distinct in being an unstable kinase, whose turnover is mediated by ubiquitin-dependent degradation (Coulombe et al, 2003; Coulombe et al, 2004). The biological functions and pathways governing MAPK6 and 4 are not well established. MAPK6 and 4 are phosphorylated downstream of class I p21 activated kinases (PAKs) in a RAC- or CDC42-dependent manner (Deleris et al, 2008; Perander et al, 2008; Deleris et al, 2011; De La Mota-Peynado et al, 2011). One of the only well established substrates of MAPK6 and 4 is MAPKAPK5, which contributes to cell motility by promoting the HSBP1-dependent rearrangement of F-actin (Gerits et al, 2007; Kostenko et al, 2009a; reviewed in Kostenko et al, 2011b). The atypical MAPKs also contribute to cell motility and invasiveness through the NCOA3:ETV4-dependent regulation of MMP gene expression (Long et al, 2012; Yan et al, 2008; Qin et al, 2008). Both of these pathways may be misregulated in human cancers (reviewed in Myant and Sansom, 2011; Kostenko et al, 2012)
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