Search results for MMP7

Showing 19 results out of 38

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Protein (6 results from a total of 6)

Identifier: R-HSA-1604766
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP7: P09237
Identifier: R-HSA-1604760
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP7: P09237
Identifier: R-HSA-1604759
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP7: P09237
Identifier: R-HSA-1604729
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP7: P09237
Identifier: R-HSA-1604734
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP7: P09237
Identifier: R-HSA-1442479
Species: Homo sapiens
Compartment: extracellular region
Primary external reference: UniProt: MMP7: P09237

Set (5 results from a total of 5)

Identifier: R-HSA-2533973
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2534228
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-1604762
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2559546
Species: Homo sapiens
Compartment: extracellular region
Identifier: R-HSA-2534258
Species: Homo sapiens
Compartment: extracellular region

Reaction (7 results from a total of 26)

Identifier: R-HSA-1604763
Species: Homo sapiens
Compartment: extracellular region
Once cleaved at Lys50-Asn51 MMP7 undergoes autocatalysis (Crabbe et al. 1992). Highly sulfated glycosaminoglycans (GAG), such as heparin, chondroitin-4,6-sulfate (CS-E), and dermatan sulfate, markedly enhance (>50-fold) the intermolecular autolytic activation of promatrilysin and the activity of fully active matrilysin (Ra et al. 2009).
Identifier: R-HSA-8940561
Species: Homo sapiens
Compartment: extracellular region
Opticin (OPTC) is a a member of the small leucine-rich repeat proteoglycan family (Reardon et al. 2000). It is found in the vitreous cavity of the eye where it co-localizes with the fine network of collagen fibrils that maintains the gel state of the vitreous and the inner-limiting lamina, and in other tissues, including the brain, heart, and cartilage (Le Goff et al. 2012). It forms a homodimer in solution through its leucine-rich repeats (Le Goff et al. 2003). OPTC has anti-angiogenic activity which is mediated by binding to vitreous collagen fibrils, which are composed of collagens II, IX, and V/XI (Bishop 2000). This binding competitively inhibits endothelial cell interactions with collagen I via Alpha-1Beta-1and Alpha-2Beta-1 integrins, preventing proangiogenic signaling via these integrins (Le Goff et al. 2012). OPTC is expressed and translocated to the nucleus of chronic lymphocytic leukemia cells (Mikaelsson et al.2013).

OPTC can be degraded by Matrix metalloprotease (MMP) -1, -2, -3, -7, -8, -9, -13 and by ADAMTS-4 and ADAMTS-5, with MMP2 and MMP7 having highest activity towards the recombinant protein (Montfort et al. 2008, Ma et al. 2012, Tio et al. 2014). MMP7 cleaves recombinant human OPTN at four positions, A20/S21LP (removing the signal peptide), E32/Q33, T87/S88, and G114/L115.
Identifier: R-HSA-4086205
Species: Homo sapiens
Compartment: extracellular region
OPN is a substrate for MMP3 and MMP7. Three cleavage sites were identified, Gly166-Leu167, Ala201-Tyr202 (MMP-3 only), and Asp210-Leu211. The resulting OPN fragments facilitate adhesion and migration in vitro through activation of beta1-containing integrins (Agnihotri et al. 2001). OPN has also been shown to be a substrate for liver transglutaminase and plasma transglutaminase factor IIIa, resulting in protein crosslinking (Prince et al. 1991), enhanced cell adhesion, spreading, focal contact formation and migration
Identifier: R-HSA-1454843
Species: Homo sapiens
Compartment: plasma membrane, extracellular region
E-cadherin (CDH1) localizes to the lateral membrane of differentiated epithelia, providing the structural foundation for adherens junctions, multiprotein complexes that link cell-cell contacts to the actin cytoskeleton and various signaling molecules (Perez-Moreno et al. 2003, Baum & Georgiou 2011). The extracellular domain has five cadherin-type repeat ectodomain (EC) modules; the most membrane-distal EC mediates binding with CDH1 on adjacent cells (Boggon et al. 2002). Calcium ions bind between the EC domains of two CDH1 peptides to form a dimer with a rod-like conformation (Boggon et al. 2002) which is required for cell-cell interaction (Gumbiner 1996, Patel et al. 2006). The cytoplasmic tail of E-cadherin binds to the armadillo repeat protein beta-catenin, a target of the Wnt signaling pathway and a cofactor for TCF/LEF-mediated transcription (Gavard & Mège 2005). Beta-catenin in turn binds alpha-catenin, which interacts with the actin microfilament network, actin and the actin-binding proteins vinculin, formins, alpha-actinin, zonula occludin protein, and afadin (Bershadsky 2004). Cell–cell adhesions also contain desmosomes, which link cell contacts to intermediate filaments, and nectin-based, calcium-independent adhesions, which are linked to actin (Takai & Nakanishi 2003, Yin and Green 2004). The critical importance of E-cadherin to normal development and tissue function is demonstrated by embryonic lethal E-cadherin gene mouse knockouts (Larue et al. 1994). Loss of cadherin-based cell-cell adhesion is a hallmark of carcinogenesis, correlating with tumour progression, allowing cells to escape normal growth control signals, resulting in loss of differentiation and increased cell proliferation associated with invasive behaviour (Frixen et al. 1991, Capaldo & Macara 2007). Full-length 120-kDa CDH1 protein is cleaved in the ectodomain close to the plasma membrane by a number of metalloproteases, generating an extracellular 38-kDa C-terminal fragment (CTF) termed CTF1 which can be further processed by a gamma-secretase-like activity to a soluble 33-kDa CTF2 (Marambaud et al. 2002, Roy & Berx 2008). MMP3, MMP7 (Noë et al. 2001, canine MMPs), MMP9 (Symowicz et al. 2007), plasmin (Ryniers et al. 2002, canine plasmin), Kallikrien 7 (Johnson et al. 2007), ADAM10 (Maretzky et al. 2005) and ADAM15 (Najy et al. 2008) all cleave CDH1 extracellularly, close to the transmembrane region. Presenilin-1 (Marambaud et al. 2002), the catalytic subunit of gamma-secretase (Herreman et al. 2003, Li et al. 2003), cleaves CDH1 producing a soluble 33-kDa fragment termed CTF2. Other enzymes like caspase-3 (Steinhusen et al. 2001) and calpain-1 (Rios-Doria et al. 2003) cleave E-cadherin in its cytoplasmic part releasing an intracellular 37 kDa C-terminal fragment.
Identifier: R-HSA-2534248
Species: Homo sapiens
Compartment: extracellular region
DCN consists of a core protein of ?40 kDa attached to a single chondroitin or dermatan sulfate glycosaminoglycan (GAG) chain. It interacts with collagen types I, II (Vogel et al. 1984), III (Witos et al. 2011), VI (Bidanset et al. 1992) and XIV (Ehnis et al. 1997). DCN acts as a sink for all three isoforms of TGF-Beta, binding them while already bound to collagen (Markmann et al. 2000). Degradation of DCN by matrix metalloproteinases MMP2, 3 or 7 results in the release of TGF-beta (Imai et al. 1997). In addition, DCN binds to EGFR (Iozzo et al. 1999) causing prolonged down-regulation of EGFR-mediated mobilization of intracellular calcium (Csordás et al. 2000).
Identifier: R-NUL-2534162
Species: Canis familiaris, Homo sapiens
Compartment: plasma membrane, extracellular region
Full-length 120-kDa CDH1 protein is cleaved in the ectodomain close to the plasma membrane by a number of metalloproteases, generating an extracellular 38-kDa C-terminal fragment (CTF) termed CTF1 which can be further processed by a gamma-secretase-like activity to a soluble 33-kDa CTF2 (Marambaud et al. 2002, Roy & Berx 2008). MMP3, MMP7 (Noë et al. 2001) and plasmin (Ryniers et al. 2002), all cleave dog CDH1 extracellularly, close to the transmembrane region.
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). CD44-anchored MMP9 cleaves and activates transforming growth factor beta (TGF-β ), degrades extracellular matrix components such as laminin, and regulates function of several membrane bound proteins (Yu Q & Stamenkovic I 2000; reviewed by Augoff K et al. 2022). MMP9 is able to cleave CD44 as shown in neurons (Bijata M et al. 2017). The CD44:MMP9 interaction is thought to promote tumor invasion and metastatic ability (Yu Q & Stamenkovic I 2000; Peng ST et al. 2007).

Complex (1 results from a total of 1)

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