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Details on Person Laminins are an important molecular component of the basemen...
| Class:Id | Summation:1566938 |
|---|---|
| _displayName | Laminins are an important molecular component of the basemen... |
| _timestamp | 2013-07-05 10:25:21 |
| created | [InstanceEdit:1566968] Jupe, S, 2011-09-06 |
| literatureReference | [LiteratureReference:2588524] Laminin-332 and -511 in skin [LiteratureReference:3788019] Laminin 332 processing impacts cellular behavior [LiteratureReference:3787966] The anchoring filament protein kalinin is synthesized and secreted as a high molecular weight precursor [LiteratureReference:2533875] Induction of cell migration by matrix metalloprotease-2 cleavage of laminin-5 [LiteratureReference:3788029] Membrane-type matrix metalloproteinase-1 (MT1-MMP) is a processing enzyme for human laminin gamma 2 chain [LiteratureReference:3788004] Binding to EGF receptor of a laminin-5 EGF-like fragment liberated during MMP-dependent mammary gland involution [LiteratureReference:2533898] Membrane type-1-matrix metalloproteinase expressed by prostate carcinoma cells cleaves human laminin-5 beta3 chain and induces cell migration [LiteratureReference:3787940] Matrilysin 1 influences colon carcinoma cell migration by cleavage of the laminin-5 beta3 chain [LiteratureReference:3787930] Processing of laminin-5 and its functional consequences: role of plasmin and tissue-type plasminogen activator [LiteratureReference:3787954] The alpha3 laminin subunit, alpha6beta4 and alpha3beta1 integrin coordinately regulate wound healing in cultured epithelial cells and in the skin [LiteratureReference:3788052] Mammalian tolloid metalloproteinase, and not matrix metalloprotease 2 or membrane type 1 metalloprotease, processes laminin-5 in keratinocytes and skin [LiteratureReference:3787946] Role of cell surface metalloprotease MT1-MMP in epithelial cell migration over laminin-5 [LiteratureReference:2533847] Matrix metalloproteinases process the laminin-5 gamma 2-chain and regulate epithelial cell migration [LiteratureReference:2533927] Matrix metalloproteinase 19 processes the laminin 5 gamma 2 chain and induces epithelial cell migration [LiteratureReference:2533883] Expression and regulation of MMP-20 in human tongue carcinoma cells [LiteratureReference:3788043] Bone morphogenetic protein 1 is an extracellular processing enzyme of the laminin 5 gamma 2 chain [LiteratureReference:2267228] Bone morphogenetic protein-1 (BMP-1) mediates C-terminal processing of procollagen V homotrimer [LiteratureReference:2533879] Plasminogen enhances neuritogenesis on laminin-1 |
| modified | [InstanceEdit:2533918] Jupe, S, 2012-10-22 [InstanceEdit:3787960] Jupe, S, 2013-07-04 [InstanceEdit:3791165] Jupe, S, 2013-07-05 |
| text | Laminins are an important molecular component of the basement membranes (BMs) in a variety of tissue types. They have a cruciform shape, and are composed of three chains, alpha, beta and gamma., all of which have multiple subtypes. At the ultrastructural level, each laminin trimer appears as a cross-like structure with a large globular domain (LG domain) at the base of the cross. The LG domain is the C-terminal domain of the alpha subunit; it is divided into five homologous subdomains LG1-5 (Sugawara et al. 2008). Keratinocytes of the skin secrete numerous laminin isoforms, including laminin-511 and laminin-332. Laminin-332 undergoes extensive proteolysis following secretion, which is essential for laminin-332 integration into the BM (Rousselle & Beck 2013). The 200 kDa alpha-3 subunit of laminin-332 is cleaved between the LG3-LG4 subdomains to generate a 165 kDa product. The 160 kDa gamma-2 subunit is cleaved at its N-terminus to produce a 105 kDa protein (Marinkovich et al. 1992). Tissue remodeling may lead to further proteolysis of the 105 kDa subunit within the N-terminus giving rise to a 80 kDa protein (Gianelli et al. 1997, Koshikawa et al. 2005). The resulting N-terminal fragment has EGF-like properties and may activate the EGF receptor, inducing cell migration (Schenk et al. 2003). In much of the early literature it is not clear which subunit of the laminin trimer was cleaved, but in vitro studies have revealed specific enzymes involved in the processing of laminin-332 including MMP2, MMP14 (MT1-MMP), and the C-proteinase family of enzymes, especially bone morphogenic protein 1 (BMP1) and mammalian tolloid (mTLD), isoforms 1 and 3 respectively of UniProt P13497 BMP1 (Sugawara et al. 2008, Rousselle & Beck 2013). Many proteases have been demonstrated to degrade specific subunits of laminin-332. The beta-3 chain is degraded by matrix metalloproteinase 14 (MMP14, MT1-MMP, Udayakumar et al. 2003) and MMP7 (Remy et al. 2006). The alpha-3 chain is degraded by plasmin (Goldfinger et al. 1998, 1999) and BMP1 (and its isoform mTLD, Veitch et al. 2003). Laminin gamma-2 chain is degraded by MMP14 (Koshikawa et al. 2000, 2005, Pirilä et al. 2003) , MMP2 (Gianelli et al. 1997, Pirilä et al. 2003), MMP3, 12, 13 (Pirilä et al. 2003), 19 (Sadowski et al. 2005), MMP20 (Väänänen et al. 2001, Pirilä et al. 2003), BMP1 (Amano et al. 2000, Kessler et al. 2001) and mTLD (Veitch et al. 2003). Plasmin cleavage of laminin-111 yields fragments with sizes that correspond to the cleavage of the alpha and beta/gamma components (Gutiérrez-Fernández et al. 2009). In this reaction laminin-322 is represented with all 3 component peptides cleaved. |
| (summation) | [Reaction:1566979] Laminin-332 degradation by laminin-322 degrading extracellular proteinases [Homo sapiens] |
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