| + |
MMP2 | up-regulates activity 
cleavage
|
Laminin-5 |
0.438 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253239 |
|
|
|
|
| pmid |
sentence |
| 9211848 |
Induction of Cell Migration by Matrix Metalloprotease-2 Cleavage of Laminin-5|MMP2 cleaved the Ln-5 gamma2 subunit at residue 587, exposing a putative cryptic promigratory site on Ln-5 that triggers cell motility. This altered form of Ln-5 is found in tumors and in tissues undergoing remodeling, but not in quiescent tissues. Cleavage of Ln-5 by MMP2 and the resulting activation of the Ln-5 cryptic site may provide new targets for modulation of tumor cell invasion and tissue remodeling. |
|
| Publications: |
1 |
| + |
Laminin-5 | up-regulates activity
binding
|
A6/b4 integrin |
0.582 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253253 |
|
|
|
|
| pmid |
sentence |
| 8832392 |
The initial adhesion of PA-JEB and normal keratinocytes to laminin-1 and laminin-5, both ligands for alpha 6 beta 1 and alpha 6 beta 4, was similar. |
|
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253238 |
|
|
|
|
| pmid |
sentence |
| 9790905 |
We propose that these alpha6 beta4/Ln-5 complexes may provide links between plasma membrane and basement membrane that resist mechanical stress and support epithelial integrity. |
|
| Publications: |
2 |
| + |
Laminin-5 | up-regulates activity
binding
|
A3/b1 integrin |
0.526 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253252 |
|
|
|
|
| pmid |
sentence |
| 2032285 |
Epiligrin, a new cell adhesion ligand for integrin alpha 3 beta 1 in epithelial basement membranes. |
|
| Publications: |
1 |
| + |
Laminin-5 | up-regulates activity
binding
|
A6/b1 integrin |
0.529 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253219 |
|
|
|
|
| pmid |
sentence |
| 12123670 |
We have developed a cell-free assay for binding of solubilized beta1 integrins to their physiologically relevant ligands using an electrochemiluminescent detection method|Binding was clearly optimal for the presumed physiological ligands, i.e., collagen IV for a1b1, collagen I for a2b1, VCAM-Ig for a4b1, fibronectin (the 120-kDa cell attachment fragment was used) for a5b1, and laminin for a6b1. |
|
| Publications: |
1 |
| + |
LAMB3 | form complex 
binding
|
Laminin-5 |
0.633 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253236 |
|
|
|
|
| pmid |
sentence |
| 9211848 |
Like the other laminins (3), Ln-5 comprises three disul- fide-bonded subunits: a3, b3, and g2. |
|
| Publications: |
1 |
| + |
LAMC2 | form complex
binding
|
Laminin-5 |
0.567 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253237 |
|
|
|
|
| pmid |
sentence |
| 9211848 |
Like the other laminins (3), Ln-5 comprises three disul- fide-bonded subunits: a3, b3, and g2. |
|
| Publications: |
1 |
| + |
LAMA3 | form complex
binding
|
Laminin-5 |
0.559 |
| Identifier |
Residue |
Sequence |
Organism |
Cell Line |
| SIGNOR-253235 |
|
|
|
|
| pmid |
sentence |
| 9211848 |
Like the other laminins (3), Ln-5 comprises three disul- fide-bonded subunits: a3, b3, and g2. |
|
| Publications: |
1 |
3.0
Laminin-5