Domain IVa of laminin α5 chain is cell-adhesive and binds β1 and αVβ3 integrins through Arg-Gly-Asp
✍ Scribed by Takako Sasaki; Rupert Timpl
- Book ID
- 117103684
- Publisher
- Elsevier Science
- Year
- 2001
- Tongue
- English
- Weight
- 522 KB
- Volume
- 509
- Category
- Article
- ISSN
- 0014-5793
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Bone sialoprotein (BSP), a secreted glycoprotein found in bone matrix, has been implicated in the formation of mammary microcalcifications and osteotropic metastasis of human breast cancer (HBC). BSP possesses an integrin-binding RGD (Arg-Gly-Asp) domain, which may promote interactions between HBC c
Gliomas, characterized by their progressively invasive phenotype, express integrin ␣31 as a major receptor for the extracellular matrix both in vivo and in vitro. Since the integrin ␣31 has been shown to be a specific receptor for laminin-5 (␣33␥2), we examined the effects of purified human lamin