Neurite outgrowth, RGD-dependent, and RGD-independent adhesion of identified molluscan motoneurons on selected substrates
✍ Scribed by Wildering, W. C. ;Hermann, P. M. ;Bulloch, A. G. M.
- Publisher
- John Wiley and Sons
- Year
- 1998
- Tongue
- English
- Weight
- 274 KB
- Volume
- 35
- Category
- Article
- ISSN
- 0022-3034
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✦ Synopsis
The extracellular matrix (ECM) ers a RGD binding site in the protein. Laminin as well provides structural support to cells and tissues and is as denatured fibronectin, but not type IV collagen, involved in the regulation of various essential physiological processes, including neurite outgrowth. Most induced neurite outgrowth from a percentage of the of the adhesive interactions between cells and ECM RPA neurons. These results demonstrate that molproteins are mediated by integrins. Integrins typically luscan neurons can attach to various substrates using recognize short linear amino acid sequences in ECM both RGD-dependent and RGD-independent adhesion proteins, one of the most common being Argininemechanisms. This suggests that at least two different Glycine-Aspartate (RGD). The present study invescell adhesion receptors, possibly belonging to the intetigated neurite outgrowth and adhesion of identified grin family, are expressed in these neurons. Moreover, molluscan neurons on a selection of substrates in vitro. the results show that vertebrate ECM proteins can Involvement of RGD binding sites in adhesion to the induce outgrowth from these neurons, suggesting that different substrates was investigated using soluble the mechanisms involved in adhesion as well as outsynthetic RGD peptides. The cells adhered to native growth promoting are evolutionarily well conserved. (i.e., nondenatured) laminin and type IV collagen, but