L13: Extra reading Flashcards
fibronectin
Parisi et al. (2019)
Fibronectin (FBN) is an extracellular matrix (ECM) component that, through binding integrin receptors of the cell surface, acts as a key player of the communication between the intra and the extracellular environment, thus controlling cell behavior. Furthermore, in regenerative dentistry the role of FBN in promoting the attachment of cells to root surface has been shown, as well as FBN probable pivotal role in bone and periodontal regeneration is of considerable interest [5]. Therefore, the modulation of integrin-FBN interaction may offer a promising approach to tailor tissue regenerative responses, i.e. bone and periodontal regeneration [6].
fibronectin in cell migration
The abundance of FBN in the clot is closely related to fibroblasts recruitment during wound healing. As such, FBN introduction on biomaterials may allow the creation of dynamic pathway for cells to move along the scaffold [26]. This implies FBN might act as a migratory signal or scaffold for these cells.
Accordingly, Nuttelman et al. (2001) observed that NIH3T3 fibroblasts migrated faster on poly(vinyl alcohol) hydrogels modified with FBN, if compared to tissue culture plate and to control hydrogels [26]. Similarly, by means of aptamers selected to recognize and bind FBN, we were so far able to improve the migratory capacity of osteoblasts into a hyaluronic acid based matrix [27].
i.e: enhanced cell migration
the ecm in cell migration
Pally and Naba (2024)
Cells secrete and deposit their ECM and actively organize it through cell surface receptors to facilitate their migration (Figure 2(a)). Fibronectin is one of the most abundant and well-studied fibrillar ECM proteins, and the mechanisms leading to its assembly mediated by integrin receptors is now well characterized in vitro [14]. Interestingly, recent experiments on the developing chicken embryo and associated computational modeling have demonstrated a novel mode of fibronectin organization mediated by migrating neural crest cells (NCCs). During NCC migration into the cranial region, leader cells remodel the unorganized and punctate fibronectin into a linear and filamentous form. Newly organized fibronectin then not only acts as a directional cue for efficient migration of follower cells [15] but also contributes to the assembly of other ECM proteins affecting overall ECM architecture. Similarly, during craniofacial skeleton development in mice, the interaction between skeletal progenitor cells and the collagen-rich ECM regulates proliferation, migration, and differentiation [16]. Loss of expression or mutations in discoidin domain receptor 2 (DDR2), a known collagen receptor, causes craniofacial malformations [17].
ecm in parkinsons
Rike and stern (2023)
Proteins and Transcriptional Dysregulation of the Brain Extracellular Matrix in Parkinson’s Disease: A Systematic Review
According to proteomic studies, proteins such as collagens, fibronectin, annexins, and tenascins were recognized to be differentially expressed in Parkinson’s disease. Transcriptomic studies displayed dysregulated pathways including ECM-receptor interaction, focal adhesion, and cell adhesion molecules in Parkinson’s disease. A limited number of relevant studies were accessed from our search, indicating that much work remains to be carried out to better understand the roles of the ECM in neurodegeneration and Parkinson’s disease. However, we believe that our review will elicit focused primary studies and thus support the ongoing efforts of the discovery and development of diagnostic biomarkers as well as therapeutic agents for Parkinson’s disease.
