Faculty Opinions recommendation of FLRT structure: balancing repulsion and cell adhesion in cortical and vascular development.

Author(s):  
Alain Chédotal ◽  
Heike Blockus
2007 ◽  
Vol 292 (6) ◽  
pp. C2070-C2083 ◽  
Author(s):  
Shuji Kondo ◽  
Elizabeth A. Scheef ◽  
Nader Sheibani ◽  
Christine M. Sorenson

Platelet endothelial cell adhesion molecule-1 (PECAM-1) has been implicated in angiogenesis through its involvement in endothelial cell-cell and cell-matrix interactions and signal transduction. Recent studies indicate that the cytoplasmic domain of PECAM-1 plays an important role in its cell adhesive and signaling properties. However, the role PECAM-1 isoforms play during angiogenic events such as cell adhesion and migration requires further delineation. To gain insight into the role PECAM-1 plays during vascular development and angiogenesis, we examined the expression pattern of PECAM-1 isoforms during kidney vascularization. We show that multiple isoforms of PECAM-1 are expressed during renal vascular development with different frequencies. The PECAM-1 that lacks exons 14 and 15 (Δ14&15) was the predominant isoform detected in the renal vasculature. To further study PECAM-1 isoform-specific functions we isolated kidney endothelial cells (EC) from wild-type and PECAM-1-deficient (PECAM-1−/−) mice with B4-lectin-coated magnetic beads. PECAM-1−/− kidney EC showed reduced migration, inability to undergo capillary morphogenesis in Matrigel, dense peripheral focal adhesions, and peripheral cortical actin distribution compared with wild-type cells. PECAM-1−/− kidney EC secreted increased amounts of fibronectin and decreased amounts of tenascin-C and thrombospondin-1. Reexpression of Δ14&15, but not full-length, PECAM-1 in PECAM-1−/− kidney EC restored cell migration and capillary morphogenesis defects. Thus PECAM-1 may regulate the adhesive and migratory properties of kidney EC in an isoform-specific fashion through modulation of integrin activity and extracellular matrix protein expression. Our results indicate that regulated expression of specific PECAM-1 isoforms may enable EC to accommodate the different stages of angiogenesis.


2014 ◽  
Vol 8 (2) ◽  
pp. 136-145 ◽  
Author(s):  
Anne Karine Lagendijk ◽  
Alpha S Yap ◽  
Benjamin M Hogan

2015 ◽  
Vol 129 (3) ◽  
pp. 217-234 ◽  
Author(s):  
Sunyoung Park ◽  
Christine M. Sorenson ◽  
Nader Sheibani

Vascular development and maintenance of proper vascular function through various regulatory mechanisms are critical to our wellbeing. Delineation of the regulatory processes involved in development of the vascular system and its function is one of the most important topics in human physiology and pathophysiology. Platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31), a cell adhesion molecule with proangiogenic and proinflammatory activity, has been the subject of numerous studies. In the present review, we look at the important roles that PECAM-1 and its isoforms play during angiogenesis, and its molecular mechanisms of action in the endothelium. In the endothelium, PECAM-1 not only plays a role as an adhesion molecule but also participates in intracellular signalling pathways which have an impact on various cell adhesive mechanisms and endothelial nitric oxide synthase (eNOS) expression and activity. In addition, recent studies from our laboratory have revealed an important relationship between PECAM-1 and endoglin expression. Endoglin is an essential molecule during angiogenesis, vascular development and integrity, and its expression and activity are compromised in the absence of PECAM-1. In the present review we discuss the roles that PECAM-1 isoforms may play in modulation of endothelial cell adhesive mechanisms, eNOS and endoglin expression and activity, and angiogenesis.


Neuron ◽  
2014 ◽  
Vol 84 (2) ◽  
pp. 370-385 ◽  
Author(s):  
Elena Seiradake ◽  
Daniel del Toro ◽  
Daniel Nagel ◽  
Florian Cop ◽  
Ricarda Härtl ◽  
...  

2005 ◽  
Vol 173 (4S) ◽  
pp. 170-170
Author(s):  
Maxine G. Tran ◽  
Miguel A. Esteban ◽  
Peter D. Hill ◽  
Ashish Chandra ◽  
Tim S. O'Brien ◽  
...  

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