Publications by authors named "Susan Summers"

Rationale: p120-catenin (p120) is an armadillo family protein that binds to the cytoplasmic domain of classical cadherins and prevents cadherin endocytosis. The role of p120 in vascular development is unknown.

Objective: The purpose of this study is to examine the role of p120 in mammalian vascular development by generating a conditionally mutant mouse lacking endothelial p120 and determining the effects of the knockout on vasculogenesis, angiogenic remodeling, and the regulation of endothelial cadherin levels.

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Infant mental health, as concept and intervention, is poorly understood by most practitioners in education settings. Direct-service personnel often lack appropriate knowledge, training, skills, and confidence in recognizing and addressing infant mental health problems. While programs and policymakers increasingly acknowledge the need to offer infant mental health services in order to prevent or mediate poor developmental outcomes among young children, effective methods of realizing an infant mental health initiative remain elusive.

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Desmosomes are adhesive intercellular junctions prominent in the skin and heart. Loss of desmosome function is associated with severe congenital and acquired disorders characterized by tissue fragility. Pemphigus vulgaris (PV) is an autoimmune disorder in which antibodies are directed against the desmosomal adhesion molecule Dsg3, resulting in severe mucosal erosions and epidermal blistering.

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p0071 is an armadillo family protein related to both the adherens junction protein p120ctn and to the desmosomal proteins plakophilins 1-3. p0071 assembles into both adherens junctions and desmosomes, suggesting that this protein may regulate the balance between adherens junction and desmosome formation. Furthermore, this subfamily of proteins may also regulate cell functions directly influenced by intercellular junctions, including the strength of cell adhesion and the ability of cells to migrate.

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VE-cadherin is an endothelial-specific cadherin that plays important roles in vascular morphogenesis and growth control. To investigate the mechanisms by which endothelial cells regulate cadherin cell surface levels, a VE-cadherin mutant containing the non-adhesive interleukin-2 (IL-2) receptor extracellular domain and the VE-cadherin cytoplasmic tail (IL-2R-VE-cadcyto) was expressed in microvascular endothelial cells. Expression of the IL-2R-VE-cadcyto mutant resulted in the internalization of endogenous VE-cadherin and in a dramatic decrease in endogenous VE-cadherin levels.

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VE-cadherin is an endothelial-specific cadherin that plays a central role in vascular barrier function and angiogenesis. The cytoplasmic domain of VE-cadherin is linked to the cytoskeleton through interactions with the armadillo family proteins beta-catenin and plakoglobin. Growing evidence indicates that beta-catenin and plakoglobin play important roles in epithelial growth and morphogenesis.

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