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The role of the kinase insert domain-containing receptor (KDR) in the Ca2+ mobilization in human umbilical vein endothelial cells (HUVEC) was determined by preparing a polyclonal mouse antibody against the first three immunoglobulin-like domains of KDR. The serum was found to inhibit vascular endothelial cell growth factor (VEGF165) binding to the KDR and signaling through Ca2+ in HUVEC. The inhibition of KDR plus the lack of response to placental growth factor suggests that the binding of VEGF165 to KDR does not translate into a Ca2+ response.

The structure of the alpha-subunit of bovine kidney epithelial Na+ channel (alpha-bENaC) obtained from the renal collecting duct is 75-85% similar to the rat and human homolog. Alpha-bENaC has an open-reading frame which produces a protein containing 697 amino acids. The expression of alpha-bENaC in Xenopus oocytes causes a Na+ current which is unaffected by an increase in the concentration of adenosine 3,5'-cyclic monophosphate but increases if protein kinase C is stimulated. The cloning and amino acid sequence of alpha-bENaC cDNA is given.