High affinity VEGF binding and developmental expression suggest Flk-1 as a major regulator of vasculogenesis and angiogenesis

Article Abstract:

The role of flk-1 receptor tyrosine kinase in vasculogenesis and angiogenesis was investigated. The study protocol involved in situ hybridization analysis of flk-1 tyrosine kinase mRNA expression at different stages of mouse development. The results showed that mRNA transcripts are associated with endothelial cells at all stages of development. Furthermore, the angiogenic mitogen vascular endothelial growth factor (VEGF) was identified as the high-affinity ligand of Flk-1. Correlation of VEGF and Flk-1 expression indicate a key role for this ligand-receptor complex in vasculogenesis and angiogenesis.

Protein tyrosine kinase, Protein-tyrosine kinase, Ligand binding (Biochemistry)

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Mammalian SH2-containing protein tyrosine phosphatases

Article Abstract:

Nomenclature adjustments are proposed for the SH2-containing protein tyrosine phosphatases (PTPase) to differentiate between the two current members of the PTPase subfamily. SHP-1 is assigned to the GenBank accession numbers M68902, M77273, M90388, X62055, with an HGMW designation PTPN6. SHP-2 is assigned to the GenBank accession numbers D13540, LO3535, LO7527, X70766, LO8663, with an HGMW designation PTPN11. SHP-1 appeared in literature as SHPTP-1, SHP, HCP, and PTP1C, while SHP-2 was known as SHPTP-2, SHPTP-3, syp, PTP2C, and PTP1D.

Enzymes, Terminology, Phosphatases, Letter to the Editor

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Targeted deficiency or cytosolic truncation of the VE-cadherin gene in mice impairs VEGF-mediated endothelial survival and angiogenesis

Article Abstract:

Vascular endothelial (VE) cadherin can influence vascular morphogenesis. Research findings reveal that VE-cadherin plays a vital role in controlling vascular endothelial growth factor-A-mediated endothelial survival through a pathway that involves the cytoplasmic domain of VE-cadherin, beta-catenin, vascular endothelial growth factor receptor-2 and P13-kinase. A relationship was also established which links the inhibition of normal vascular development with the loss or truncation of VE-cadherin.

Endothelium, Morphogenesis, Cytology

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