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1. Structural relationships between clathrin assembly proteins from the Golgi and the plasma membrane.

Author

Ahle, S., Mann, A., Eichelsbacher, U., and Ungewickell, E.

Abstract

We have established by peptide mapping and immunochemical analysis of purified clathrin assembly protein preparations from bovine brain, that the cluster of components of mol. wt 100‐120 kd fall into four classes, which we term alpha, beta, beta‘ and gamma. The beta and beta’ proteins are immunologically related and generate a series of common tryptic peptides. The same criteria reveal no such homologies between the alpha, beta(beta‘) and gamma polypeptides. The so‐called HA‐II assembly protein group contains equimolar amounts of alpha and beta class polypeptides, which are shown to interact with each other. In the HA‐I group assembly protein complex gamma and beta’ class polypeptides form a stoichiometric complex. Immunofluorescence microscopy reveals that the HA‐I complex is specifically associated with clathrin‐coated membranes in the Golgi region of cultured cells, whereas the HA‐II complex appears to be restricted to coated pits on the plasma membrane. The data lead to the tentative conclusion that the clathrin assembly proteins are involved in the recognition of the intracellular targets by uncoated vesicles.

Published
1988
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2. EphB4 controls blood vascular morphogenesis during postnatal angiogenesis.

Author

Erber R, Eichelsbacher U, Powajbo V, Korn T, Djonov V, Lin J, Hammes HP, Grobholz R, Ullrich A, and Vajkoczy P

Subjects
Angiopoietin-1 metabolism, Animals, Brain Neoplasms blood supply, Brain Neoplasms metabolism, Capillary Permeability, Cell Line, Endothelial Cells metabolism, Ephrin-B2 biosynthesis, Glioma blood supply, Glioma metabolism, Humans, Mice, Mice, Inbred C57BL, Mice, Nude, Neoplasm Transplantation, Receptor, EphB4 biosynthesis, Receptor, TIE-2 metabolism, Retinal Vessels growth & development, Signal Transduction, Transplantation, Heterologous, Morphogenesis, Neovascularization, Pathologic, Neovascularization, Physiologic, Receptor, EphB4 physiology
Abstract

Guidance molecules have attracted interest by demonstration that they regulate patterning of the blood vascular system during development. However, their significance during postnatal angiogenesis has remained unknown. Here, we demonstrate that endothelial cells of human malignant brain tumors also express guidance molecules, such as EphB4 and its ligand ephrinB2. To study their function, EphB4 variants were overexpressed in blood vessels of tumor xenografts. Our studies revealed that EphB4 acts as a negative regulator of blood vessel branching and vascular network formation, switching the vascularization program from sprouting angiogenesis to circumferential vessel growth. In parallel, EphB4 reduces the permeability of the tumor vascular system via activation of the angiopoietin-1/Tie2 system at the endothelium/pericyte interface. Furthermore, overexpression of EphB4 variants in blood vessels during (i) vascularization of non-neoplastic cell grafts and (ii) retinal vascularization revealed that these functions of EphB4 apply to postnatal, non-neoplastic angiogenesis in general. This implies that both neoplastic and non-neoplastic vascularization is driven not only by a vascular initiation program but also by a vascular patterning program mediated by guidance molecules.

Published
2006
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