𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Rapid isolation of plasmalemma from cultured A431 cells: Characterization of epidermal growth factor receptors

✍ Scribed by Peter H. Lin; Richard H. Selinfreund; Eric Wakshull; Walker Wharton

Publisher
Elsevier Science
Year
1988
Tongue
English
Weight
507 KB
Volume
168
Category
Article
ISSN
0003-2697

No coin nor oath required. For personal study only.

✦ Synopsis

A rapid method for the purification of plasma membrane from a relatively small number of A431 cells is described. The method is a simple, two-step differential centrifugation in the presence of Ca2+ that requires a total centrifugation time of 7 min. The membrane preparations contained a high level of epidermal growth factor (EGF) receptor activity demonstrated by both the quantity of specific ligand binding and the amount of EGF-dependent phosphorylation of the receptor and an exogenous substrate. EGF-dependent autophosphorylation identified the EGF receptor in the purified membranes as an undegraded 170-kDa protein.

πŸ“œ SIMILAR VOLUMES

Characterization of the metabolic turnov
Characterization of the metabolic turnover of epidermal growth factor receptor protein in A-431 cells
✍ Christa M. Stoscheck; Graham Carpenter πŸ“‚ Article πŸ“… 1984 πŸ› John Wiley and Sons 🌐 English βš– 909 KB

## Abstract The metabolism of the receptor for epidermal growth factor (EGF) in A‐431 cells has been measured by labeling the receptor in vivo with radioactive amino acid precursors and then determining, by immunoprecipitation with specific anti‐EGF receptor antisera, the rate of degradation of the

Ligand-induced association of epidermal
Ligand-induced association of epidermal growth factor receptor to the cytoskeleton of A431 cells
✍ P. M. P. van Bergen en Henegouwen; L. H. K. Defize; J. de Kroon; H. van Damme; A πŸ“‚ Article πŸ“… 1989 πŸ› John Wiley and Sons 🌐 English βš– 625 KB

Recently, we have obtained evidence in favor of a structural interaction between the epidermal growth factor (EGF) receptor and the Triton X-100-insoluble cytoskeleton of epidermoid carcinoma A431 cells. Here we present a further analysis of the properties of EGF receptors attached to the cytoskelet

Presence of epidermal growth factor rece
Presence of epidermal growth factor receptors and influence of epidermal growth factor on proliferation and aging in cultured smooth muscle cells
✍ Girija Bhargava; Leonard Rifas; Maynard H. Makman πŸ“‚ Article πŸ“… 1979 πŸ› John Wiley and Sons 🌐 English βš– 744 KB

## Abstract Epidermal growth factor (EGF) at nanomolar concentrations stimulated DNA synthesis in confluent, serum‐starved cultures of calf aorta and human uterine smooth muscle cells. Stimulation of DNA synthesis in lens epithelial cells was studied for comparison. L and D‐ascorbic acid potentiate

Submicromolar doses of alkyl-lysophospho
Submicromolar doses of alkyl-lysophospholipids induce rapid internalization, but not activation, of epidermal growth factor receptor and concomitant MAPK/ERK activation in A431 cells
✍ Gerald A. Ruiter; Marcel Verheij; Shuraila F. Zerp; Wouter H. Moolenaar; Wim J. πŸ“‚ Article πŸ“… 2002 πŸ› John Wiley and Sons 🌐 French βš– 715 KB

Synthetic ALPs, e.g., Et-18-OCH(3) and HePC, are anticancer agents that accumulate in cell membranes, where they interfere with lipid-mediated signal transduction. We previously reported that ALPs, when added at micromolar concentrations (5-25 microM), inhibit growth factor-induced MAPK/ERK activati

Similarities in glycosylation and transp
Similarities in glycosylation and transport between the secreted and plasma membrane forms of the epidermal growth factor receptor in A-431 cells
✍ Ann Mangelsdorf Soderquist; Christa Stoscheck; Graham Carpenter πŸ“‚ Article πŸ“… 1988 πŸ› John Wiley and Sons 🌐 English βš– 846 KB

We have studied the synthesis and oligosaccharide processing of the 110,000 dalton form of the epidermal growth factor (EGF) receptor that is secreted into the medium of A-431 cells. Its 90,000 dalton precursor is soluble within the lumen of intracellular membrane vesicles shortly after synthesis, i