𝔖 Bobbio Scriptorium
✦   LIBER   ✦

Interaction between monensin and lysosomotropic amines in the regulation of the processing of epidermal growth factor by BALB/c 3T3 cells

✍ Scribed by Janet L. Cooper; Richard Selinfreund; Eric Wakshull; Walker Wharton


Publisher
Springer
Year
1987
Tongue
English
Weight
663 KB
Volume
73
Category
Article
ISSN
0300-8177

No coin nor oath required. For personal study only.


📜 SIMILAR VOLUMES


Regulation of the Balb/c-3T3 cell cycle-
✍ Stiles, C. D. ;Pledger, W. J. ;Tucker, R. W. ;Martin, R. G. ;Scher, C. D. 📂 Article 📅 1980 🏛 Wiley (John Wiley & Sons) 🌐 English ⚖ 649 KB

## Abstract The platelet‐derived growth factor (PDGF), which is found in serum but not in plasma, has been purified to homogeneity; it stimulates replication at a concentration of 10^−10^M. Brief treatment with PDGF causes densityinhibited Balb/c‐3T3 cells to become competent to synthesize DNA; pit

Epidermal growth factor and the control
✍ Kenneth D. Brown; Robert W. Holley 📂 Article 📅 1979 🏛 John Wiley and Sons 🌐 English ⚖ 614 KB

## Abstract Benzo[a]pyrene‐transformed Balb 3T3 cells (BP3T3) exhibit “normal” growth controls at low concentrations of serum. Epidermal growth factor (EGF) stimulates DNA synthesis and cell division in both Balb 3T3 and BP3T3 cells at physiological concentrations. The growth response of BP3T3 cell

The binding and processing of plasminoge
✍ Jerry Tobler; Monty Krieger; Robert M. Stroud 📂 Article 📅 1981 🏛 John Wiley and Sons 🌐 English ⚖ 989 KB

## Abstract The binding and processing of plasminogen by Balb/c 3T3 and SV3T3 cells was studied using ^125^I‐labeled canine plasminogen. Throughout a 3‐day period, ^125^I‐plasminogen in the incubation medium bound to the cells and was degraded, first to intermediate‐sized macromolecules that were t

Binding, internalization, and degradatio
✍ Kenneth D. Brown; Yun-Chi Yeh; Robert W. Holley 📂 Article 📅 1979 🏛 John Wiley and Sons 🌐 English ⚖ 852 KB

## Abstract Epidermal growth factor (EGF) stimulates the growth of both benzo[a]pyrene‐transformed Balb 3T3 cells (BP3T3) and untransformed Balb 3T3 cells. We describe here the binding, internalization, and degradation of [^125^I]‐EGF by BP3T3 cells and 3T3 cells. Binding of [^125^I]‐EGF reaches a

Modulation of the epidermal growth facto
✍ Shuan Shian Huang; Vinata B. Lokeshwar; Jung San Huang 📂 Article 📅 1988 🏛 John Wiley and Sons 🌐 English ⚖ 721 KB

Incubation of Swiss mouse 3T3 cells at 37°C with bovine brain-derived growth factor (BDGF) decreased the cell surface '251-EGF binding activity of these cells by 70-80%. This down-modulation of the EGF receptor by BDGF was time, temperature, and dose dependent. Scatchard plot analysis indicated that

Characterization of the rebinding of 125
✍ Janet L. Cooper; Eric Wakshull; Walker Wharton 📂 Article 📅 1988 🏛 John Wiley and Sons 🌐 English ⚖ 846 KB

Lysosomotropic amines, such as chloroquine and methylamine, increase the intracellular accumulation of 125I-EGF by inhibiting lysosomal degradation. It has been shown previously that BALB/c-3T3 cells, prelabeled at 4 degrees C with 125I-EGF for 3 h and subsequently chased at 37 degrees C in the pres