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Title: Zinc uptake into endothelial cells involves a carrier mediated component

Conference · · FASEB Journal (Federation of American Societies for Experimental Biology); (United States)
OSTI ID:5215221
; ;  [1]
  1. USDA-ARS Human Nutrition Center, Grand Forks, ND (United States)

The mechanism of zinc (Zn) uptake by endothelial cells was examined. Bovine pulmonary endothelial cells were grown to a confluent monolayer in T-25 flasks with minimum essential medium (MEM) containing 10% fetal bovine serum. Zn uptake was studied by replacing the growth medium with experimental media of MEM, 14% EDTA dialyzed serum, and 250 nCi {sup 65}Zn/mL. The transport mechanism was studied by manipulating the composition of the experimental media and measuring the accumulation of {sup 65}Zn by the cells during a 10 min incubation period at 37C, 90% relative humidity, and 5% CO{sub 2}. The rate of Zn uptake increased as the Zn concentration in the media increased from 1 to 26 {mu}M. The data were described by a rectangular hyperbola with V{sub max} = 27.2 {plus minus} 0.84 pmoles Zn and K{sub m} = 4.1 {plus minus} 0.46 {mu}M Zn. The mechanism was studied further with 6 {mu}M added Zn (ZnCl{sub 2}) in the experimental media. Zn uptake was temperature dependent; the rate was less than 6C than at 24C, which was less than at 33C. The Zn uptake rate was reduced by the metabolic inhibitors iodoacetate, sodium fluoride, and N-ethylmaleimide. Cadmium competitively inhibited Zn uptake; copper and manganese had no effect. Increasing the concentration of albumin tin the media reduced the Zn uptake rate over the range from 0 to 40 {mu}M albumin in the media reduced the Zn uptake rate over the range from 0 to 40 {mu}M albumin, but not at 50 {mu}M albumin, with 10 {mu}M Zn. The addition of Zn binding ligands decreased the Zn uptake rate in the absence of serum, but increased the rate when serum was present. These results demonstrate that Zn uptake into endothelial cells is facilitated by a transporter possessing a recognition site that is saturable and at least partially energy dependent. Additionally, the uptake rate apparently is influenced by the ligand to which Zn is bound in the extracellular fluid.

OSTI ID:
5215221
Report Number(s):
CONF-9104107-; CODEN: FAJOE
Journal Information:
FASEB Journal (Federation of American Societies for Experimental Biology); (United States), Vol. 5:5; Conference: 75. annual meeting of the Federation of American Societies for Experimental Biology (FASEB), Atlanta, GA (United States), 21-25 Apr 1991; ISSN 0892-6638
Country of Publication:
United States
Language:
English

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