Mechanisms of zinc uptake in gills of freshwater rainbow trout: Interplay with calcium transport

Christer Hogstrand, Pieter M. Verbost, Sjoerd E. Wendelaar Bonga, Chris M. Wood

Research output: Contribution to journalArticle

130 Citations (Scopus)

Abstract

The uptake mechanism of Zn2+ through the gill epithelium of freshwater rainbow trout was investigated both in intact animals and in isolated basolateral membranes. Involvement of the apical Ca2+ uptake sites in Zn2+ uptake was examined in vivo by pharmacological manipulation of the apical Ca2+ permeability. The apical entries of Ca2+ and Zn2+, but not Na+ and Cl, were inhibited by addition of La to the water. Addition of 1.0 μM La reduced the influxes of Ca2+ and Zn2+ to 22 ± 3 and 53 ± 7% (means ± SE) of the control value, respectively. Injection of CaCl2 also reduced the branchial influxes of Ca2+ and Zn2+. This treatment decreased the influx of Ca2+ to 45 ± 4% of the control level and the Zn2+ influx to 68 ± 5%. These results strongly imply that Zn2+ passes across the apical membrane of the chloride cells of the gills via the same pathway as Ca2+. The presence of an active basolateral transporter for Zn2+ was investigated in vitro on isolated basolateral membranes. There was no ATP- dependent or Na+-gradient driven transport of Zn2+ at physiological Zn2+ activities. The same system was used to study potential effects of Zn2+ on the basolateral Ca2+-adenosinetriphosphatase. Zn2+ was found to be a potent blocker of this transporter, causing a mixed inhibitory effect on the ATP-driven Ca2+ transport at a free Zn2+ activity of 100 pM.

Original languageEnglish
JournalAmerican Journal of Physiology - Regulatory Integrative and Comparative Physiology
Volume270
Issue number5 39-5
StatePublished - Jun 25 1996

Fingerprint

Oncorhynchus mykiss
Fresh Water
Zinc
Adenosine Triphosphate
Calcium
Membranes
Adenosine Triphosphatases
Chlorides
Permeability
Epithelium
Cell Membrane
Pharmacology
Injections
Water
Therapeutics
In Vitro Techniques

Keywords

  • Ca channel
  • Ca- adenosinetriphosphatase
  • chloride cells
  • inhibition
  • ionocytes
  • lanthanum
  • regulation
  • stanniocalcin

ASJC Scopus subject areas

  • Physiology
  • Physiology (medical)

Cite this

Mechanisms of zinc uptake in gills of freshwater rainbow trout : Interplay with calcium transport. / Hogstrand, Christer; Verbost, Pieter M.; Wendelaar Bonga, Sjoerd E.; Wood, Chris M.

In: American Journal of Physiology - Regulatory Integrative and Comparative Physiology, Vol. 270, No. 5 39-5, 25.06.1996.

Research output: Contribution to journalArticle

Hogstrand, Christer ; Verbost, Pieter M. ; Wendelaar Bonga, Sjoerd E. ; Wood, Chris M. / Mechanisms of zinc uptake in gills of freshwater rainbow trout : Interplay with calcium transport. In: American Journal of Physiology - Regulatory Integrative and Comparative Physiology. 1996 ; Vol. 270, No. 5 39-5.
@article{991d5a14ecb54340bb7555b43c768f90,
title = "Mechanisms of zinc uptake in gills of freshwater rainbow trout: Interplay with calcium transport",
abstract = "The uptake mechanism of Zn2+ through the gill epithelium of freshwater rainbow trout was investigated both in intact animals and in isolated basolateral membranes. Involvement of the apical Ca2+ uptake sites in Zn2+ uptake was examined in vivo by pharmacological manipulation of the apical Ca2+ permeability. The apical entries of Ca2+ and Zn2+, but not Na+ and Cl, were inhibited by addition of La to the water. Addition of 1.0 μM La reduced the influxes of Ca2+ and Zn2+ to 22 ± 3 and 53 ± 7{\%} (means ± SE) of the control value, respectively. Injection of CaCl2 also reduced the branchial influxes of Ca2+ and Zn2+. This treatment decreased the influx of Ca2+ to 45 ± 4{\%} of the control level and the Zn2+ influx to 68 ± 5{\%}. These results strongly imply that Zn2+ passes across the apical membrane of the chloride cells of the gills via the same pathway as Ca2+. The presence of an active basolateral transporter for Zn2+ was investigated in vitro on isolated basolateral membranes. There was no ATP- dependent or Na+-gradient driven transport of Zn2+ at physiological Zn2+ activities. The same system was used to study potential effects of Zn2+ on the basolateral Ca2+-adenosinetriphosphatase. Zn2+ was found to be a potent blocker of this transporter, causing a mixed inhibitory effect on the ATP-driven Ca2+ transport at a free Zn2+ activity of 100 pM.",
keywords = "Ca channel, Ca- adenosinetriphosphatase, chloride cells, inhibition, ionocytes, lanthanum, regulation, stanniocalcin",
author = "Christer Hogstrand and Verbost, {Pieter M.} and {Wendelaar Bonga}, {Sjoerd E.} and Wood, {Chris M.}",
year = "1996",
month = "6",
day = "25",
language = "English",
volume = "270",
journal = "American Journal of Physiology - Cell Physiology",
issn = "0363-6143",
publisher = "American Physiological Society",
number = "5 39-5",

}

TY - JOUR

T1 - Mechanisms of zinc uptake in gills of freshwater rainbow trout

T2 - Interplay with calcium transport

AU - Hogstrand, Christer

AU - Verbost, Pieter M.

AU - Wendelaar Bonga, Sjoerd E.

AU - Wood, Chris M.

PY - 1996/6/25

Y1 - 1996/6/25

N2 - The uptake mechanism of Zn2+ through the gill epithelium of freshwater rainbow trout was investigated both in intact animals and in isolated basolateral membranes. Involvement of the apical Ca2+ uptake sites in Zn2+ uptake was examined in vivo by pharmacological manipulation of the apical Ca2+ permeability. The apical entries of Ca2+ and Zn2+, but not Na+ and Cl, were inhibited by addition of La to the water. Addition of 1.0 μM La reduced the influxes of Ca2+ and Zn2+ to 22 ± 3 and 53 ± 7% (means ± SE) of the control value, respectively. Injection of CaCl2 also reduced the branchial influxes of Ca2+ and Zn2+. This treatment decreased the influx of Ca2+ to 45 ± 4% of the control level and the Zn2+ influx to 68 ± 5%. These results strongly imply that Zn2+ passes across the apical membrane of the chloride cells of the gills via the same pathway as Ca2+. The presence of an active basolateral transporter for Zn2+ was investigated in vitro on isolated basolateral membranes. There was no ATP- dependent or Na+-gradient driven transport of Zn2+ at physiological Zn2+ activities. The same system was used to study potential effects of Zn2+ on the basolateral Ca2+-adenosinetriphosphatase. Zn2+ was found to be a potent blocker of this transporter, causing a mixed inhibitory effect on the ATP-driven Ca2+ transport at a free Zn2+ activity of 100 pM.

AB - The uptake mechanism of Zn2+ through the gill epithelium of freshwater rainbow trout was investigated both in intact animals and in isolated basolateral membranes. Involvement of the apical Ca2+ uptake sites in Zn2+ uptake was examined in vivo by pharmacological manipulation of the apical Ca2+ permeability. The apical entries of Ca2+ and Zn2+, but not Na+ and Cl, were inhibited by addition of La to the water. Addition of 1.0 μM La reduced the influxes of Ca2+ and Zn2+ to 22 ± 3 and 53 ± 7% (means ± SE) of the control value, respectively. Injection of CaCl2 also reduced the branchial influxes of Ca2+ and Zn2+. This treatment decreased the influx of Ca2+ to 45 ± 4% of the control level and the Zn2+ influx to 68 ± 5%. These results strongly imply that Zn2+ passes across the apical membrane of the chloride cells of the gills via the same pathway as Ca2+. The presence of an active basolateral transporter for Zn2+ was investigated in vitro on isolated basolateral membranes. There was no ATP- dependent or Na+-gradient driven transport of Zn2+ at physiological Zn2+ activities. The same system was used to study potential effects of Zn2+ on the basolateral Ca2+-adenosinetriphosphatase. Zn2+ was found to be a potent blocker of this transporter, causing a mixed inhibitory effect on the ATP-driven Ca2+ transport at a free Zn2+ activity of 100 pM.

KW - Ca channel

KW - Ca- adenosinetriphosphatase

KW - chloride cells

KW - inhibition

KW - ionocytes

KW - lanthanum

KW - regulation

KW - stanniocalcin

UR - http://www.scopus.com/inward/record.url?scp=0029931696&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0029931696&partnerID=8YFLogxK

M3 - Article

C2 - 8928918

AN - SCOPUS:0029931696

VL - 270

JO - American Journal of Physiology - Cell Physiology

JF - American Journal of Physiology - Cell Physiology

SN - 0363-6143

IS - 5 39-5

ER -