Molecular mechanisms of prostaglandin transport

Research output: Contribution to journalArticle

134 Citations (Scopus)

Abstract

Despite the fact that prostaglandins (PGs) have low intrinsic permeabilities across the plasma membrane, they must cross it twice: first upon release from the cytosol into the blood, and again upon cellular uptake prior to oxidation. Until recently, there were no cloned carriers that transported PGs. PGT is a broadly-expressed, 12-membrane-spanning domain integral membrane protein. When heterologously expressed in HeLa cells or Xenopus oocytes, it catalyzes the rapid, specific, and high-affinity uptake of PGF2, PGF(2α), PGD2, 8-iso-PGF(2α), and thromboxane B2. Functional studies indicate that PGT transports its substrate as the charged anion. The PGT substrate specificity and inhibitor profile match remarkably well with earlier in situ studies on the metabolic clearance of PGs by rat lung. Because PGT expression is especially high in this tissue, it is likely that PGT mediates the membrane step in PG clearance by the pulmonary circulation. Evidence is presented that PGT may play additional roles in other tissues and that there may be additional PG transporters yet to be identified molecularly.

Original languageEnglish (US)
Pages (from-to)221-242
Number of pages22
JournalAnnual Review of Physiology
Volume60
DOIs
StatePublished - 1998

Fingerprint

Prostaglandins
Prostaglandins F
Prostaglandin D2
Thromboxane B2
Dinoprost
Pulmonary Circulation
Membranes
Substrate Specificity
Xenopus
HeLa Cells
Cytosol
Oocytes
Anions
Permeability
Membrane Proteins
Cell Membrane
Lung

Keywords

  • Biological transport
  • Carrier proteins
  • Eicosanoids
  • Molecular cloning

ASJC Scopus subject areas

  • Physiology

Cite this

Molecular mechanisms of prostaglandin transport. / Schuster, Victor L.

In: Annual Review of Physiology, Vol. 60, 1998, p. 221-242.

Research output: Contribution to journalArticle

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