Human platelet-derived growth factor stimulates amino acid transport and protein synthesis by human diploid fibroblasts in plasma-free media.

Abstract:

:Purified human platelet-derived growth factor (PDGF) induces an increase in amino acid uptake via system A in quiescent human diploid fibroblasts. Cells must be exposed to PDGF for 45 min to obtain maximum transport stimulation. Transport stimulation requires protein synthesis. Transient exposure to PDGF, alone, in the absence of plasma components can stimulate transport. Acid-insoluble [3H]leucine incorporation is also stimulated by PDGF treatment, and this event also does not require the presence of plasma components. Finally, antiserum to PDGF that blocks PDGF-stimulated DNA synthesis in these cells also blocks PDGF-stimulated amino acid uptake and protein synthesis. Increased amino acid uptake and protein synthesis that occur soon after addition of fresh serum to quiescent cells can be attributed to the action of PDGF acting alone and should be useful as markers for the investigation of early cellular events caused by PDGF.

authors

Owen AJ 3rd,Geyer RP,Antoniades HN

doi

10.1073/pnas.79.10.3203

subject

Has Abstract

pub_date

1982-05-01 00:00:00

pages

3203-7

issue

10

eissn

0027-8424

issn

1091-6490

journal_volume

79

pub_type

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