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Related Experiment Videos

Characterization of FAP-1 expression and function in thyroid follicular cells.

A Myc1, P L Arscott, J D Bretz

  • 1Department of Internal Medicine, Center for Biologic Nanotechnology, University of Michigan, Ann Arbor 48109, USA.

Endocrinology
|October 28, 1999
PubMed
Summary

Human thyrocytes resist Fas-mediated cell death due to Fas-associated phosphatase-1 (FAP-1). Inhibiting FAP-1 with Ac-SLV tripeptide increases thyrocyte death, revealing FAP-1

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Area of Science:

  • Cell Biology
  • Immunology
  • Endocrinology

Background:

  • Human thyrocytes exhibit resistance to Fas-mediated programmed cell death (PCD).
  • A labile protein inhibitor is implicated in thyrocyte protection from PCD, reversible by cycloheximide (CHX).
  • Fas-associated phosphatase-1 (FAP-1) interacts with Fas and inhibits apoptosis in other cell types.

Purpose of the Study:

  • To investigate the role of FAP-1 in protecting human thyrocytes from Fas-mediated PCD.
  • To determine if FAP-1 functions as a PCD inhibitor in thyrocytes.

Main Methods:

  • Detection of FAP-1 mRNA and protein in primary human thyrocytes.
  • Immunohistochemistry and flow cytometry were used to confirm FAP-1 presence.
  • Incubation with Ac-SLV tripeptide (FAP-1 inhibitor) and CHX to assess PCD.

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Main Results:

  • FAP-1 mRNA and protein were detected in human thyrocytes.
  • FAP-1 protein levels decreased in response to CHX.
  • Ac-SLV tripeptide treatment significantly increased thyrocyte cell death, synergistically with CHX.

Conclusions:

  • Fas-associated phosphatase-1 (FAP-1) is present and functional in human thyrocytes.
  • FAP-1 acts as a regulator of Fas-induced programmed cell death in thyrocytes.