T Cell maturation stage-linked heterogeneity of the glycosylphosphatidylinositol membrane anchor of Thy-1

Izumi Nakashima, Tomoaki Yoshida, Yue Hua Zhang, Mei Yi Pu, Ryo Taguchi, Hiroh Ikezawa, Ken Ichi Isobe, Takashi Iwamoto, Masashi Kato, Tint Lwin, Mahbuba Parvin

Research output: Contribution to journalArticlepeer-review

4 Citations (Scopus)

Abstract

We showed that some of Thy-1 molecules on murine thymocytes are resistant to phosphatidylinositol-specific phospholipase C (PI-PLC) derived from Bacillus thuringiensis. Both immature thymocytes with low CD3 expression and mature thymic T lymphocytes with high CD3 expression carried the PI-PLC-resistant Thy-1, and the PI-PLC-sensitivity of Thy-1 extensively varied among thymocyte subpopulations. In contrast, the same PI-PLC fully hydrolysed the anchor of Thy-1 on peripheral T lymphocytes. When the latter cells were activated with mitogen in vitro, however, some Thy-1 on them became resistant to PI-PLC. We then found that virtually all Thy-1 molecules on thymocytes became sensitive to PI-PLC when they were treated with hydroxylamine that should cleave ester-linked lipids. The result ruled out the possibility that the PI-PLC-resistant Thy-1 had a trans membraneous peptide sequence, and suggested the presence of an additional fatty acyl group on the inositol ring of the Thy-1 anchor. In addition, the molecular size of the PI-PLC-resistant membrane-bound Thy-1 was only marginally larger than that of the PI-PLC-sensitive solubilized Thy-1 in detergent-partitioning SDS-PAGE analysis.

Original languageEnglish
Pages (from-to)466-474
Number of pages9
JournalImmunobiology
Volume185
Issue number5
DOIs
Publication statusPublished - 1992
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Immunology and Allergy
  • Immunology
  • Hematology

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