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Updated: Jul 10, 2026

08:07
Identification of Plasmodesmal Localization Sequences in Proteins In Planta
Published on: August 15, 2017
P-セレクチンのPSGL-1認識は,PSGL-1アミノ端末のチロシン硫化コンセンサスによって制御されます
1Department of Genetics, Harvard Medical School, Massachusetts General Hospital, Boston 02114, USA.
Cell
|October 20, 1995
まとめ
P-セレクチン・グリコプロテイン・リガンド1 (PSGL-1) のチロシン硫化作用は,P-セレクチンが中性粒子の結合に不可欠である. 硫化を阻害すると,この重要な細胞粘着プロセスが著しく弱まります.
科学分野:
- 細胞および分子生物学
- 免疫学 免疫学とは
- グライコバイオロジーは,
背景:
- P-セレクチンは,活性化された内皮への中性粒子の粘着を媒介する.
- P-セレクチングリコタンパク質リガンド1 (PSGL-1) とシアリルルイスX (sLex) は,この相互作用の重要な決定因子である.
研究 の 目的:
- PSGL-1およびP-セレクチン結合におけるチロシン硫化作用を調査する.
- P-セレクチン粘着に欠かせないPSGL-1の特定の領域を特定する.
主な方法:
- PSGL-1タイロシンのサイト指向型変異.
- PSGL-1合成中の硫化抑制.
- HL-60細胞とP-セレクチンでコーティングされた表面を用いた細胞粘着測定法.
- ムシンのような分子を含む機能的研究.
主要な成果:
- ティロシン硫化コンセンサスを含むPSGL-1の特定のN末端セグメントは,P-セレクチン結合に不可欠である.
- 硫化阻害剤で合成されたPSGL-1は,弱いP-セレクチン結合を示す.
- N端のチロシンからフェニララニンへの変異は,P-セレクチン結合を廃止する.
- N端のセグメントは,他のムシンのような分子にPセレクチン結合能力を授与することができます.
結論:
- PSGL-1のN端のチロシン硫化は,P-セレクチン媒介による中性粒子の粘着に不可欠である.
- この硫化現象は,PSGL-1をP-selectin.によって認識するための決定的な決定因子です.
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