Abstract
MR1 is a major histocompatibility complex (MHC) class I-related gene conserved among mammals, and its predicted amino acid sequence is relatively closer to the classical MHC class I molecules among several divergent class I molecules. However, as its molecular nature and function have not yet been clarified, we set out in this study to establish transfected P388 murine cell lines that stably produce a large number of MR1 proteins and conducted analyses to investigate the molecular nature of MR1. Immunoprecipitation and Western blot analyses with specific antisera revealed that the MR1 protein can associate with β2-microglobulin, suggesting its molecular form of a typical class I heterodimer composed of a heavy and a light chain (β2-microglobulin), like the classical MHC class I molecules.
| Original language | English |
|---|---|
| Pages (from-to) | 722-729 |
| Number of pages | 8 |
| Journal | Biochemical and Biophysical Research Communications |
| Volume | 290 |
| Issue number | 2 |
| DOIs | |
| Publication status | Published - 01-01-2002 |
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All Science Journal Classification (ASJC) codes
- Biophysics
- Biochemistry
- Molecular Biology
- Cell Biology
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Association of MR1 protein, an MHC class I-related molecule, with β2-microglobulin. / Yamaguchi, Hisateru; Hashimoto, Keiichiro.
In: Biochemical and Biophysical Research Communications, Vol. 290, No. 2, 01.01.2002, p. 722-729.Research output: Contribution to journal › Article
TY - JOUR
T1 - Association of MR1 protein, an MHC class I-related molecule, with β2-microglobulin
AU - Yamaguchi, Hisateru
AU - Hashimoto, Keiichiro
PY - 2002/1/1
Y1 - 2002/1/1
N2 - MR1 is a major histocompatibility complex (MHC) class I-related gene conserved among mammals, and its predicted amino acid sequence is relatively closer to the classical MHC class I molecules among several divergent class I molecules. However, as its molecular nature and function have not yet been clarified, we set out in this study to establish transfected P388 murine cell lines that stably produce a large number of MR1 proteins and conducted analyses to investigate the molecular nature of MR1. Immunoprecipitation and Western blot analyses with specific antisera revealed that the MR1 protein can associate with β2-microglobulin, suggesting its molecular form of a typical class I heterodimer composed of a heavy and a light chain (β2-microglobulin), like the classical MHC class I molecules.
AB - MR1 is a major histocompatibility complex (MHC) class I-related gene conserved among mammals, and its predicted amino acid sequence is relatively closer to the classical MHC class I molecules among several divergent class I molecules. However, as its molecular nature and function have not yet been clarified, we set out in this study to establish transfected P388 murine cell lines that stably produce a large number of MR1 proteins and conducted analyses to investigate the molecular nature of MR1. Immunoprecipitation and Western blot analyses with specific antisera revealed that the MR1 protein can associate with β2-microglobulin, suggesting its molecular form of a typical class I heterodimer composed of a heavy and a light chain (β2-microglobulin), like the classical MHC class I molecules.
UR - http://www.scopus.com/inward/record.url?scp=0036297768&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0036297768&partnerID=8YFLogxK
U2 - 10.1006/bbrc.2001.6277
DO - 10.1006/bbrc.2001.6277
M3 - Article
C2 - 11785959
AN - SCOPUS:0036297768
VL - 290
SP - 722
EP - 729
JO - Biochemical and Biophysical Research Communications
JF - Biochemical and Biophysical Research Communications
SN - 0006-291X
IS - 2
ER -