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Updated: Jul 28, 2026

A Method For Production of Recombinant mCD1d Protein in Insect Cells.
Published on: December 11, 2007
Human CD1d associates with prolyl-4-hydroxylase during its biosynthesis
H S Kim1, S P Colgan, R Pitman
1Division of Gastroenterology, Department of Medicine, Brigham and Women's Hospital, Harvard Medical School, 75 Francis Street, Boston, MA 02115, USA.
The study reveals that prolyl-4-hydroxylase (P4H) associates with CD1d during its biosynthesis in intestinal cells. This interaction leads to hydroxyproline modification in the 37-kDa CD1d form, suggesting a novel post-translational modification pathway.
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- CD1d proteins present glycolipid antigens to T cells.
- CD1d exists in two forms in human intestinal epithelial cells (IECs): 37-kDa (beta2m independent) and 47-kDa (beta2m dependent).
- The biosynthesis and generation mechanisms of these CD1d forms in IECs are currently unknown.
Purpose of the Study:
- To investigate the biosynthetic pathways and generation mechanisms of distinct CD1d forms in human IECs.
- To identify proteins interacting with CD1d during its biosynthesis.
- To determine if CD1d forms contain hydroxyproline residues.
Main Methods:
- Utilized a human colonic cell line (T84) transfected with CD1d.
- Employed pulse-chase metabolic labeling studies.
- Performed microsequencing and amino acid composition analysis.
Main Results:
- CD1d was found to be a stable protein over a 4-day chase period.
- A 65-kDa glycoprotein, identified as prolyl-4-hydroxylase (P4H) subunits, co-immunoprecipitated with CD1d within 24 hours.
- Amino acid analysis confirmed hydroxyproline residues only in the 37-kDa CD1d form, not the 48-kDa form.
Conclusions:
- CD1d exhibits a prolonged association with P4H during biosynthesis.
- The 37-kDa CD1d form contains hydroxyproline residues, indicating a novel post-translational modification.
- P4H association likely contributes to the generation of distinct CD1d biochemical forms.
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