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Related Experiment Video

Updated: Jul 28, 2026

A Method For Production of Recombinant mCD1d Protein in Insect Cells.

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.

Molecular Immunology

|March 21, 2001

Summary

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.

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Published on: October 29, 2018

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.