Isolation and Partial Characterization of a Murine Cell Surface Glycoprotein with Affinity for Exogenously Added β<sub>2</sub>‐Microglobulin

Sege, Karin; Peterson, Per A.

doi:10.1111/j.1365-3083.1980.tb00014.x

Cited by 5 publications

(1 citation statement)

References 20 publications

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“…We conclude that the HLA antigen heavy chains in DAUDI cells are normally synthesized but not terminally glycosylated. These data have been presented in preliminary form (Sege & Peterson, 1980).…”

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confidence: 99%

Role of .beta.2-microglobulin in the intracellular processing of HLA antigens

Sege¹,

Rask²,

Peterson³

1981

Biochemistry

110

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The biosynthesis of HLA-A, -B, and -C antigens was examined in the two lymphoblastoid cell lines DAUDI and RAJI. In RAJI cells the HLA-A, -B, and -C antigen heavy chains become core-glycosylated in the endoplasmic reticulum as evidenced by their sensitivity to endo-H digestion and tunicamycin treatment. Beta2-Microglobulin is present in excess in the endoplasmic reticulum of the RAJI cells and associates with the heavy chain at the time of synthesis of the heavy chain. Pulse-chase experiments demonstrated that the RAJI HLA-A, -B, and -C antigen heavy chains become terminally glycosylated since their changed characteristics included resistance to endo-H digestion, sensitivity to neuraminidase treatment, and incorporation fucose. DAUDI HLA-A, -B, and -C antigen heavy chains are synthesized normally and become core-glycosylated but not terminally glycosylated. Other glycosylated cell surface proteins, like the HLA-DR antigens, display normal glycosylation in DAUDI cells. Therefore it is unlikely that the absence of terminally glycosylated HLA-A, -B, and -C antigen heavy chains is the result of a general defect in the biosynthetic machinery of DAUDI cells. However, DAUDI cells lack the ability to synthesize beta2-microglobulin, the common subunit of all HLA-A, -B, and -C antigens. Therefore, it seems reasonable to conclude that beta2-microglobulin is of importance for intracellular transport of newly synthesized HLA-A, -B, and -C antigens.

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mentioning

confidence: 99%

Role of .beta.2-microglobulin in the intracellular processing of HLA antigens

Sege¹,

Rask²,

Peterson³

1981

Biochemistry

110

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Β2-microglobulin secretion from lymphoid cells: A study at the cellular level

Hammarström

Smith

1985

Med Microbiol Immunol

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A protein plaque assay was developed for the detection of human lymphocytes secreting beta 2-microglobulin. The development of plaques required production of beta 2-microglobulin by viable cells at an estimated rate exceeding 25 molecules per second. It has previously been suggested that beta 2-microglobulin secretion is restricted to certain lymphoid cell subpopulations. However, both T- and B-cells were shown to form plaques in normal donors and immunodeficient patients after activation with various mitogens. A close correlation between beta 2-microglobulin production and DNA synthesis was evident. However, secretion of immunoglobulin did not correlate with the proportion of cells secreting beta 2-microglobulin.

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