A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms

B. J. Scallon, E. Scigliano, Victoria H. Freedman, M. C. Miedel, Y. C E Pan, J. C. Unkeless, J. P. Kochan

Research output: Contribution to journalArticle

94 Citations (Scopus)

Abstract

Several cDNA clones encoding the human immunoglobulin G receptor CD16 were isolated from human lung or peripheral blood leukocyte cDNA libraries. Nucleotide sequence comparisons revealed that the cDNAs could be divided into two groups. cDNA clones in one group encode a protein that terminates 4 amino acids after the putative transmembrane domain. Clones in the second group encode a protein with an extra 21 amino acids that could comprise a cytoplasmic domain. Direct peptide sequencing was used to determine the N terminus of the mature CD16 receptor protein and supported the existence of the two forms of the receptor. Treatment of neutrophils with phosphatidylinositol-specific phospholipase C resulted in the release of a large percentage of the CD16 molecules from the cell surface. In contrast, treatment of natural killer cells with phosphatidylinositol-specific phospholipase C did not release any CD16 from the cell surface. These data demonstrate that both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms of the CD16 molecule exist and that they are differentially expressed on neutrophils and natural killer cells.

Original languageEnglish (US)
Pages (from-to)5079-5083
Number of pages5
JournalProceedings of the National Academy of Sciences of the United States of America
Volume86
Issue number13
StatePublished - 1989
Externally publishedYes

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IgG Receptors
Glycosylphosphatidylinositols
Phosphoinositide Phospholipase C
Complementary DNA
Clone Cells
Natural Killer Cells
Peptides
Neutrophils
Amino Acids
Proteins
Gene Library
Leukocytes
Lung

ASJC Scopus subject areas

  • General
  • Genetics

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A human immunoglobulin G receptor exists in both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms. / Scallon, B. J.; Scigliano, E.; Freedman, Victoria H.; Miedel, M. C.; Pan, Y. C E; Unkeless, J. C.; Kochan, J. P.

In: Proceedings of the National Academy of Sciences of the United States of America, Vol. 86, No. 13, 1989, p. 5079-5083.

Research output: Contribution to journalArticle

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AU - Scigliano, E.

AU - Freedman, Victoria H.

AU - Miedel, M. C.

AU - Pan, Y. C E

AU - Unkeless, J. C.

AU - Kochan, J. P.

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AB - Several cDNA clones encoding the human immunoglobulin G receptor CD16 were isolated from human lung or peripheral blood leukocyte cDNA libraries. Nucleotide sequence comparisons revealed that the cDNAs could be divided into two groups. cDNA clones in one group encode a protein that terminates 4 amino acids after the putative transmembrane domain. Clones in the second group encode a protein with an extra 21 amino acids that could comprise a cytoplasmic domain. Direct peptide sequencing was used to determine the N terminus of the mature CD16 receptor protein and supported the existence of the two forms of the receptor. Treatment of neutrophils with phosphatidylinositol-specific phospholipase C resulted in the release of a large percentage of the CD16 molecules from the cell surface. In contrast, treatment of natural killer cells with phosphatidylinositol-specific phospholipase C did not release any CD16 from the cell surface. These data demonstrate that both polypeptide-anchored and phosphatidylinositol-glycan-anchored forms of the CD16 molecule exist and that they are differentially expressed on neutrophils and natural killer cells.

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