Characterization of the processed form of a ubiquitous protein displaying a variable membrane organization in erythroid cells

Robert Allen, B. A. Hoover

Research output: Contribution to journalArticle

4 Citations (Scopus)

Abstract

We recently identified a group of proteins that are present in all hematopoietic cells but are organized in the cell membrane of erythrocytes in a lineage-specific fashion. One of these polypeptides has a mol wt of approximately 37,000 (p37T) when translated in vitro from messenger RNA (mRNA) extracted from the erythroleukemic K562 cell line. The membrane-associated form of the p37 translation product has been analyzed in detail here. When detergent lysates prepared from biosynthetically labeled K562 cells were reacted with an antiserum containing anti-p37T antibodies, one of the proteins immunoprecipitated had a nominal mol wt of 36,000 to 37,000 (p37M). Several results suggest that this protein is homologous to the p37 translation product: (1) the protein, like the mRNA coding for the p37 translation product, was expressed in cell lines with diverse differentiated phenotypes; (2) the antigenic determinant(s) on p37M and p37T are oriented to the inner surface of the erythrocyte membrane while being oriented to the outer surface of erythroleukemic cells; and (3) one-dimensional peptide maps show homology between p37M and p37T. P37M does not appear to possess an N-terminal leader sequence that is proteolytically cleaved as the molecule is inserted into the membrane. In addition, p37M is not glycosylated.

Original languageEnglish
Pages (from-to)1048-1055
Number of pages8
JournalBlood
Volume65
Issue number5
StatePublished - 1 Jan 1985

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Erythroid Cells
Membranes
K562 Cells
Proteins
Cells
Cell Line
Messenger RNA
Peptides
Erythrocyte Membrane
Cell membranes
Detergents
Immune Sera
Epitopes
Anti-Idiotypic Antibodies
Erythrocytes
Cell Membrane
Phenotype
Molecules

Cite this

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title = "Characterization of the processed form of a ubiquitous protein displaying a variable membrane organization in erythroid cells",
abstract = "We recently identified a group of proteins that are present in all hematopoietic cells but are organized in the cell membrane of erythrocytes in a lineage-specific fashion. One of these polypeptides has a mol wt of approximately 37,000 (p37T) when translated in vitro from messenger RNA (mRNA) extracted from the erythroleukemic K562 cell line. The membrane-associated form of the p37 translation product has been analyzed in detail here. When detergent lysates prepared from biosynthetically labeled K562 cells were reacted with an antiserum containing anti-p37T antibodies, one of the proteins immunoprecipitated had a nominal mol wt of 36,000 to 37,000 (p37M). Several results suggest that this protein is homologous to the p37 translation product: (1) the protein, like the mRNA coding for the p37 translation product, was expressed in cell lines with diverse differentiated phenotypes; (2) the antigenic determinant(s) on p37M and p37T are oriented to the inner surface of the erythrocyte membrane while being oriented to the outer surface of erythroleukemic cells; and (3) one-dimensional peptide maps show homology between p37M and p37T. P37M does not appear to possess an N-terminal leader sequence that is proteolytically cleaved as the molecule is inserted into the membrane. In addition, p37M is not glycosylated.",
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Characterization of the processed form of a ubiquitous protein displaying a variable membrane organization in erythroid cells. / Allen, Robert; Hoover, B. A.

In: Blood, Vol. 65, No. 5, 01.01.1985, p. 1048-1055.

Research output: Contribution to journalArticle

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