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6416240 
Journal Article 
Characterization of a human glycoprotein (erythropoietin) produced in cultured tobacco cells 
Matsumoto, S; Ikura, K; Ueda, M; Sasaki, R 
1995 
1 
Plant Molecular Biology
ISSN: 0167-4412
EISSN: 1573-5028 
27 
6 
1163-1172 
English 
7766897 
Erythropoietin (Epo), a glycoprotein that regulates the formation of erythrocytes in mammals, was produced in cultured tobacco BY2 cells (Nicotiana tabacum L. cv. Bright Yellow 2) by introducing human Epo cDNA via Agrobacterium tumefaciens-mediated gene transfer. Epo was correctly processed and subsequently penetrated the plasma membrane of tobacco cells. However, it remained attached to the cell wall and was not released into the culture medium. Although Epo produced by tobacco cells was glycosylated with N-linked oligosaccharides, these carbohydrates were smaller than those of the recombinant Epo produced in mammalian cells. Epo produced in tobacco exhibited in vitro biological activities by inducing the differentiation and proliferation of erythroid cells. However, it had no in vivo biological activities. A lectin-binding assay indicated the lack of sialic acid residues in the N-linked oligosaccharides of Epo, suggesting that Epo was removed from the circulation before it reached erythropoietic tissues. 
; Amino Acid Sequence; Carbohydrates/analysis; Cells; Cultured; Cloning; Molecular; DNA; Complementary; Erythropoietin/chemistry; Erythropoietin/genetics; Humans; Molecular Sequence Data; Plants; Toxic; Protein Conformation; Recombinant Proteins/chemistry; Recombinant Proteins/genetics; Tobacco/cytology; Tobacco/genetics; Index Medicus/