Structure and function of the Golgi complex in rice cells: characterization of Golgi membrane glycoproteins
1993
Kimura, S. | Yamada, M. | Igaue, I. | Mitsui, T.
The structure and synthesis of the saccharide chains of Golgi membrane glycoproteins in suspension-cultured rice (Oryza sativa L.) cells were studied. Peanut lectin (PNA) and Ulex europaeus lectin-I (UEA-I) have high affinity for typical O-linked saccharide chains and both recognized the saccharide chains of rice Golgi membrane glycoproteins. These glycoproteins were also sensitive to alkali and to O-glycanase. These results indicate that the Golgi membrane glycoproteins have O-linked saccharide chains. Brefeldin A, a specific inhibitor of Golgi-mediated secretion, induced morphological changes in Golgi complexes and prevented the synthesis of the saccharide chains of the membrane glycoproteins that could be recognized by PNA and UEA-I. These glycoproteins were typically localized in all compartments of the Golgi complex. Monensin can arrest the transport of secretory proteins from medial to trans Golgi compartments but did not affect the formation and localization of the Golgi membrane glycoproteins. Tunicamycin, an inhibitor of the synthesis of N-linked saccharide chains, did not inhibit the synthesis of the saccharide chains of these Golgi membrane glycoproteins. These results strongly suggest that the synthesis of O-linked saccharide chains of Golgi membrane glycoproteins is initiated in the cis Golgi compartment.
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