Glycosylated forms of nuclear lamins

Chromatin and pore complex-lamina preparations were obtained from pig and chicken tissues, and their proteins were analysed by mono- and bidimensional electrophoresis. A glycosylated form of lamin A, recognized by concanavalin A, was shown to be present in at least 3 of the tissues examined. Glycosy...

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Veröffentlicht in:	FEBS Letters 1989-11, Vol.257 (2), p.241-246
Hauptverfasser:	Ferrare, A., Eufemi, M., Cervoni, L., Marinetti, R., Turano, C.
Format:	Artikel
Sprache:	eng
Schlagworte:	Analytical, structural and metabolic biochemistry Animals Biological and medical sciences Cell Nucleus - metabolism Chickens Chromatin - metabolism Concanavalin A Concanavalin A - metabolism Electrophoresis, Gel, Two-Dimensional Fundamental and applied biological sciences. Psychology Glycoprotein Glycosylation Holoproteins Lamin Lamin Type A Lamins Molecular Weight Nuclear proteins Nuclear Proteins - metabolism nuclei Proteins Swine
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Beschreibung
Zusammenfassung:	Chromatin and pore complex-lamina preparations were obtained from pig and chicken tissues, and their proteins were analysed by mono- and bidimensional electrophoresis. A glycosylated form of lamin A, recognized by concanavalin A, was shown to be present in at least 3 of the tissues examined. Glycosylation is suggested to be a further postsynthetic modification, besides phosphorylation and methylation, which can modify the properties of lamins.
ISSN:	0014-5793 1873-3468
DOI:	10.1016/0014-5793(89)81543-1