A multifunctional protein: involvement of the alpha-1 serum protease inhibitor in SDS and high salt-stable DNA-protein complexes

• Published in: FEBS letters 1997-08, Vol.413 (1), p.50-54
• Main Authors: Glaser, Tova, Rothbarth, Karsten, Stammer, Hermann, Kempf, Tore, Spiess, Eberhard, Werner, Dieter
• Format: Article
• Language: English
• Subjects: alpha 1-Antitrypsin - genetics; alpha 1-Antitrypsin - isolation & purification; alpha 1-Antitrypsin - metabolism; alpha 1-Antitrypsin - ultrastructure; Alpha-1 antitrypsin; Alpha-1 serum protease inhibitor; Amino Acid Sequence; Animals; Blotting, Western; Carcinoma, Ehrlich Tumor - chemistry; DNA-Binding Proteins - genetics; DNA-Binding Proteins - isolation & purification; DNA-Binding Proteins - metabolism; DNA-Binding Proteins - ultrastructure; Endopeptidase K - pharmacology; Fluorescent Antibody Technique, Indirect; Green fluorescent protein; Molecular Sequence Data; Multifunctional proteins; Nuclear protein; Recombinant Proteins - metabolism; Sodium Dodecyl Sulfate - pharmacology
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(97)00876-4

Occasionally new and intriguing roles arise for proteins with well established functions. The alpha-1 serum protease inhibitor (α-1 PI) represents another example. Sequence identities exist in the α-1 PI and in a nuclear 52-kDa glycoprotein which is involved in resistant DNA-polypeptide complexes. The results of Western blots support the identity of the two proteins and immunocytochemical studies indicate the nuclear location of the α-1 PI. Consistently, e.g. Ehrlich ascites tumor cells express the α-1 PI, and the fusion protein between the α-1 PI and the green fluorescent protein from Aequorea victoria shows intracellular accumulation and partly nuclear location.