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J. Biochem, 1994, Vol. 115, No. 2 293-297
© 1994 Japanese Biochemical Society

research-article

Secretion of {alpha}2-Plasmin Inhibitor Is Impaired by Amino Acid Deletion in a Small Region of the Molecule1

Shigeo Toyota, Shinsaku Hirosawa and Nobuo Aoki2

The First Department of Internal Medicine, Tokyo Medical and Dental University 1-5-45 Yushuna, Bunkyo-ku, Tokyo 113

2To whom correspondence should be addressed.

{alpha}2-Plasmin inhibitor ({alpha}2PI) deficiency Okinawa results from defective secretion of the inhibitor from the liver and appears to be a direct consequence of the deletion of Glu137 in the amino acid sequence of {alpha}2PI. To examine the effects of replacing the amino acid occupying position 137 or deleting its neighboring amino acid on {alpha}2PI secretion, we used oligonucleotide-directed mutagenesis of {alpha}2PI cDNA to change the codon specifying Glu137 or delete a codon specifying its neighboring amino acid. The effects were determined by pulse-chase experiments and by enzyme-linked immunosorbent assay of media from transiently transfected COS-7 cells. Replacement of Glu137 with an amino acid other than Cys had little effect on {alpha}2PI secretion. In contrast, deletion of an amino acid in a region spanning a sequence of less than 30 amino acids including positions 127 and 137 severely impaired the secretion. The results suggest that structural integrity of the region, rather than its component amino acids, is important for the intracellular transport and secretion of {alpha}2PI.

1This work was supported by a Grant-in-Aid for Scientific Research (03454522) from the Ministry of Education, Science and Culture of Japan


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[Abstract] [Full Text] [PDF]


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