Conversion of proteins from a non-polarized to an apical secretory pattern in MDCK cells

Journal Article · Fri May 13 00:00:00 EDT 2005 · Biochemical and Biophysical Research Communications

DOI:https://doi.org/10.1016/j.bbrc.2005.03.030· OSTI ID:20709177

Vogel, Lotte K ^[1]; Larsen, Jakob E ^[1]; Hansen, Martin ^[2]; Truffer, Renato ^[1]

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1. Department of Medical Biochemistry and Genetics, University of Copenhagen (Denmark)
2. Department of Oncology, University of Cambridge, Cambridge (United Kingdom)

Previously it was shown that fusion proteins containing the amino terminus of an apical targeted member of the serpin family fused to the corresponding carboxyl terminus of the non-polarized secreted serpin, antithrombin, are secreted mainly to the apical side of MDCK cells. The present study shows that this is neither due to the transfer of an apical sorting signal from the apically expressed proteins, since a sequence of random amino acids acts the same, nor is it due to the deletion of a conserved signal for correct targeting from the non-polarized secreted protein. Our results suggest that the polarity of secretion is determined by conformational sensitive sorting signals.

• OSTI ID: 20709177
• Journal Information: Biochemical and Biophysical Research Communications, Vol. 330, Issue 3; Other Information: DOI: 10.1016/j.bbrc.2005.03.030; PII: S0006-291X(05)00516-4; Copyright (c) 2005 Elsevier Science B.V., Amsterdam, The Netherlands, All rights reserved; Country of input: International Atomic Energy Agency (IAEA); ISSN 0006-291X
• Country of Publication: United States
• Language: English

Related Subjects

60 APPLIED LIFE SCIENCES
AMINO ACID SEQUENCE
AMINO ACIDS
PROTEINS
RANDOMNESS
SECRETION
SIGNALS
SORTING