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  Biosynthesis and secretion of an osteopontin-related 20-kDa polypeptide in the Madin-Darby canine kidney cell line

Ullrich, O., Mann, K., Haase, W., & Koch-Brandt, C. (1991). Biosynthesis and secretion of an osteopontin-related 20-kDa polypeptide in the Madin-Darby canine kidney cell line. Journal of Biological Chemistry, 266(6), 3518-3525. doi:10.1016/S0021-9258(19)67826-9.

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 Creators:
Ullrich, Oliver1, Author
Mann, Karlheinz2, Author
Haase, Winfried3, Author           
Koch-Brandt, Claudia1, Author
Affiliations:
1Institut für Biochemie, Abteilung Molekulare Genetik, Universität Frankfurt, 6000 Frankfurt am Main, Germany, ou_persistent22              
2Max-Planck-lnstitut für Biochemie, Am Klopferspitz 18 a, 8033 Martinsried, Germany, ou_persistent22              
3Department of Physiology, Max Planck Institute of Biophysics, Max Planck Society, ou_2068297              

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 Abstract: We describe a 20-kDa phosphorylated polypeptide, which is secreted constitutively at the apical surface of the kidney-derived Madin-Darby canine kidney cell line. Using polyclonal antibodies raised against this protein, we show that it is generated from a 60-kDa O-glycosylated, sulfated, and phosphorylated precursor protein by an intracellular proteolytic maturation step, which is pH-sensitive. Amino acid sequence analysis of the 20-kDa secreted polypeptide demonstrated that it displays 70% identity with the carboxyl-terminal amino acids of human osteopontin. The amino-terminal amino acid of the 20-kDa polypeptide corresponds to amino acid 213 of human osteopontin. Thrombin has been shown to cleave rat osteopontin in vivo and in vitro at amino acid 153, yielding two fragments of 28 and 26 kDa. A similar cleavage product can be detected by thrombin treatment of the 60-kDa precursor, suggesting that the precursor is identical or closely related to osteopontin. In the rat nephron, the protein has been localized along the luminal surfaces of the proximal and distal tubule and the collecting duct cells. These results show that in the kidney-derived cell line Madin-Darby canine kidney osteopontin or a closely related protein is proteolytically processed to a 20-kDa polypeptide, raising the possibility that diverse functions of osteopontin in various tissues might be attributed to specific processing to distinct polypeptides.

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Language(s): eng - English
 Dates: 1990-07-182021-01-041991-02-25
 Publication Status: Issued
 Pages: 8
 Publishing info: -
 Table of Contents: -
 Rev. Type: Peer
 Identifiers: DOI: 10.1016/S0021-9258(19)67826-9
PMID: 1995615
 Degree: -

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Title: Journal of Biological Chemistry
  Other : J. Biol. Chem.
Source Genre: Journal
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Publ. Info: Baltimore, etc. : American Society for Biochemistry and Molecular Biology [etc.]
Pages: - Volume / Issue: 266 (6) Sequence Number: - Start / End Page: 3518 - 3525 Identifier: ISSN: 0021-9258
CoNE: https://pure.mpg.de/cone/journals/resource/954925410826