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Etude de p76, une nouvelle protéine mannose-6-phosphate : caractérisations biochimiques, localisation lysosomale et approche de la fonction.

Abstract : The protein « p76 » (« hypothetical protein LOC196463 ») was identified some years ago in our laboratory during the course of a proteomic analysis of mannose-6-phosphate proteins purified from human cell lines. The present thesis describes the biochemical characterisation and the intracellular localisation of p76, as well as some functional tests carried out with recombinant p76. We demonstrated that human p76 sequence bears 6 N-glycosylations and that mannose-6-phosphate sugars were present. Proteolytic maturation of human and murine p76 precursors was observed; a few intermediate forms were partially characterised thanks to anti-p76 antibodies which were developed in the laboratory. Most importantly, we were able to demonstrate the lysosomal localisation of this protein by both immunofluorescence and sub-cellular fractionation of mouse liver homogenates. As p76 shows a significant sequence homology to a recently cloned phospholipase B from Dictyostelium discoideum, some functional tests were performed, but no phospholipase activity could be detected with recombinant hp76-myc. However, a fat blot experiment showed that hp76-myc binds cardiolipin, a particular phospholipid enriched in mitochondrial and bacterial membranes.
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https://tel.archives-ouvertes.fr/tel-00157044
Contributor : Anaïs Jensen <>
Submitted on : Monday, June 25, 2007 - 11:42:42 AM
Last modification on : Friday, November 6, 2020 - 4:08:47 AM
Long-term archiving on: : Thursday, April 8, 2010 - 9:27:34 PM

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  • HAL Id : tel-00157044, version 1

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Anaïs Jensen. Etude de p76, une nouvelle protéine mannose-6-phosphate : caractérisations biochimiques, localisation lysosomale et approche de la fonction.. Biochimie [q-bio.BM]. Université Joseph-Fourier - Grenoble I, 2007. Français. ⟨tel-00157044⟩

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