Normal lysosomal morphology and function in LAMP-1-deficient mice

Nicole Andrejewski, Eeva Liisa Punnonen, Gundula Guhde, Yoshitaka Tanaka, Renate Lüllmann-Rauch, Dieter Hartmann, Kurt Von Figura, Paul Saftig

Research output: Contribution to journalArticlepeer-review

130 Citations (Scopus)

Abstract

Lysosomal membranes contain two highly glycosylated proteins, designated LAMP-1 anti LAMP-2, as major components. LAMP-1 and LAMP-2 are structurally related. To investigate the physiological role of LAMP-1, we have generated mice deficient for this protein. LAMP-1-deficient mice are viable and fertile. In LAMP-1-deficient brain, a mild regional astrogliosis and altered immunoreactivity against cathepsin-D was observed. Histological and ultrastructural analyses of all other tissues did not reveal abnormalities. Lysosomal properties, such as enzyme activities, lysosomal pH, osmotic stability, density, shape, and subcellular distribution were not changed in comparison with controls. Western blot analyses of LAMP-1-deficient and heterozygote tissues revealed an up-regulation of the LAMP-2 protein pointing to a compensatory effect of LAMP-2 in response to the LAMP-1 deficiency. The increase of LAMP-2 was neither correlated with an increase in the level of lamp-2 mRNAs nor with increased half-life time of LAMP-2. This findings suggest a translational regulation of LAMP-2 expression.

Original languageEnglish
Pages (from-to)12692-12701
Number of pages10
JournalJournal of Biological Chemistry
Volume274
Issue number18
DOIs
Publication statusPublished - Apr 30 1999
Externally publishedYes

All Science Journal Classification (ASJC) codes

  • Biochemistry
  • Molecular Biology
  • Cell Biology

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