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 language | English |
|---|---|
| Pages (from-to) | 12692-12701 |
| Number of pages | 10 |
| Journal | Journal of Biological Chemistry |
| Volume | 274 |
| Issue number | 18 |
| DOIs | |
| Publication status | Published - Apr 30 1999 |
| Externally published | Yes |
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All Science Journal Classification (ASJC) codes
- Biochemistry
- Molecular Biology
- Cell Biology
Cite this
Normal lysosomal morphology and function in LAMP-1-deficient mice. / Andrejewski, Nicole; Punnonen, Eeva Liisa; Guhde, Gundula; Tanaka, Yoshitaka; Lüllmann-Rauch, Renate; Hartmann, Dieter; Von Figura, Kurt; Saftig, Paul.
In: Journal of Biological Chemistry, Vol. 274, No. 18, 30.04.1999, p. 12692-12701.Research output: Contribution to journal › Article
}
TY - JOUR
T1 - Normal lysosomal morphology and function in LAMP-1-deficient mice
AU - Andrejewski, Nicole
AU - Punnonen, Eeva Liisa
AU - Guhde, Gundula
AU - Tanaka, Yoshitaka
AU - Lüllmann-Rauch, Renate
AU - Hartmann, Dieter
AU - Von Figura, Kurt
AU - Saftig, Paul
PY - 1999/4/30
Y1 - 1999/4/30
N2 - 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.
AB - 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.
UR - http://www.scopus.com/inward/record.url?scp=0033617286&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0033617286&partnerID=8YFLogxK
U2 - 10.1074/jbc.274.18.12692
DO - 10.1074/jbc.274.18.12692
M3 - Article
C2 - 10212251
AN - SCOPUS:0033617286
VL - 274
SP - 12692
EP - 12701
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
SN - 0021-9258
IS - 18
ER -