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The inactivation of the sortilin gene leads to a partial disruption of prosaposin trafficking to the lysosomes

Zeng, Jibin, Racicott, Jesse, Morales, Carlos R.·2009·Experimental Cell Research
DOI 10.1016/j.yexcr.2009.08.016
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Abstract

Lysosomes are intracellular organelles which contain enzymes and activator proteins involved in the digestion and recycling of a variety of cellular and extracellular substances. We have identified a novel sorting receptor, sortilin, which is involved in the lysosomal trafficking of the sphingolipid activator proteins, prosaposin and GM(2)AP, and the soluble hydrolases cathepsin D, cathepsin H, and acid sphingomyelinase. Sortilin belongs to a growing family of receptors with homology to the yeast Vps10 protein, which acts as a lysosomal sorting receptor for carboxypeptidase Y. In this study we examined the effects of the sortilin gene inactivation in mice. The inactivation of this gene did not yield any noticeable lysosomal pathology. To determine the existence of an alternative receptor complementing the sorting function of sortilin, we quantified the concentration of prosaposin in the lysosomes of the nonciliated epithelial cells lining the efferent ducts. These cells were chosen because they express sortilin and have a large number of lysosomes containing prosaposin. In addition, the nonciliated cells are known to endocytose luminal prosaposin that is synthesized and secreted by Sertoli cells into the seminiferous luminal fluids. Consequently, the nonciliated cells are capable of targeting both exogenous and endogenous prosaposin to the lysosomes. Using electron microscope immunogold labeling and quantitative analysis, our results demonstrate that inactivation of the sorti…

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  • Sortilin is a lysosomal sorting protein that binds ligands both in the Golgi apparatus and at the plasma membrane and traffics them to the lysosome.

    “Sortilin is a lysosomal sorting protein that binds ligands both in the Golgi apparatus and at the plasma membrane and traffics them to the lysosome.”

    From Hepatic sortilin regulates both apolipoprotein B secretion and LDL catabolism (2012) · cites this paper as [7]

  • In a sortilin-knockout mouse devoid of any sortilin protein, on a chow diet, sortilin deficiency was associated with reduced APOB production.

    “Using a different sortilin-knockout mouse proven to be devoid of any sortilin protein (7), we found that on a chow diet, sortilin deficiency was associated with reduced APOB production (data not shown).”

    From Hepatic sortilin regulates both apolipoprotein B secretion and LDL catabolism (2012) · cites this paper as [7]

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Metadata

Authors
Zeng, J., Racicott, J., & Morales, C. R.
Venue
Experimental Cell Research
Publisher
Elsevier BV
Published
2009-11
Volume
315
Issue
18
Pages
3112-3124
ISSN
0014-4827
DOI
10.1016/j.yexcr.2009.08.016
Cited by
54
References
1
Language
en
Licence
www.elsevier.com/tdm/userlicense/1.0/ (tdm)

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