| Accumulation of Ym1 and formation of intracellular crystalline bodies in alveolar macrophages lacking heparanase. | |
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MedLine Citation:
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PMID: 20226534 Owner: NLM Status: MEDLINE |
Abstract/OtherAbstract:
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Heparanase is a heparan sulfate (HS) degrading endoglucuronidase that has been implicated in cell migration and inflammatory conditions. Here we used mice deficient of heparanase (Hpse(-/-)) to study the impact of heparanase on airway leukocytes. Normal numbers of macrophages and lymphocytes were present in bronchoalveolar lavage fluid of Hpse(-/-) mice, indicating that heparanase is not essential for proper homing of leukocytes to airways. While lymphocytes from Hpse(-/-) mice displayed normal morphology, Hpse(-/-) alveolar macrophages showed a striking, age-dependent appearance of granule-like structures in the cytoplasm. Transmission electron microscopy revealed that these structures corresponded to membrane-enclosed crystalline bodies that closely resembled the intracellular crystals known to be formed by the HS-binding protein Ym1, suggesting that heparanase deficiency is associated with intracellular Ym1 deposition. Indeed, applying immunocytochemistry, we found markedly higher levels of intracellular Ym1 protein in Hpse(-/-) versus WT alveolar macrophages, and there was a significant correlation between levels of Ym1 protein detected by immunoblotting and amounts of crystalline material in BAL cells. Biosynthetic radio-labeling of the macrophages revealed accumulation of non-degraded HS chains in Hpse(-/-) macrophages. Together, these findings implicate heparanase in normal processing of HS in macrophages, and indicate that heparanase regulates intracellular Ym1 accumulation and crystal formation in airways. |
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Authors:
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Ida Waern; Juan Jia; Gunnar Pejler; Eyal Zcharia; Israel Vlodavsky; Jin-Ping Li; Sara Wernersson |
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Publication Detail:
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Type: Journal Article; Research Support, Non-U.S. Gov't Date: 2010-03-11 |
Journal Detail:
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Title: Molecular immunology Volume: 47 ISSN: 1872-9142 ISO Abbreviation: Mol. Immunol. Publication Date: 2010 Apr |
Date Detail:
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Created Date: 2010-04-05 Completed Date: 2010-04-22 Revised Date: 2011-12-07 |
Medline Journal Info:
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Nlm Unique ID: 7905289 Medline TA: Mol Immunol Country: England |
Other Details:
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Languages: eng Pagination: 1467-75 Citation Subset: IM |
Copyright Information:
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Copyright 2010 Elsevier Ltd. All rights reserved. |
Affiliation:
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Department of Anatomy, Physiology and Biochemistry, Swedish University of Agricultural Sciences, Sweden. |
Export Citation:
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| MeSH Terms | |
Descriptor/Qualifier:
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Animals Cell Line Cell Shape Crystallins / metabolism* Glucuronidase / deficiency, metabolism* Intracellular Space / metabolism Lectins / metabolism* Macrophages, Alveolar / immunology, metabolism*, ultrastructure Mice Mice, Knockout Microscopy, Electron, Transmission beta-N-Acetylhexosaminidases / metabolism* |
| Grant Support | |
ID/Acronym/Agency:
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R01 CA106456-09/CA/NCI NIH HHS |
| Chemical | |
Reg. No./Substance:
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0/Crystallins; 0/Lectins; EC 3.2.1.-/heparanase; EC 3.2.1.31/Glucuronidase; EC 3.2.1.52/Chi3l3 protein, mouse; EC 3.2.1.52/beta-N-Acetylhexosaminidases |
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