Heparanase cleavage of perlecan heparan sulfate modulates FGF10 activity during ex vivo submandibular gland branching morphogenesis

@inproceedings{Patel2007HeparanaseCO,  title={Heparanase cleavage of perlecan heparan sulfate modulates FGF10 activity during ex vivo submandibular gland branching morphogenesis},  author={Vaishali N Patel and Sarah M. Knox and Karen M Likar and Colin A Lathrop and Rydhwana Hossain and Siavash Eftekhari and John M. Whitelock and Michael Elkin and Israel Vlodavsky and Matthew P. Hoffman},  booktitle={Development},  year={2007},  url={https://api.semanticscholar.org/CorpusID:25819221}}
Results show heparanase releases FGF10 from perlecan HS in the basement membrane, increasing MAPK signaling, epithelial clefting, and lateral branch formation, which results in increased branching morphogenesis.

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65 References

Heparanase Uptake Is Mediated by Cell Membrane Heparan Sulfate Proteoglycans*

Evidence is provided that heparanase resides in the endosomal/lysosomal compartment for a relatively long period of time and is likely to play a role in the normal turnover of HS, and co-localization studies and cell fractionation following heparinase addition identify syndecan family members as candidate molecules responsible for heparAnase uptake.

Heparan sulfates expressed in the distal lung are required for Fgf10 binding to the epithelium and for airway branching.

It is shown that altering endogenous gradients of HS sulfation with sodium chlorate or over-O-sulfated synthetic heparin in lung organ cultures dramatically decreases Fgf10 binding, and that under these conditions epithelial binding is not improved by providing exogenous FGF10, and the data suggest that, not only ligand availability, but also the presence of specific patterns of HS modification in the distal lung epithelium are critical determinants of FgF10 binding

Heparanase Degrades Syndecan-1 and Perlecan Heparan Sulfate

It is demonstrated that cell-surface syndecan-1 and ECM perlecan are degradative targets of HPSE-1, and syndeca-1 regulates HPSe-1 biological activity, which suggest that expression of syndecans-1 on the melanoma cell surface and its degradation by HPS e-1 are important determinants in the control of tumor cell invasion and metastasis.

Role of heparan sulfate as a tissue-specific regulator of FGF-4 and FGF receptor recognition

It is suggested that FGF and FR recognition of specific HS sulfation patterns is critical for the activation of FGF signaling, and that synthesis of these patterns is regulated during embryonic development.

Activation, processing and trafficking of extracellular heparanase by primary human fibroblasts.

It is shown that primary human fibroblasts are capable of binding and converting the 65 kDa heparanase precursor into its highly active 50 kDa form, concomitantly with its cytoplasmic accumulation.

Enzymatic remodeling of heparan sulfate proteoglycans within the tumor microenvironment: Growth regulation and the prospect of new cancer therapies

This review focuses on remodeling of HSPGs by three distinct mechanisms that occur in vivo; shedding of proteoglycan extracellular domains from cell surfaces, fragmentation of heparan sulfate chains byHeparanase, and removal of sulfates from the 6‐O position of heParan sulfates chains by ext racellular sulfatases.

Not all Perlecans are Created Equal: Interactions with Fibroblast Growth Factor 2 and FGF receptors

It is shown that the bioactivity of HS decorating a single PG is dependent on its cell source and that subtle changes in structure including secondary interactions have a profound effect on biological activity.
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