Editorial: Heparan sulfate-binding proteins in health and disease.

Front Mol Biosci

Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States.

Published: March 2024

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http://www.ncbi.nlm.nih.gov/pmc/articles/PMC10988385PMC
http://dx.doi.org/10.3389/fmolb.2024.1386623DOI Listing

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Polymerizing laminins in development, health, and disease.

J Biol Chem

July 2024

Department of Biochemistry and Microbiology, Institute for Quantitative Biomedicine, Rutgers University, Piscataway, New Jersey, USA.

Polymerizing laminins are multi-domain basement membrane (BM) glycoproteins that self-assemble into cell-anchored planar lattices to establish the initial BM scaffold. Nidogens, collagen-IV and proteoglycans then bind to the scaffold at different domain loci to create a mature BM. The LN domains of adjacent laminins bind to each other to form a polymer node, while the LG domains attach to cytoskeletal-anchoring integrins and dystroglycan, as well as to sulfatides and heparan sulfates.

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Editorial: Heparan sulfate-binding proteins in health and disease.

Front Mol Biosci

March 2024

Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies, Rensselaer Polytechnic Institute, Troy, NY, United States.

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Heparan sulfate proteoglycans (HSPGs) surround the surface of odontoblasts, and their modification affects their affinity for Wnt ligands. This study proposes applying Matching Transformation System (MA-T), a novel chlorinated oxidant, to enhance dentinogenesis. MA-T treatment in odontoblasts decreased sulfation of HSPG and upregulated the expression of () and () via activation of canonical Wnt signaling .

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Introduction: We discovered that the APOE3 Christchurch (APOE3Ch) variant may provide resistance to Alzheimer's disease (AD). This resistance may be due to reduced pathological interactions between ApoE3Ch and heparan sulfate proteoglycans (HSPGs).

Methods: We developed and characterized the binding, structure, and preclinical efficacy of novel antibodies targeting human ApoE-HSPG interactions.

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