ArticleThe Journal of biological chemistry2013
Acidic domain in dentin phosphophoryn facilitates cellular uptake: implications in targeted protein delivery.
Article in The Journal of biological chemistry, 2013. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 18 papers.
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Who cites it
18 citing papers in PubMed, 28 citations in OpenAlex.
- Transcriptome profiling of DPP stimulated DPSCs identifies the role of autophagy in odontogenic differentiation.Journal of structural biology · 2024Article
- Bone-targeting engineered milk-derived extracellular vesicles for MRI-assisted therapy of osteoporosis.Regenerative biomaterials · 2024Article
- Bone-Targeting Peptide and RNF146 Modified Apoptotic Extracellular Vesicles Alleviate Osteoporosis.International journal of nanomedicine · 2024Article
- Design of bacteriophage T4-based artificial viral vectors for human genome remodeling.Nature communications · 2023Article
- Mitochondrial Targeting Probes, Drug Conjugates, and Gene Therapeutics.Methods in molecular biology (Clifton, N.J.) · 2022Article
- Dentine sialophosphoprotein signal in dentineogenesis and dentine regeneration.European cells & materials · 2021Review
- Allosteric interference in oncogenic FLI1 and ERG transactions by mithramycins.Structure (London, England : 1993) · 2021Article
- Cytosolic delivery of membrane-penetrating QDs into T cell lymphocytes: implications in immunotherapy and drug delivery.Nanoscale · 2021Article
- Preparation and Characterization of Dentin Phosphophoryn-Derived Peptide-Functionalized Lignin Nanoparticles for Enhanced Cellular Uptake.Small (Weinheim an der Bergstrasse, Germany) · 2019Article
- Inhibition of osteoblastic Smurf1 promotes bone formation in mouse models of distinctive age-related osteoporosis.Nature communications · 2018Article
- Single domain antibodies for the knockdown of cytosolic and nuclear proteins.Protein science : a publication of the Protein Society · 2017Review
- Endocytosis in gene therapy with non-viral vectors.Wiener medizinische Wochenschrift (1946) · 2016Review
- QD-Based FRET Probes at a Glance.Sensors (Basel, Switzerland) · 2015Review
- Dentin Matrix Proteins in Bone Tissue Engineering.Advances in experimental medicine and biology · 2015Review
- Multifunctional ECM proteins in bone and teeth.Experimental cell research · 2014Review
- Adhesive and migratory effects of phosphophoryn are modulated by flanking peptides of the integrin binding motif.PloS one · 2014Article
- Article
- Continuing progress toward controlled intracellular delivery of semiconductor quantum dots.Wiley interdisciplinary reviews. Nanomedicine and nanobiotechnologyReview
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Authors and funding
4 authors at 1 institution in 1 country.
Funding
Abstract
Dentin phosphophoryn is nature's most acidic protein found predominantly in the dentin extracellular matrix. Its unique amino acid composition containing Asp-Ser (DS)-rich repeats makes it highly anionic. It has a low isoelectric point (pI 1.1) and, therefore, tends to be negatively charged at physiological pH. Phosphophoryn is normally associated with matrix mineralization as it can bind avidly to Ca(2+). It is well known that several macromolecules present in the extracellular matrix can be internalized and localized to specific intracellular compartments. In this study we demonstrate that dentin phosphophoryn (DPP) is internalized by several cell types via a non-conventional endocytic process. Utilizing a DSS polypeptide derived from DPP, we demonstrate the repetitive DSS-rich domain facilitates that endocytosis. As a proof-of-concept, we further demonstrate the use of this polypeptide as a protein delivery vehicle by delivering the osteoblast transcription factor Runx2 to the nucleus of mesenchymal cells. The functionality of the endocytosed Runx2 protein was demonstrated by performing gene expression analysis of Runx2 target genes. Nuclear localization was also demonstrated with the fusion protein DSS-Runx2 conjugated to quantum dots in two- and three-dimensional culture models in vitro and in vivo. Overall, we demonstrate that the DSS domain of DPP functions as a novel cell-penetrating peptide, and these findings demonstrate new opportunities for intracellular delivery of therapeutic proteins and cell tracking in vivo.
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Registered trials
Read under generation 80e0d062 · epoch 390. Bibliography from PubMed, PubMed Central and OpenAlex; grants from NIH RePORTER; trial links from ClinicalTrials.gov; estimates, votes and beliefs from the OpenQuestion graph.