ArticleThe Journal of clinical investigation1997
The syndecan family of proteoglycans. Novel receptors mediating internalization of atherogenic lipoproteins in vitro.
Article in The Journal of clinical investigation, 1997. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 65 papers.
What it found
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
The trial behind it
Trials whose registry record cites this paper, or whose number appears in the abstract. A trial that started after this paper was published is citing it as background, not reporting it.
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Who cites it
65 citing papers in PubMed, 239 citations in OpenAlex.
- Trial
- The Substructure of the Endothelial Glycocalyx in Rat Aorta and Its Interaction with the Low-Density Lipoproteins.The American journal of pathology · 2025Article
- Genetic modifiers of body mass index in individuals with cystic fibrosis.American journal of human genetics · 2024Article
- Global impact of proteoglycan science on human diseases.iScience · 2023Review
- The association between a genetic variant in theCardiovascular endocrinology & metabolism · 2023Article
- Receptor control by membrane-tethered ubiquitin ligases in development and tissue homeostasis.Current topics in developmental biology · 2022Article
- Factors Enhancing Serum Syndecan-1 Concentrations: A Large-Scale Comprehensive Medical Examination.Journal of clinical medicine · 2019Article
- Triglyceride-rich lipoprotein binding and uptake by heparan sulfate proteoglycan receptors in a CRISPR/Cas9 library of Hep3B mutants.Glycobiology · 2019Article
- Article
- The heparan sulfate proteoglycan grip on hyperlipidemia and atherosclerosis.Matrix biology : journal of the International Society for Matrix Biology · 2018Review
- Dually modified transmembrane proteoglycans in development and disease.Cytokine & growth factor reviews · 2018Review
- Suppression of Hepatic FLOT1 (Flotillin-1) by Type 2 Diabetes Mellitus Impairs the Disposal of Remnant Lipoproteins via Syndecan-1.Arteriosclerosis, thrombosis, and vascular biology · 2018Article
- Heparan sulfate proteoglycans present PCSK9 to the LDL receptor.Nature communications · 2017Article
- Decoding the Matrix: Instructive Roles of Proteoglycan Receptors.Biochemistry · 2015Review
- Syndecan-1 and Its Expanding List of Contacts.Advances in wound care · 2015Review
- Proteoglycan form and function: A comprehensive nomenclature of proteoglycans.Matrix biology : journal of the International Society for Matrix Biology · 2015Review
- Acidification of the intimal fluid: the perfect storm for atherogenesis.Journal of lipid research · 2015Review
- Processing of heparanase is mediated by syndecan-1 cytoplasmic domain and involves syntenin and α-actinin.Cellular and molecular life sciences : CMLS · 2014Article
- SULF2 strongly prediposes to fasting and postprandial triglycerides in patients with obesity and type 2 diabetes mellitus.Obesity (Silver Spring, Md.) · 2014Article
- Reply to "heparan sulfate in baculovirus binding and entry of Mammalian cells".Journal of virology · 2014Article
5 more citing papers are in PubMed but not listed here.
Corrections and comments
PubMed lists nothing against this paper. Absence here is not a guarantee, only a check that was made.
Authors and funding
9 authors at 4 institutions in 1 country.
Funding
Abstract
Cell-surface heparan sulfate proteoglycans have been shown to participate in lipoprotein catabolism, but the roles of specific proteoglycan classes have not been examined previously. Here, we studied the involvement of the syndecan proteoglycan family. First, transfection of CHO cells with expression vectors for several syndecan core proteins produced parallel increases in the cell association and degradation of lipoproteins enriched in lipoprotein lipase, a heparan-binding protein. Second, a chimeric construct, FcR-Synd1, that consists of the ectodomain of the IgG Fc receptor Ia linked to the highly conserved transmembrane and cytoplasmic domains of syndecan-1 directly mediated efficient internalization, in a process triggered by ligand clustering. Third, internalization of lipase-enriched lipoproteins via syndecan-1 and of clustered IgGs via the chimera showed identical kinetics (t1/2 = 1 h) and identical dose-response sensitivities to cytochalasin B, which disrupts microfilaments, and to genistein, which inhibits tyrosine kinases. In contrast, internalization of the receptor-associated protein, which proceeds via coated pits, showed a t1/2 < 15 min, limited sensitivity to cytochalasin B, and complete insensitivity to genistein. Thus, syndecan proteoglycans can directly mediate ligand catabolism through a pathway with characteristics distinct from coated pits, and might act as receptors for atherogenic lipoproteins and other ligands 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.