ArticleMolecular and cellular biochemistry2012
Human parotid secretory protein is a lipopolysaccharide-binding protein: identification of an anti-inflammatory peptide domain.
Article in Molecular and cellular biochemistry, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 23 papers.
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Who cites it
23 citing papers in PubMed, 50 citations in OpenAlex.
- Relevance of autoantibodies to carbonic anhydrase 6 (CA6), parotid secretory protein (PSP) and salivary gland protein 1 (SP1) to dry eye disease (DED).BMJ open ophthalmology · 2026Article
- Targeted Modification of the Antimicrobial Peptide DGL13K Reveals a Naturally Optimized Sequence for Topical Applications.Microorganisms · 2025Article
- Revealing pH-dependent antimicrobial peptide, GL13K, characteristics: A constant pH molecular dynamics study.bioRxiv : the preprint server for biology · 2025Article
- A proteomics perspective on 2 years of high-intensity training in horses: a pilot study.Scientific reports · 2024Article
- The oral pathogen Porphyromonas gingivalis gains tolerance to the antimicrobial peptide DGL13K by synonymous mutations in hagA.PloS one · 2024Article
- A Proteomics Investigation of Salivary Profiles as Potential Biomarkers for Autism Spectrum Disorder (ASD).The protein journal · 2023Article
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- The parotid secretory protein BPIFA2 is a salivary surfactant that affects lipopolysaccharide action.Experimental physiology · 2020Article
- Human and Nonhuman Primate Lineage-Specific Footprints in the Salivary Proteome.Molecular biology and evolution · 2020Article
- In vivo activity and low toxicity of the second-generation antimicrobial peptide DGL13K.PloS one · 2019Article
- Glycan recognition at the saliva - oral microbiome interface.Cellular immunology · 2018Review
- BPI fold-containing family a member 2 as a biomarker of acute kidney injury-close but no (clinical) cigar?Annals of translational medicine · 2018Article
- Presence of BPIFB1 in saliva from non-obese diabetic mice.Odontology · 2018Article
- Associations of Salivary BPIFA1 Protein in Chronic Periodontitis Patients with Type 2 Diabetes Mellitus.International journal of endocrinology · 2017Article
- A Novel RNase 3/ECP Peptide for Pseudomonas aeruginosa Biofilm Eradication That Combines Antimicrobial, Lipopolysaccharide Binding, and Cell-Agglutinating Activities.Antimicrobial agents and chemotherapy · 2016Article
- Lipopolysaccharide-binding protein is efficient in biodosimetry during radiotherapy of lung cancer.Biomedical reports · 2016Article
- A systems biology approach identifies a regulatory network in parotid acinar cell terminal differentiation.PloS one · 2015Article
- Allergen ligands in the initiation of allergic sensitization.Current allergy and asthma reports · 2014Article
- Antimicrobial peptide GL13K is effective in reducing biofilms of Pseudomonas aeruginosa.Antimicrobial agents and chemotherapy · 2013Article
Corrections and comments
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Authors and funding
5 authors at 3 institutions in 2 countries.
Funding
Abstract
Parotid secretory protein (PSP) (C20orf70) is a salivary protein of unknown function. The protein belongs to the palate, lung, and nasal epithelium clone (PLUNC) family of mucosal secretory proteins that are predicted to be structurally similar to lipid-binding and host-defense proteins including bactericidal/permeability-increasing protein and lipopolysaccharide-binding protein. However, the PLUNC proteins exhibit significant sequence variation and different biological functions have been proposed for different family members. This study tested the functional implications of the proposed similarity of PSP to the acute phase protein lipopolysaccharide-binding protein (LBP). PSP was identified in human saliva and was soluble in 70% ethanol, as shown for other PLUNC proteins. PSP binds lipopolysaccharide and can be eluted by non-ionic detergent, but not by urea or high salt. A synthetic PSP peptide, GL13NH2, which corresponds to a lipopolysaccharide-inhibiting peptide from LBP, inhibited the binding of lipopolysaccharide to both PSP and lipopolysaccharide-binding protein. Peptides from other regions of PSP and the control peptide polymyxin B showed no effect on the binding of PSP to lipopolysaccharide. GL13NH2 also inhibited lipopolysaccharide-stimulated secretion of tumor necrosis factor from macrophages. The other PSP peptides had no effect in this assay. PSP peptides had no or only minor effect on macrophage cell viability. These results indicate that PSP is a lipopolysaccharide-binding protein that is functionally related to LBP, as suggested by their predicted structural similarities.
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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.