ArticleBMC biochemistry2011
Porcine dentin sialoprotein glycosylation and glycosaminoglycan attachments.
Article in BMC biochemistry, 2011. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 13 papers.
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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.
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Who cites it
13 citing papers in PubMed, 22 citations in OpenAlex.
- Functions of secretory calcium-binding phosphoproteins in dental mineralization.Journal of bone and mineral research : the official journal of the American Society for Bone and Mineral Research · 2025Review
- DSP and DPP are dispensable for initiation of dentin and enamel mineralization but critical for circumpulpal dentin mineralization.Scientific reports · 2025Article
- Inositol-requiring enzyme 1 alpha is essential for dentinogenesis.Frontiers in physiology · 2025Article
- The significant role of glycosaminoglycans in tooth development.Glycobiology · 2024Review
- Article
- Enamel Defects Associated With Dentin Sialophosphoprotein Mutation in Mice.Frontiers in physiology · 2021Article
- Novel frameshift mutations in DSPP cause dentin dysplasia type II.Oral diseases · 2019Article
- Structural features, processing mechanism and gene splice variants of dentin sialophosphoprotein.The Japanese dental science review · 2018Review
- The dentin phosphoprotein repeat region and inherited defects of dentin.Molecular genetics & genomic medicine · 2016Article
- DPP and DSP are Necessary for Maintaining TGF-β1 Activity in Dentin.Journal of dental research · 2014Article
- Article
- Enamel malformations associated with a defined dentin sialophosphoprotein mutation in two families.European journal of oral sciences · 2011Article
- Accelerated enamel mineralization in Dspp mutant mice.Matrix biology : journal of the International Society for Matrix BiologyArticle
Corrections and comments
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Authors and funding
5 authors at 2 institutions in 2 countries.
Funding
Abstract
backgroundDentin sialophosphoprotein (Dspp) is a multidomain, secreted protein that is critical for the formation of tooth dentin. Mutations in DSPP cause inherited dentin defects categorized as dentin dysplasia type II and dentinogenesis imperfecta type II and type III. Dentin sialoprotein (Dsp), the N-terminal domain of dentin sialophosphoprotein (Dspp), is a highly glycosylated proteoglycan, but little is known about the number, character, and attachment sites of its carbohydrate moieties.
resultsTo identify its carbohydrate attachment sites we isolated Dsp from developing porcine molars and digested it with endoproteinase Glu-C or pronase, fractionated the digestion products, identified fractions containing glycosylated peptides using a phenol sulfuric acid assay, and characterized the glycopeptides by N-terminal sequencing, amino acid analyses, or LC/MSMS. To determine the average number of sialic acid attachments per N-glycosylation, we digested Dsp with glycopeptidase A, labeled the released N-glycosylations with 2-aminobenzoic acid, and quantified the moles of released glycosylations by comparison to labeled standards of known concentration. Sialic acid was released by sialidase digestion and quantified by measuring β-NADH reduction of pyruvic acid, which was generated stoichiometrically from sialic acid by aldolase. To determine its forms, sialic acid released by sialidase digestion was labeled with 1,2-diamino-4,5-methyleneoxybenzene (DMB) and compared to a DMB-labeled sialic acid reference panel by RP-HPLC. To determine the composition of Dsp glycosaminoglycan (GAG) attachments, we digested Dsp with chondroitinase ABC and compared the chromotagraphic profiles of the released disaccharides to commercial standards. N-glycosylations were identified at Asn37, Asn77, Asn136, Asn155, Asn161, and Asn176. Dsp averages one sialic acid per N-glycosylation, which is always in the form of N-acetylneuraminic acid. O-glycosylations were tentatively assigned at Thr200, Thr216 and Thr316. Porcine Dsp GAG attachments were found at Ser238 and Ser250 and were comprised of chondroitin 6-sulfate and chondroitin 4-sulfate in a ratio of 7 to 3, respectively.
conclusionsThe distribution of porcine Dsp posttranslational modifications indicate that porcine Dsp has an N-terminal domain with at least six N-glycosylations and a C-terminal domain with two GAG attachments and at least two O-glycosylations.
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What OpenQuestion holds
Registered trials
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