A comparative study of sialic acid-rich proteins in rat bone and dentin.

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  • Additional Information
    • Source:
      Publisher: Wiley-Blackwell Country of Publication: England NLM ID: 9504563 Publication Model: Print Cited Medium: Print ISSN: 0909-8836 (Print) Linking ISSN: 09098836 NLM ISO Abbreviation: Eur J Oral Sci Subsets: MEDLINE
    • Publication Information:
      Publication: Chichester : Wiley-Blackwell
      Original Publication: Copenhagen : Munksgaard, c1995-
    • Subject Terms:
      Bone and Bones/*chemistry ; Dentin/*chemistry ; Extracellular Matrix Proteins/*chemistry ; Sialoglycoproteins/*chemistry; Animals ; Blotting, Western ; Chromatography, DEAE-Cellulose ; Electrophoresis, Polyacrylamide Gel ; Extracellular Matrix Proteins/isolation & purification ; Glycoproteins/chemistry ; Glycoproteins/isolation & purification ; Integrin-Binding Sialoprotein ; Molecular Weight ; Osteopontin ; Phosphoproteins/chemistry ; Phosphoproteins/isolation & purification ; Protein Processing, Post-Translational ; Rats ; Sequence Analysis, Protein ; Sialoglycoproteins/isolation & purification
    • Abstract:
      Four sialic acid-rich (SA-rich) proteins found in bone and dentin, osteopontin (OPN), bone sialoprotein (BSP), bone acidic glycoprotein-75 (BAG-75), and dentin matrix protein 1 (DMP1), share some common features. We used SDS-PAGE and Western immunoblots to analyze and compare SA-rich proteins in bone and dentin extracts from rats with a single chromatographic procedure. OPN was detected in dentin extracts, with a relative level less than one-seventieth of that in bone. Both bone and dentin BSP demonstrated an extremely broad distribution pattern, probably due to a high degree of heterogeneity in post-translational modifications. BAG-75 in both bone and dentin was detected as an 83 kDa band, dramatically distinct from that of DMPI. Using a polyclonal antibody raised against a purified bone 57 kDa protein (a portion of DMPI), we detected 150 kDa protein bands in bone fraction; the same bands were recognized by antirecombinant rat DMPI antibody. Bands from dentin migrating at about 150 kDa in earlier fractions and progressing to 200 kDa in later fractions showed a clear immunoreactivity to the anti-57 kDa antibody. We conclude that the majority of DMPI in rat bone is processed into fragments, whereas that in dentin remains intact.
    • Grant Information:
      DE 05092 United States DE NIDCR NIH HHS
    • Accession Number:
      0 (DMP1 protein, human)
      0 (Dmp1 protein, rat)
      0 (Extracellular Matrix Proteins)
      0 (Glycoproteins)
      0 (IBSP protein, human)
      0 (Ibsp protein, rat)
      0 (Integrin-Binding Sialoprotein)
      0 (Phosphoproteins)
      0 (SPP1 protein, human)
      0 (Sialoglycoproteins)
      0 (Spp1 protein, rat)
      0 (bone acidic glycoprotein-75, rat)
      106441-73-0 (Osteopontin)
    • Publication Date:
      Date Created: 20010512 Date Completed: 20010920 Latest Revision: 20191104
    • Publication Date:
      20240829
    • Accession Number:
      10.1034/j.1600-0722.2001.00001.x
    • Accession Number:
      11347657