Distribution and processing of a disintegrin and metalloproteinase with thrombospondin motifs-4, aggrecan, versican, and hyaluronan in equine digital laminae.

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  • Additional Information
    • Source:
      Publisher: American Veterinary Medical Association Country of Publication: United States NLM ID: 0375011 Publication Model: Print Cited Medium: Internet ISSN: 1943-5681 (Electronic) Linking ISSN: 00029645 NLM ISO Abbreviation: Am J Vet Res Subsets: MEDLINE
    • Publication Information:
      Publication: Schaumburg, Ill. : American Veterinary Medical Association
      Original Publication: Chicago : American Veterinary Medical Assn.
    • Subject Terms:
      ADAM Proteins/*metabolism ; Aggrecans/*metabolism ; Hoof and Claw/*metabolism ; Horses/*metabolism ; Hyaluronic Acid/*metabolism ; Procollagen N-Endopeptidase/*metabolism ; Versicans/*metabolism; ADAM Proteins/genetics ; ADAMTS4 Protein ; Aggrecans/genetics ; Animals ; Blotting, Western/veterinary ; Gene Expression Profiling/veterinary ; Hyaluronic Acid/genetics ; Immunohistochemistry/veterinary ; Procollagen N-Endopeptidase/genetics ; RNA/chemistry ; RNA/genetics ; Reverse Transcriptase Polymerase Chain Reaction/veterinary ; Versicans/genetics
    • Abstract:
      Objective: To determine the expression and distribution of a disintegrin and metalloproteinase with thrombospondin motifs-4 (ADAMTS-4), its substrates aggrecan and versican, and their binding partner hyaluronan in laminae of healthy horses.
      Sample: Laminae from the forelimb hooves of 8 healthy horses.
      Procedures: Real-time quantitative PCR assay was used for gene expression analysis. Hyaluronidase, chondroitinase, and keratanase digestion of lamina extracts combined with SDS-PAGE and western blotting were used for protein and proteoglycan analysis. Immunofluorescent and immunohistochemical staining of tissue sections were used for protein and hyaluronan localization.
      Results: Genes encoding ADAMTS-4, aggrecan, versican, and hyaluronan synthase II were expressed in laminae. The ADAMTS-4 was predominantly evident as a 51-kDa protein bearing a catalytic site neoepitope indicative of active enzyme and in situ activity, which was confirmed by the presence of aggrecan and versican fragments bearing ADAMTS-4 cleavage neoepitopes in laminar protein extracts. Aggrecan, versican, and hyaluronan were localized to basal epithelial cells within the secondary epidermal laminae. The ADAMTS-4 localized to these cells but was also present in some cells in the dermal laminae.
      Conclusions and Clinical Relevance: Within digital laminae, versican exclusively and aggrecan primarily localized within basal epithelial cells and both were constitutively cleaved by ADAMTS-4, which therefore contributed to their turnover. On the basis of known properties of these proteoglycans, it is possible that they can protect the basal epithelial cells of horses from biomechanical and concussive stress.
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    • Grant Information:
      R01 DE016289 United States DE NIDCR NIH HHS; DE016289 United States DE NIDCR NIH HHS
    • Accession Number:
      0 (Aggrecans)
      126968-45-4 (Versicans)
      63231-63-0 (RNA)
      9004-61-9 (Hyaluronic Acid)
      EC 3.4.24.- (ADAM Proteins)
      EC 3.4.24.14 (Procollagen N-Endopeptidase)
      EC 3.4.24.82 (ADAMTS4 Protein)
    • Publication Date:
      Date Created: 20120629 Date Completed: 20121121 Latest Revision: 20211021
    • Publication Date:
      20250114
    • Accession Number:
      PMC3535468
    • Accession Number:
      10.2460/ajvr.73.7.1035
    • Accession Number:
      22738056