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Cyclophilin B Deficiency Causes Abnormal Dentin Collagen Matrix.

Masahiko Terajima1, Yuki Taga2, Wayne A Cabral3

  • 1Oral and Craniofacial Health Sciences, School of Dentistry, University of North Carolina , Chapel Hill, North Carolina 27599, United States.

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Cyclophilin B (CypB) is crucial for dentin collagen formation, impacting its hydroxylation and glycosylation. Its absence in knockout mice leads to defective dentin matrix, suggesting links to osteogenesis imperfecta.

Keywords:
collagencyclophilin Bdentinglycosylationhydroxylysinepost-translational modification

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Area of Science:

  • Biochemistry
  • Molecular Biology
  • Biomineralization

Background:

  • Cyclophilin B (CypB) is an endoplasmic reticulum protein involved in collagen folding.
  • CypB regulates prolyl 3-hydroxylation (P3H) and lysine (Lys) hydroxylation of collagen.
  • Recessive osteogenesis imperfecta type IX is modeled by CypB null (KO) mice.

Purpose of the Study:

  • To characterize dentin type I collagen in CypB null (KO) mice.
  • To compare dentin collagen from KO mice with wild-type (WT) and heterozygous (Het) mice.
  • To elucidate the role of CypB in dentin matrix formation.

Main Methods:

  • Mass spectrometric analysis of dentin type I collagen.
  • Histological analysis of dentin and predentin.
  • Comparison of molecular phenotypes between KO, WT, and Het mice.

Main Results:

  • Dentin collagen in KO mice showed significantly diminished P3H compared to WT/Het.
  • Lys hydroxylation was reduced at key cross-linking sites in KO mice, altering cross-link profiles.
  • Glycosylation of hydroxylysine residues was generally higher in KO mice.
  • Histology revealed wider, irregular predentin and smaller, sparser collagen fibrils in KO mice.
  • Observed dentin phenotypes were distinct from other KO tissues, indicating CypB's dentin-specific role.

Conclusions:

  • CypB plays a critical role in dentin matrix formation.
  • Defects in CypB function impact collagen post-translational modifications in dentin.
  • This study suggests a potential association between recessive osteogenesis imperfecta and undetected dentin defects.