title: Regional alterations of type I collagen in rat tibia induced by skeletal unloading.
abstract: Skeletal unloading induces loss of mineral density in weight-bearing bones that leads to inferior bone mechanical strength. This appears to be caused by a failure of bone formation; however, its mechanisms still are not well understood. The objective of this study was to characterize collagen, the predominant matrix protein in bone, in various regions of tibia of rats that were subjected to skeletal unloading by 4 weeks tail suspension. Sixteen male Sprague-Dawley rats (4 months old) were divided into tail suspension and ambulatory controls (eight rats each). After the tail suspension, tibias from each animal were collected and divided into five regions and collagen was analyzed. The collagen cross-linking and the extent of lysine (Lys) hydroxylation in unloaded bones were significantly altered in proximal epiphysis, diaphysis, and, in particular, proximal metaphysis but not in distal regions. The pool of immature/nonmineralized collagen measured by its extractability with a chaotropic solvent was significantly increased in proximal metaphysis. These results suggest that skeletal unloading induced an accumulation of post-translationally altered nonmineralized collagen and that these changes are bone region specific. These alterations might be caused by impaired osteoblastic function/differentiation resulting in a mineralization defect.
authors.affiliation: Dental Research Center, University of North Carolina at Chapel Hill, 27599, USA.
authors.forename: Masashi
authors.initials: M
authors.lastname: Shiiba
authors.forename: Sara B
authors.initials: SB
authors.lastname: Arnaud
authors.forename: Hideki
authors.initials: H
authors.lastname: Tanzawa
authors.forename: Eiji
authors.initials: E
authors.lastname: Kitamura
authors.forename: Mitsuo
authors.initials: M
authors.lastname: Yamauchi
mesh_terms: D000596:Amino Acids / Q000032:analysis; D000818:Animals; D001696:Biomechanical Phenomena; D015519:Bone Density; D024042:Collagen Type I / Q000737:chemistry / Q000378:metabolism*; D019417:Hindlimb Suspension / Q000009:adverse effects / Q000502:physiology*; D006900:Hydroxylation; D008239:Lysine / Q000031:analogs & derivatives / Q000032:analysis; D008297:Male; D011392:Proline / Q000031:analogs & derivatives / Q000032:analysis; D051381:Rats; D017207:Rats, Sprague-Dawley; D013977:Tibia / Q000378:metabolism* / Q000502:physiology; D018474:Weightlessness Simulation
chemical_list: D000596:Amino Acids; D024042:Collagen Type I; D011392:Proline; D008239:Lysine