title: Transport properties of the human cartilage endplate in relation to its composition and calcification.
abstract: METHODS
  The transport properties of solutes of different sizes and conformations were studied in cartilage endplates.
  
  
  OBJECTIVE
  The results were correlated with the composition of the cartilage matrix to determine if a relationship existed between this and the movement of molecules within it.
  
  
  BACKGROUND
  Solute transport through the hyaline cartilage endplate is important not only for the physiologic and metabolic processes of that tissue, but also for those of the adjacent intervertebral disc. Movement of solutes depends on solute size, shape or charges, and the composition of the matrix itself. Changes in composition of the cartilage endplate, such as those that occur in degeneration or scoliosis, may affect transport.
  
  
  METHODS
  Partition and diffusion coefficients of solutes ranging in molecular weight from 115 to 70,000 d have been measured on cores of cartilage endplate. Transport properties were assessed in relation to core composition.
  
  
  RESULTS
  The shape and size of the solutes were found to affect their transport through cartilage matrix, with larger molecules being more highly excluded and diffusing more slowly. Long-chain polymers were able to penetrate the matrix less readily than the more globular molecules. The more hydrated the matrix, the higher the degree of penetration and the more easily solutes could move, in contrast to the inverse relationship between the other components of the matrix and solute transport. With increased proteoglycan, collagen, or calcification in the tissue, there was greater restriction of solute movement.
  
  
  CONCLUSIONS
  The proteoglycans normally found in the endplate regulate movement of solutes into and out of the disc. It has been shown previously that removal of proteoglycans from the endplate accelerates the loss of proteoglycans from the nucleus. Hence, a major function of the cartilage endplate may be to prevent fragments of osmotically active proteoglycans from leaving the disc.
authors.affiliation: Centre for Spinal Studies, Robert Jones and Agnes Hunt Orthopaedic and District Hospital NHS Trust, Oswestry, U.K.
authors.forename: S
authors.initials: S
authors.lastname: Roberts
authors.forename: J P
authors.initials: JP
authors.lastname: Urban
authors.forename: H
authors.initials: H
authors.lastname: Evans
authors.forename: S M
authors.initials: SM
authors.lastname: Eisenstein
mesh_terms: D000293:Adolescent; D000328:Adult; D000368:Aged; D002113:Calcification, Physiologic / Q000502:physiology*; D002356:Cartilage / Q000000981:diagnostic imaging / Q000378:metabolism*; D002648:Child; D002675:Child, Preschool; D003094:Collagen / Q000378:metabolism; D006801:Humans; D007403:Intervertebral Disc / Q000000981:diagnostic imaging / Q000378:metabolism*; D017136:Ion Transport / Q000502:physiology*; D008875:Middle Aged; D011509:Proteoglycans / Q000378:metabolism; D011859:Radiography
chemical_list: D011509:Proteoglycans; D003094:Collagen