TY - JOUR
T1 - Age‐related changes in hyaluronan, proteoglycan, collagen, and osteonectin synthesis by human bone cells
AU - Fedarko, N. S.
AU - Vetter, U. K.
AU - Weinstein, S.
AU - Robey, P. Gehron
PY - 1992/5
Y1 - 1992/5
N2 - Human bone cells grown in culture, representative of a preosteoblastic stage of maturation, produce an extracellular matrix composed of collagen several noncollagenous glycoproteins, hyaluronan, and four distinct proteoglycans (PGs). The influence of donor age on the levels of expression of these molecules in vitro has not been well characterized. In this study, human bone cells derived from sources ranging from fetal to 60‐year‐old donors were grown in culture, radiolabeled for 24 h, and the amount of incorporation of [35S]sulfate into PGs, [3H]glucosamine into hyaluronan, [3H]leucine/proline into osteonectin, and [3H]proline into collagen was determined. Cell proliferation was most rapid in fetal‐derived bone cells and decreased with increasing age. Total protein and PG synthesis also decreased with increasing age, falling to 1/3 and 1/4, respectively, of fetal levels after age 30. A large chondroitin sulfate PG (Mr ∼ 600,000 Da) was the major fetal PG and its levels were highly correlated with cellular proliferation. [3H]Collagen and [35S]decorin levels increased with the increasing age of the donor, reached a maximum in puberty‐derived cells, and decreased to 1/3 maximal levels after age 20. The heparan sulfate PG (Mr ∼ 400,000 Da) exhibited steadystate levels regardless of donor age. [3H]Osteonectin and [35S]biglycan levels were high in fetal‐derived cells and in cells derived from pubescent donors. The percentage of collagen and four proteoglycans associated with the cell layer pool changed with donor age. All fetal‐derived PG core proteins possessed more N‐ and O‐linked oligosaccharides than newborn or adult derived PGs. © 1992 Wiley‐Liss, Inc.
AB - Human bone cells grown in culture, representative of a preosteoblastic stage of maturation, produce an extracellular matrix composed of collagen several noncollagenous glycoproteins, hyaluronan, and four distinct proteoglycans (PGs). The influence of donor age on the levels of expression of these molecules in vitro has not been well characterized. In this study, human bone cells derived from sources ranging from fetal to 60‐year‐old donors were grown in culture, radiolabeled for 24 h, and the amount of incorporation of [35S]sulfate into PGs, [3H]glucosamine into hyaluronan, [3H]leucine/proline into osteonectin, and [3H]proline into collagen was determined. Cell proliferation was most rapid in fetal‐derived bone cells and decreased with increasing age. Total protein and PG synthesis also decreased with increasing age, falling to 1/3 and 1/4, respectively, of fetal levels after age 30. A large chondroitin sulfate PG (Mr ∼ 600,000 Da) was the major fetal PG and its levels were highly correlated with cellular proliferation. [3H]Collagen and [35S]decorin levels increased with the increasing age of the donor, reached a maximum in puberty‐derived cells, and decreased to 1/3 maximal levels after age 20. The heparan sulfate PG (Mr ∼ 400,000 Da) exhibited steadystate levels regardless of donor age. [3H]Osteonectin and [35S]biglycan levels were high in fetal‐derived cells and in cells derived from pubescent donors. The percentage of collagen and four proteoglycans associated with the cell layer pool changed with donor age. All fetal‐derived PG core proteins possessed more N‐ and O‐linked oligosaccharides than newborn or adult derived PGs. © 1992 Wiley‐Liss, Inc.
UR - http://www.scopus.com/inward/record.url?scp=0026588602&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=0026588602&partnerID=8YFLogxK
U2 - 10.1002/jcp.1041510202
DO - 10.1002/jcp.1041510202
M3 - Article
C2 - 1572898
AN - SCOPUS:0026588602
SN - 0021-9541
VL - 151
SP - 215
EP - 227
JO - Journal of Cellular Physiology
JF - Journal of Cellular Physiology
IS - 2
ER -