TY - JOUR
T1 - The effect of serum growth factors and xyloside on molecular aging of proteoglycan in embryonal chick cartilage
AU - Nevo, Zvi
AU - Lis, Dora
AU - Silbergeld, Aviva
AU - Levin, Shmuel
AU - Zak, Yosef
AU - Zadik, Zvi
N1 - Funding Information:
This research program was supported by grants (Gr 224/13 and GR 224/15-2) from the Deutsche Forschungsgemeinschaft. The authors gratefully acknowledge the generous supply of IGF and IGF determinations provided by Profs. Froesch, Zapf and Humbel of the University Hospital of Zurich, Switzerland.
PY - 1984/8
Y1 - 1984/8
N2 - The effects of normal human serum, insulin-like growth factor and β-d-xyloside on the synthesis of proteoglycan, as well as their differential effect on the synthesis of chondroitin sulfate and keratan sulfate side-chains, were studied in chick embryonal cartilage. The glycosaminoglycans found in the incubation medium were mainly intact carbohydrate moieties of partially degraded proteoglycan molecules, whereas the tissue-bound glycosaminoglycans were of intact proteoglycan molecules. In incubations with normal human serum, the synthesis of the chondroitin sulfate side-chains of the tissue-bound glycosaminoglycans was preferentially stimulated, while the percentage of medium glycosaminoglycan (out of the total glycosaminoglycan in tissue and medium) was reduced, compared to control incubations. In incubations with insulin-like growth factor, the synthesis of the keratan sulfate side-chains of the tissue-bound glycosaminoglycan was preferentially stimulated, whereas the percentage of the medium glycosaminoglycan resembled that of control incubations. In incubations with xyloside, a marked reduction of tissue-bound glycosaminoglycan was noticed, mainly of chondroitin sulfate chains, and only a slight decrease in keratan sulfate chains. Human serum of various age groups stimulated proteoglycan synthesis in embryonal chick cartilage to almost the same extent. However, sera from babies and adults were found to stimulate chondroitin sulfate chains preferentially, whereas serum of aged subjects preferentially enhanced the synthesis of keratan sulfate chains. These findings suggest that the synthesis and/or degradation of the various types of glycosaminoglycan chains (chondroitin sulfate and keratan sulfate) of cartilage proteoglycan can be regulated differentially by serum growth factors. Secondly, the growth hormone-mediated serum factor (insulin-like growth factor) seems to play a role in molecular aging of proteoglycans.
AB - The effects of normal human serum, insulin-like growth factor and β-d-xyloside on the synthesis of proteoglycan, as well as their differential effect on the synthesis of chondroitin sulfate and keratan sulfate side-chains, were studied in chick embryonal cartilage. The glycosaminoglycans found in the incubation medium were mainly intact carbohydrate moieties of partially degraded proteoglycan molecules, whereas the tissue-bound glycosaminoglycans were of intact proteoglycan molecules. In incubations with normal human serum, the synthesis of the chondroitin sulfate side-chains of the tissue-bound glycosaminoglycans was preferentially stimulated, while the percentage of medium glycosaminoglycan (out of the total glycosaminoglycan in tissue and medium) was reduced, compared to control incubations. In incubations with insulin-like growth factor, the synthesis of the keratan sulfate side-chains of the tissue-bound glycosaminoglycan was preferentially stimulated, whereas the percentage of the medium glycosaminoglycan resembled that of control incubations. In incubations with xyloside, a marked reduction of tissue-bound glycosaminoglycan was noticed, mainly of chondroitin sulfate chains, and only a slight decrease in keratan sulfate chains. Human serum of various age groups stimulated proteoglycan synthesis in embryonal chick cartilage to almost the same extent. However, sera from babies and adults were found to stimulate chondroitin sulfate chains preferentially, whereas serum of aged subjects preferentially enhanced the synthesis of keratan sulfate chains. These findings suggest that the synthesis and/or degradation of the various types of glycosaminoglycan chains (chondroitin sulfate and keratan sulfate) of cartilage proteoglycan can be regulated differentially by serum growth factors. Secondly, the growth hormone-mediated serum factor (insulin-like growth factor) seems to play a role in molecular aging of proteoglycans.
KW - Embryonal chick cartilage
KW - Molecular aging of proteoglycan
KW - Serum growth factors
KW - Xyloside
UR - http://www.scopus.com/inward/record.url?scp=0021210420&partnerID=8YFLogxK
U2 - 10.1016/0047-6374(84)90089-7
DO - 10.1016/0047-6374(84)90089-7
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AN - SCOPUS:0021210420
SN - 0047-6374
VL - 26
SP - 133
EP - 147
JO - Mechanisms of Ageing and Development
JF - Mechanisms of Ageing and Development
IS - 2-3
ER -