Regulation of osteopontin expression by type I collagen in preosteoblastic UMR201 cells

被引:9
作者
Traianedes, K
Martin, TJ
Findlay, DM
机构
[1] ST VINCENTS INST MED RES, FITZROY, VIC 3065, AUSTRALIA
[2] UNIV MELBOURNE, ST VINCENTS HOSP, DEPT MED, FITZROY, VIC 3065, AUSTRALIA
基金
英国医学研究理事会;
关键词
collagen; osteoblasts; osteopontin; alkaline phosphatase; gene expression;
D O I
10.3109/03008209609028894
中图分类号
Q2 [细胞生物学];
学科分类号
071009 ; 090102 ;
摘要
When UMR201 cells, phenotypically preosteoblastic, were plated onto a type I collagen gel, expression of osteopontin (OP) mRNA and protein were strongly upregulated, compared to cells plated onto plastic. This upregulation was dose-dependent, with respect to the concentration of collagen gel, and was observable within hours of cells having attached and spread on the substrate. Retinoic acid (RA) acted synergistically with type I collagen at each concentration to induce a much greater increase in or mRNA than in cells on plastic. In addition, RA increased the phosphorylation of secreted OP. The exogenous collagen substrate inhibited the growth of UMR201 cells, with the extent and duration of inhibition dependent on the collagen concentration. The effect of type I collagen was specific; plating cells on fibronectin, laminin or vitronectin did not upregulate OP expression. In contrast to the effects on OP expression, the strong RA induction of alkaline phosphatase (ALP) mRNA in cells on plastic was attenuated in cells plated on type I collagen. Growth on type I collagen did not change or mRNA stability or transcription rate, although there was decreased stability of the ALP mRNA in cells on collagen.
引用
收藏
页码:63 / 74
页数:12
相关论文
共 50 条
[21]   MULTIPLE FORMS OF SPPI (SECRETED PHOSPHOPROTEIN, OSTEOPONTIN) SYNTHESIZED BY NORMAL AND TRANSFORMED RAT BONE CELL-POPULATIONS - REGULATION BY TGF-BETA [J].
KUBOTA, T ;
ZHANG, Q ;
WRANA, JL ;
BER, R ;
AUBIN, JE ;
BUTLER, WT ;
SODEK, J .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1989, 162 (03) :1453-1459
[22]   CLEAVAGE OF STRUCTURAL PROTEINS DURING ASSEMBLY OF HEAD OF BACTERIOPHAGE-T4 [J].
LAEMMLI, UK .
NATURE, 1970, 227 (5259) :680-+
[23]  
MAJESKA RJ, 1993, J BONE MINER RES, V8, P277
[24]  
MANJI SS, 1995, IN PRESS J BIOL CHEM
[25]   IMMUNOHISTOCHEMICAL DEMONSTRATION OF A 44-KD PHOSPHOPROTEIN IN DEVELOPING RAT BONES [J].
MARK, MP ;
PRINCE, CW ;
OOSAWA, T ;
GAY, S ;
BRONCKERS, ALJJ ;
BUTLER, WT .
JOURNAL OF HISTOCHEMISTRY & CYTOCHEMISTRY, 1987, 35 (07) :707-715
[26]   44-KDAL BONE PHOSPHOPROTEIN (OSTEOPONTIN) ANTIGENICITY AT ECTOPIC SITES IN NEWBORN RATS - KIDNEY AND NERVOUS TISSUES [J].
MARK, MP ;
PRINCE, CW ;
GAY, S ;
AUSTIN, RL ;
BUTLER, WT .
CELL AND TISSUE RESEARCH, 1988, 251 (01) :23-30
[27]   MATRIX MINERALIZATION AND THE DIFFERENTIATION OF OSTEOCYTE-LIKE CELLS IN CULTURE [J].
MIKUNITAKAGAKI, Y ;
KAKAI, Y ;
SATOYOSHI, M ;
KAWANO, E ;
SUZUKI, Y ;
KAWASE, T ;
SAITO, S .
JOURNAL OF BONE AND MINERAL RESEARCH, 1995, 10 (02) :231-242
[28]   POSTTRANSLATIONAL PROCESSING OF CHICKEN BONE PHOSPHOPROTEINS - IDENTIFICATION OF BONE (PHOSPHO)PROTEIN KINASE [J].
MIKUNITAKAGAKI, Y ;
GLIMCHER, MJ .
BIOCHEMICAL JOURNAL, 1990, 268 (03) :593-597
[29]  
MIYAUCHI A, 1991, J BIOL CHEM, V266, P20369
[30]  
NEMIR M, 1989, J BIOL CHEM, V264, P18202