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在F-9畸胎瘤干细胞分化过程中,纤连蛋白积累的改变并不依赖于纤连蛋白的修饰。

Altered accumulations of fibronectin are not dependent on fibronectin modifications during the differentiation of F-9 teratocarcinoma stem cells.

作者信息

Dahl S C, Grabel L B

机构信息

Department of Biology, Wesleyan University, Middletown, Connecticut 06457.

出版信息

Exp Cell Res. 1988 Jun;176(2):234-47. doi: 10.1016/0014-4827(88)90327-8.

DOI:10.1016/0014-4827(88)90327-8
PMID:3288485
Abstract

F-9 teratocarcinoma stem cells differentiate into parietal endoderm when monolayer cultures are treated with retinoic acid. This change in phenotype is accompanied by increased accumulation and altered organization of fibronectin deposits. Although both stem cells and treated cells synthesize and accumulate fibronectin, only the treated cells deposit a fibrillar array of the protein. We have monitored the accumulation of fibronectin in nontreated and treated F-9 cells with indirect immunofluorescence and have biochemically analyzed the fibronectin synthesized by each cell type with one- and two-dimensional acrylamide gels and peptide maps. Our data suggest that no differences exist between these fibronectins to account for the observed changes in accumulation. Thus, another mechanism may regulate the organization of matrix deposition.

摘要

当单层培养的F-9畸胎癌细胞用视黄酸处理时,它们会分化为滋养层内胚层。这种表型变化伴随着纤连蛋白沉积物积累的增加和组织方式的改变。虽然干细胞和处理后的细胞都能合成并积累纤连蛋白,但只有处理后的细胞会沉积出该蛋白的纤维状阵列。我们用间接免疫荧光监测了未处理和处理后的F-9细胞中纤连蛋白的积累情况,并用一维及二维丙烯酰胺凝胶和肽图对每种细胞类型合成的纤连蛋白进行了生化分析。我们的数据表明,这些纤连蛋白之间不存在差异来解释观察到的积累变化。因此,可能有另一种机制调节基质沉积的组织方式。

相似文献

1
Altered accumulations of fibronectin are not dependent on fibronectin modifications during the differentiation of F-9 teratocarcinoma stem cells.在F-9畸胎瘤干细胞分化过程中,纤连蛋白积累的改变并不依赖于纤连蛋白的修饰。
Exp Cell Res. 1988 Jun;176(2):234-47. doi: 10.1016/0014-4827(88)90327-8.
2
Expression of laminin and fibronectin in endodermal and neural differentiation of F9 embryonal carcinoma cells.
Prog Clin Biol Res. 1984;151:233-47.
3
Integrin phosphorylation is modulated during the differentiation of F-9 teratocarcinoma stem cells.整合素磷酸化在F-9畸胎瘤干细胞分化过程中受到调节。
J Cell Biol. 1989 Jan;108(1):183-90. doi: 10.1083/jcb.108.1.183.
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The outgrowth of parietal endoderm from mouse teratocarcinoma stem-cell embryoid bodies.
Differentiation. 1986;32(1):67-73. doi: 10.1111/j.1432-0436.1986.tb00557.x.
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The role of extracellular matrix in the migration and differentiation of parietal endoderm from teratocarcinoma embryoid bodies.细胞外基质在畸胎瘤胚状体中壁内胚层迁移和分化中的作用。
J Cell Biol. 1987 Jul;105(1):441-8. doi: 10.1083/jcb.105.1.441.
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Stimulation of retinoic acid of synthesis and turnover of basement membrane in mouse embryonal carcinoma-derived endoderm cells.视黄酸对小鼠胚胎癌衍生内胚层细胞基底膜合成与周转的刺激作用。
Coll Relat Res. 1982 Mar;2(2):93-110. doi: 10.1016/s0174-173x(82)80026-5.
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An adhesion-defective variant of F9 embryonal carcinoma cells fails to differentiate into visceral endoderm.F9胚胎癌细胞的一种粘连缺陷变体无法分化为脏内胚层。
Dev Biol. 1987 Mar;120(1):1-11. doi: 10.1016/0012-1606(87)90098-4.
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Roles of extracellular matrix components in differentiating teratocarcinoma cells.细胞外基质成分在畸胎癌细胞分化中的作用。
J Biol Chem. 1985 Oct 5;260(22):12252-8.
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Effects of extracellular matrices on F9 teratocarcinoma stem cells: a crucial role of type IV collagen in the early stage of differentiation of F9 stem cells.细胞外基质对F9畸胎瘤干细胞的影响:IV型胶原在F9干细胞分化早期的关键作用。
Pathobiology. 2002;70(4):219-28. doi: 10.1159/000069333.
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Embryonal carcinoma cells adhere preferentially to fibronectin and laminin but their endodermal differentiation leads to a reduced adherence to laminin.胚胎癌细胞优先黏附于纤连蛋白和层粘连蛋白,但其内胚层分化导致对层粘连蛋白的黏附减少。
Exp Cell Res. 1989 May;182(1):26-32. doi: 10.1016/0014-4827(89)90276-0.

引用本文的文献

1
Integrin phosphorylation is modulated during the differentiation of F-9 teratocarcinoma stem cells.整合素磷酸化在F-9畸胎瘤干细胞分化过程中受到调节。
J Cell Biol. 1989 Jan;108(1):183-90. doi: 10.1083/jcb.108.1.183.
2
Colonial morphology of tumour cells and susceptibility to cytolysis by tumour necrosis factor. The role of cellular fibronectin deposition in the extracellular matrix.肿瘤细胞的菌落形态及对肿瘤坏死因子细胞溶解的敏感性。细胞纤连蛋白在细胞外基质中沉积的作用。
Br J Cancer. 1990 Jun;61(6):831-5. doi: 10.1038/bjc.1990.186.