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层粘连蛋白的亚基在小鼠卵子和早期胚胎中差异合成。

Subunits of laminin are differentially synthesized in mouse eggs and early embryos.

作者信息

Cooper A R, MacQueen H A

出版信息

Dev Biol. 1983 Apr;96(2):467-71. doi: 10.1016/0012-1606(83)90183-5.

DOI:10.1016/0012-1606(83)90183-5
PMID:6403399
Abstract

Synthesis of laminin by mouse preimplantation embryos was examined by specific immunoprecipitation of [35S]methionine-labeled cell lysates. The three polypeptide subunits of laminin, A, B1, and B2, are not necessarily synchronously expressed during development. Oocytes and eggs synthesize only one immunoprecipitable polypeptide, which comigrates with the intracellular B1 chains made by PYS cells and contains N-linked oligosaccharide residues which are sensitive to endo-beta-N-acetylglucosaminidase H. From the 4- to 8-cell stage, only B1 and B2 polypeptides are synthesized, whereas from the 16-cell stage onwards all three laminin polypeptides are made.

摘要

通过对[35S]甲硫氨酸标记的细胞裂解物进行特异性免疫沉淀,检测了小鼠植入前胚胎层粘连蛋白的合成。层粘连蛋白的三个多肽亚基A、B1和B2在发育过程中不一定同步表达。卵母细胞和卵子仅合成一种可免疫沉淀的多肽,其与PYS细胞产生的细胞内B1链迁移率相同,并含有对内切β-N-乙酰葡糖胺酶H敏感的N-连接寡糖残基。从4细胞期到8细胞期,仅合成B1和B2多肽,而从16细胞期开始,所有三种层粘连蛋白多肽均被合成。

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