Primary structure, developmental expression, and immunolocalization of the murine laminin alpha 4 chain

被引:68
作者
Iivanainen, A
Kortesmaa, J
Sahlberg, C
Morita, T
Bergmann, U
Thesleff, I
Tryggvason, K
机构
[1] KAROLINSKA INST, DEPT MED BIOCHEM & BIOPHYS, DIV MATRIX BIOL, S-17177 STOCKHOLM, SWEDEN
[2] UNIV OULU, BIOCTR, SF-90570 OULU, FINLAND
[3] UNIV OULU, DEPT BIOCHEM, SF-90570 OULU, FINLAND
[4] UNIV HELSINKI, FAC VET MED, DEPT ANAT & EMBRYOL, FIN-00014 HELSINKI, FINLAND
[5] UNIV HELSINKI, INST BIOTECHNOL, FIN-00014 HELSINKI, FINLAND
关键词
D O I
10.1074/jbc.272.44.27862
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
The complete primary structure of the mouse laminin alpha 4 chain was derived from cDNA clones. The translation product contains a 24-residue signal peptide preceding the mature alpha 4 chain of 1,792 residues. Northern analysis on whole mouse embryos revealed that the expression was weak at day 7, but it later increased and peaked at day 15. In adult tissues the strongest expression was observed in lung and cardiac and skeletal muscles. Weak expression was also seen in other adult tissues such as brain, spleen, liver, kidney, and testis. By in situ hybridization of fetal and newborn tissues, expression of the laminin alpha 4 chain was mainly localized to mesenchymal cells. Strong expression was seen in the villi and submucosa of the developing intestine, the mesenchymal stroma surrounding the branching lung epithelia, and the external root sheath of vibrissae follicles, as well as in cardiac and skeletal muscle fibers. In the developing kidney, intense but transient expression was associated with the differentiation of epithelial kidney tubules from the nephrogenic mesenchyme. Immunohistologic staining with affinity-purified IgG localized the laminin alpha 4 chain primarily to lung septa, heart, and skeletal muscle, capillaries, and perineurium.
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收藏
页码:27862 / 27868
页数:7
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