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. 1993 Apr;205(2):251-60.
doi: 10.1006/excr.1993.1084.

Secretion of endogenous 16-kDa beta-galactoside-binding lectin from vitamin A-pretreated chick embryonic cultured skin

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Secretion of endogenous 16-kDa beta-galactoside-binding lectin from vitamin A-pretreated chick embryonic cultured skin

Y Akimoto et al. Exp Cell Res. 1993 Apr.

Abstract

Localization of endogenous beta-galactoside-binding 16-kDa lectin and its gene expression pattern were investigated during differentiation of chick embryonic skin in vivo and in vitro and were compared with those of a 14-kDa lectin. By light microscopy, immunostaining of the 16-kDa lectin was weak in the undifferentiated epidermis, while it became intense in the keratinized epidermis, particularly in the intermediate cells. Essentially the same staining pattern was observed both in vivo and in vitro. The gene expression pattern was consistent with these immunohistochemical observations. These results were similar to those of the 14-kDa lectin [1]. On the other hand, in the vitamin A-pretreated cultured skin, mucous metaplasia of the epidermis was induced and marked changes in localization of these two isolectins were observed. The 16-kDa lectin expression was increased in the epidermis, especially in the superficial cells, and the gene expression was detected in all layers of the epidermis. However, 14-kDa lectin expression was markedly reduced in the metaplastic epidermis. In the keratinized epidermis, detailed localization of these lectins under the electron microscope was almost the same. Both of them were located primarily along the plasma membrane, in the intercellular space, and in the desmosomes. In the mucous metaplastic epidermis, however, the localization of the 16-kDa lectin was completely different from that of the 14-kDa lectin; e.g., the former was detected in the mucous granules and on the microvilli of the superficial cells, while the latter was scarcely observed in the epidermis. The present results revealed that (1) the 16-kDa lectin as well as 14-kDa lectin were expressed during the epidermal differentiation and (2) much of the 16-kDa lectin was produced and secreted from the vitamin A-pretreated cultured epidermis, while 14-kDa lectin disappeared. In the view of these facts, it is suggested that (1) both 14- and 16-kDa lectins may play an important role in differentiation of the skin and (2) the gene expression of 14- and 16-kDa lectins is regulated independently.

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