Change in the Mode of Gene Expression of the Hypopharyngeal Gland Cells with an Age-dependent Role Change of the Worker Honeybee Apis mellifera L.


  • Note. The novel nucleotide sequence data published here have been deposited in the DDBJ, EMBL and GenBank sequence data bank and are available under the accession number D79207.

T. Kubo, Faculty of Pharmaceutical Sciences, University of Tokyo, Bunkyo-ku, Tokyo, Japan 113
Fax:+81 3 5684 2973.


Major proteins synthesized in the hypopharyngeal gland of the worker honeybee change from bee-milk proteins to α-glucosidase in accordance with the age-dependent role change of the worker bee. Previously, we showed that the gene for α-glucosidase is expressed specifically in the forager-bee gland [Ohashi, K., Sawata, M., Takeuchi, H., Natori, S. & Kubo, T. (1996) Biochem. Biophys. Res. Commun. 221, 380–385]. Here, we describe the isolation and analysis of cDNAs for two bee-milk 56-kDa and 64-kDa proteins. The 56-kDa protein was a glycoprotein which shared 63.2% and 56.9% amino acid sequence identities with proteins encoded by cDNA for royal-jelly-related protein 57–1 (pRJP57-l) and pRJP57–2. The 64-kDa protein cDNA was identical to pRJP57-l. Thus, these bee-milk proteins seem to form a structurally related protein family. The gene for the 64-kDa protein/RJP57-1 was expressed specifically in the nurse-bee gland, whereas that for the 56-kDa protein was expressed in both the nurse-bee and forager-bee glands. mRNAs for the 56-kDa and 64-kDa proteins were detected by in situ hybridization in a whole acinus of the nurse-bee gland, whereas mRNAs for the 56-kDa protein and α-glucosidase were detected in that of the forager-bee gland. Therefore, the individual secretory cells of the acinus of the hypopharyngeal gland were shown to express these genes differently with the age-dependent role change of the worker bee.


α-Glucosidase (EC


exonuclease 111 (EC 3.1 .11.2)


mung bean nuclease (EC


alkaline phosphatase (EC