title: 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.
abstract: Major proteins synthesized in the hypopharyngeal gland of the worker honeybee change from bee-milk proteins to alpha-glucosidase in accordance with the age-dependent role change of the worker bee. Previously, we showed that the gene for alpha-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 (pRJP57-1) and pRJP57-2. The 64-kDa protein cDNA was identical to pRJP57-1. 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 alpha-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.
authors.affiliation: Faculty of Pharmaceutical Sciences, University of Tokyo, Japan.
authors.forename: K
authors.initials: K
authors.lastname: Ohashi
authors.forename: S
authors.initials: S
authors.lastname: Natori
authors.forename: T
authors.initials: T
authors.lastname: Kubo
mesh_terms: D000375:Aging; D000581:Amidohydrolases / Q000378:metabolism; D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D001516:Bees / Q000235:genetics* / Q000378:metabolism; D015152:Blotting, Northern; D003001:Cloning, Molecular; D004591:Electrophoresis, Polyacrylamide Gel; D005088:Exocrine Glands / Q000378:metabolism; D005227:Fatty Acids / Q000737:chemistry; D005786:Gene Expression Regulation; D006023:Glycoproteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics* / Q000302:isolation & purification; D006031:Glycosylation; D007013:Hypopharynx / Q000166:cytology / Q000201:enzymology / Q000378:metabolism; D017403:In Situ Hybridization; D019476:Insect Proteins / Q000096:biosynthesis / Q000737:chemistry / Q000235:genetics*; D008969:Molecular Sequence Data; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D012313:RNA / Q000032:analysis; D016601:RNA-Binding Proteins; D017386:Sequence Homology, Amino Acid; D000520:alpha-Glucosidases / Q000096:biosynthesis / Q000235:genetics; D000099219:Royal Jelly
chemical_list: D000581:Amidohydrolases; D005227:Fatty Acids; D006023:Glycoproteins; D019476:Insect Proteins; D043524:Peptide-N4-(N-acetyl-beta-glucosaminyl) Asparagine Amidase; D012313:RNA; D016601:RNA-Binding Proteins; D000520:alpha-Glucosidases; D000099219:Royal Jelly; C109593:MRJP3 protein, Apis mellifera