title: Small ampullate glands of Nephila clavipes.
abstract: The small ampullate glands of the orb-web spider, Nephila clavipes, have been studied and compared to other of the silk producing glands from this organism. They exhibit the same gross morphological features of the other glands. Electrophoretic analyses show that the gland's luminal contents migrate as a single band, while the contents of the secretory epithelium reveal a step-ladder array of peptides in addition to the full size product. Previous studies from our laboratory identified these peptides as products generated by translational pauses. This alternate mode of translation is typical of fibroin synthesis in all the spider glands thus far studied as well as in those of the silkworm. The correlation of the peptides to the process of fibroin synthesis is shown through experimental evidence in this paper. The gradual ultrastructural changes in Golgi vesicles elicited by the fibroin synthesis stimulus can be seen in this paper. The response to stimulation is of a higher magnitude in these glands than in any of those previously analyzed. These studies show the small ampullate glands are a promising and certainly exploitable model system for studies on the synthesis of tissue-specific protein product and its control. J. Exp. Zool. 286:114-119, 2000.
authors.affiliation: Graciela C. Candelas, Department of Biology, University of Puerto Rico, San Juan, Puerto Rico 00931-3360, USA.
authors.forename: R
authors.initials: R
authors.lastname: Ortíz
authors.forename: W
authors.initials: W
authors.lastname: Céspedes
authors.forename: L
authors.initials: L
authors.lastname: Nieves
authors.forename: I V
authors.initials: IV
authors.lastname: Robles
authors.forename: A
authors.initials: A
authors.lastname: Plazaola
authors.forename: S
authors.initials: S
authors.lastname: File
authors.forename: G C
authors.initials: GC
authors.lastname: Candelas
mesh_terms: D000818:Animals; D004591:Electrophoresis, Polyacrylamide Gel / Q000662:veterinary; D005088:Exocrine Glands / Q000378:metabolism; D005349:Fibroins / Q000096:biosynthesis; D019476:Insect Proteins / Q000096:biosynthesis*; D008854:Microscopy, Electron / Q000662:veterinary; D047011:Silk; D013112:Spiders / Q000033:anatomy & histology* / Q000502:physiology
chemical_list: D019476:Insect Proteins; D047011:Silk; D005349:Fibroins