The small ampullate glands of the orb-web spider, Nephila clavipes, have be
en studied and compared to other of the silk producing glands from this org
anism. They exhibit the same gross morphological features of the other glan
ds. 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. Previou
s studies from our laboratory identified these peptides as products generat
ed by translational pauses. This alternate mode of translation is typical o
f 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 f
ibroin synthesis is shown through experimental evidence in this paper. The
gradual ultrastructural changes in Golgi vesicles elicited by the fibroin s
ynthesis 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 anal
yzed. These studies show the small ampullate glands are a promising and cer
tainly exploitable model system for studies on the synthesis of tissue-spec
ific protein product and its control. (C) 2000 Wiley-Liss, Inc.