E. Horler et H. Briegel, PROTEOLYTIC-ENZYMES OF FEMALE ANOPHELES - BIPHASIC SYNTHESIS, REGULATION, AND MULTIPLE FEEDING, Archives of insect biochemistry and physiology, 28(2), 1995, pp. 189-205
Two types of trypsin activity were detected in Anopheles albimanus, a
constitutive and an inductive component, which have identical immunopa
tterns. The constitutive trypsin in synthesized shortly after eclosion
and is retained in the midgut epithelial cells. The inductive trypsin
is synthesized and released continuously after a blood meal has been
ingested; maximal activities vary between 12 h and 18 h after a blood
meal. Once digestion is completed, trypsin is excreted, but the consti
tutive trypsin level is restored within 24 h, before the next blood me
al is taken. In A. gambiae, A. stephensi, and A. quadrimaculatus, the
constitutive trypsin component is also present, but at much lower leve
ls. In A. albimanus fed multiple blood meals al 24 h intervals, trypsi
n oscillates at nearly maximal levels as long as blood is present in t
he midgut and depending on the ovarian status. Expression of the two t
rypsin components in A. albimanus was found to be independent of the n
eurosecretory system, but synthesis of the constitutive trypsin appear
s to require the presence of the corpora allata. In all species tested
, chymotrypsin is secreted after a blood meal in a similar temporal pa
ttern as trypsin, but it is never present before the blood meal. Reinv
estigating several aedine species for the presence of chymotrypsin by
using different substrates revealed measurable quantities in blood-fed
females compared to earlier reports. Equally, aminopeptidase activity
is present in all species tested and characterized by a constitutive
component. Its activities follow different temporal patterns than the
endopeptidases. (C) 1995 Wiley-Liss, Inc.