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Haemocytes of larval Malacosoma disstria (Lepidoptera: Lasiocampidae) and factors affecting their adhesion to glass slides
Author(s) -
Giannoulis Paschalis,
Brooks Cory L.,
Gulii Vladislav,
Dunphy Gary B.
Publication year - 2005
Publication title -
physiological entomology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.693
H-Index - 57
eISSN - 1365-3032
pISSN - 0307-6962
DOI - 10.1111/j.1365-3032.2005.00459.x
Subject(s) - biology , activator (genetics) , calcium , lepidoptera genitalia , microbiology and biotechnology , instar , biochemistry , protein kinase a , botany , enzyme , larva , receptor , materials science , metallurgy
. Although haemocytes of the forest pest lepidopteran, Malacosoma disstria (L.) have been studied, the physico‐chemical factors and signalling components affecting their non‐self activities have not been examined. Both the ameboid and stellate forms of plasmatocytes and the granular cells from fifth‐instar larvae adhere best to glass slides with phosphate‐buffered saline (PBS), with maximum granular cell binding within a pH range of 6.0–7.0 and plasmatocyte binding at pH 6.0. The divalent cations, calcium and magnesium, do not affect granular cell attachment. However, calcium in Galleria ‐anticoagulant and PBS and, to a lesser extent, magnesium in the anticoagulant, increase plasmatocyte‐glass contact. Based upon the use of selective type I protein kinase A inhibitor (Rp‐8‐Br‐cAMPS) and activator (Sp‐8‐Br‐cAMPS), active protein kinase A inhibits the adhesion of both haemocyte types. Similarly, protein kinase C inhibited by Gö 6976 enhances haemocyte adhesion whereas the enzyme activator, phorbol‐myristate‐acetate, impairs attachment.