Slippery pores: anti-adhesive effect of nanoporous substrates on the beetle attachment system.

Traction experiments with adult seven-spotted ladybird beetles Coccinella septempunctata (L.) were carried out to study the influence of surface structure on insect attachment. Force measurements were performed with tethered walking insects, both males and females, on five different substrates: (i) smooth glass plate, (ii) smooth solid Al(2)O(3) (sapphire) disc, and (iii-v) porous Al(2)O(3) discs (anodisc membranes) with the same pore diameter but different porosity. The traction force of beetles ranged from 0.16 to 16.59 mN in males and from 0.32 to 8.99 mN in females. In both sexes, the highest force values were obtained on smooth solid surfaces, where males showed higher forces than females. On all three porous substrates, forces were significantly reduced in both males and females, and the only difference within these surfaces was obtained between membranes with the highest and lowest porosity. Males produced essentially lower forces than females on porous samples. The reduction in insect attachment on anodisc membranes may be explained by (i) possible absorption of the secretion fluid from insect adhesive pads by porous media and/or (ii) the effect of surface roughness. Differences in attachment between males and females were probably caused by the sexual dimorphism in the terminal structure of adhesive setae.

Inhibition of IL-6-dependent growth of myeloma cells by an acidic peptide repressing the gp130-mediated activation of Src family kinases.

An acidic domain (AD) of gp130 was previously found to interact with the Src family kinase (SFK) Hck. Here, the influence of myristoylated peptides derived from this AD was assessed in the mouse myeloma cell line, 7TD1. The IL-6-dependent growth of 7TD1 cells was reduced by approximately 75%, if 100 microM of myristoylated 18mer peptide (18AD) was included in the growth medium, but was unaffected by a control peptide with scrambled sequence (18sc). A similar differential inhibition by peptides 18AD and 18sc was observed for the erythropoietin-dependent growth of BaF-EH cells expressing chimeric erythropoietin receptor-gp130 and human Hck and for the human myeloma cell line INA-6. While the peptide 18AD concentration inhibiting 50% was approximately 30 microM in 7TD1 and BaF-EH cells, peptide 18AD did not significantly inhibit growth of IL-6-independent MM1.S myeloma and OKT1 hybridoma cells or of BaF-EH cells supplied with IL-3. Treatment with 100 microM peptide 18AD caused the same degree or 60% of apoptosis induction as IL-6 deprivation in 7TD1 or INA-6 cells, respectively. Co-immunoprecipitation experiments revealed that peptide 18AD interfered with the association of Hck and gp130 in 7TD1 lysates in a concentration-dependent manner. IL-6-treatment of INA-6 cells induced the kinase activities of Fyn, Lyn and Hck, but not Src, and the IL-6-induced SFK activities were inhibited by peptide 18AD. Expression in 7TD1 cells of a kinase-inactive Hck mutant (K269R) elicited a dominant-negative effect on cell number increases providing further evidence that SFKs are required for gp130 signalling in myeloma cells.