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Iraa pri<strong>or</strong> experimental analysis of such inf<strong>or</strong>mation exchange between the feeding-inhibit<strong>or</strong>y messenger menadione<br />

(2-methyt-t ,4-naphthoquinone) from the environment, and sulthydryls in the dendritic membrane of chemosensitive neurons<br />

in the antenna of Periplaneta americana, the electrochemical transduction of inf<strong>or</strong>mational energy into <strong>or</strong>ganismal response<br />

(i.e., activity) was described mathematically as a regression with r= 0.997 (N<strong>or</strong>ris 1986, 1988). Thus, one unit of experimentally<br />

determined input (stimulus) energy from the environment can be mapped (c<strong>or</strong>related) inf<strong>or</strong>mationally upon (related to)<br />

one unit of output (<strong>or</strong>ganismal-response) energy using the proposed sulfur-based encoding mechanism. Some key parameters<br />

of <strong>this</strong> experimentally elucidated sulflaydryl / disulfide-dependent electrochemical mechanism are further discussed in Table<br />

2.<br />

Table 2.--Some key fascets of the sulfhydryl / disulfide-dependent electrochemical mechanism involved in insect perception<br />

of phytochemical (e.g. 1,4-naphthoquinone) messengers.<br />

1. Each of the three possible pairings of the chem<strong>or</strong>eception parameters (a, b, e) yields a linear regression with r > 0.95: (a)<br />

the moles of messenger required in a standardized insect behavi<strong>or</strong>al assay to cause a > 99% change in that behavi<strong>or</strong>; (b) the<br />

maximum in vitro polarographic U_/2shift in millivolts by the involved recept<strong>or</strong> and energy-transducer sulflaydryl / disulfide<br />

protein from the insect's antennal chemosens<strong>or</strong>y neurons when saturated with the above messenger: and (e) the maximum<br />

percent inhibition of a standardized excitant-stimulated electroantannogram (EAG) by the above messenger (Rozental and<br />

N<strong>or</strong>ris 1973, 1975; N<strong>or</strong>ris and Chu 1974; N<strong>or</strong>ris 1979, 1986, 1988).<br />

2. Simultaneous solution of the three linear relationships among the parameters in (1) showed that the c<strong>or</strong>relation (rZ= 0.95)<br />

between (a) the maximum U_/2shift elicited in the sulfhydryl / disulfide recept<strong>or</strong> and energy-transducer protein by the<br />

messenger and (b) the maximum percent inhibition of the standardized EAG by that messenger is so high that only one of<br />

these two parameters need be considered in a mathematical description of the transduction of the molar-messenger energy<br />

into insect behavi<strong>or</strong>al change. Log Y - 3.40 - 0.112 Log X, quantifies the energy-transduction relationship (N<strong>or</strong>ris 1986,<br />

11988).<br />

3. Based on behavi<strong>or</strong>al analyses (Rozental and N<strong>or</strong>ris 1975; N<strong>or</strong>ris 1986, 1988), three distinct sets of sulfhydryl (thiol)dependent<br />

recept<strong>or</strong> sites f<strong>or</strong> 2-methyl-1,4-naphthoquinone (menadione) messenger exist in the recept<strong>or</strong> and energy-transducing<br />

protein in Periplaneta americana. Those sulfhydryls in each of these three sets of recept<strong>or</strong> sites cause a 4-5 millivolt<br />

shift in the recept<strong>or</strong> and energy-transducing protein's U_/2value when they react at the mercury electrode involved in <strong>this</strong><br />

polarographic analysis (Rozental and N<strong>or</strong>ris 1973; N<strong>or</strong>ris 1979, 1986, 1988).<br />

4. Based on the EAG-inhibition assay, messenger-menadione saturation of one set of recept<strong>or</strong> sites, as described in (3),<br />

causes about an 8% inhibition (N<strong>or</strong>ris and Chu 1974; N<strong>or</strong>ris 1986, 1988). Thus, the the<strong>or</strong>etical maximal inhibition of the<br />

standardized EAG by saturation of the recept<strong>or</strong>s in all three sites with menadione might be predicted as 3 (sites) times 8%,<br />

which equals 24%. It is interesting and significant that the experimentally determined range in maximal percent of EAG<br />

inhibition by saturation with menadione was 23-25%.<br />

5. Data summarized in (3) and (4) above lead to the interpretation that a recept<strong>or</strong> and energy-transducer Uz/2shift of 4-5 mV<br />

equals an 8% inhibition in the EAG. This means that each 4-5 mV shift in the Uu2 is accompanied by an 8% inhibition in the<br />

standardized EAG. The observed linear relationship between the U_a millivolt shift in the recept<strong>or</strong> and energy-transducer<br />

protein and the percent EAG inhibition shows that the primary encoding of the message dictating the whole-insect behavi<strong>or</strong><br />

occurs in the energy-transducer protein in the chemosens<strong>or</strong>y sensillum (N<strong>or</strong>ris 1979, 1986, 1988).<br />

6. Our research explains f<strong>or</strong> the first time, both in electrochemical and electrophysiological parameters, why the EAG is so<br />

meaningful to an understanding of the chemical senses of insects. EAG does not just measure millivolts of electrical energy,<br />

but also the energy after it has already been coded as inf<strong>or</strong>mation in the recept<strong>or</strong> and energy-transducer protein adequately to<br />

elicit a predictable behavi<strong>or</strong> in (by) the insect (N<strong>or</strong>ris 1979, 1981, 1986, 1988).<br />

7. Saturation of the recept<strong>or</strong> and energy-transducer protein with p-chl<strong>or</strong>omercuribenzoate (PCMB), a compound which reacts<br />

. specifically and irreversibly with sulfhydryls, blocks the above characterized messenger-induced Uu2 shift in the protein.<br />

Thus, the conversion of molar-messenger energy into electrochemically based inf<strong>or</strong>mation adequate to predict whole-insect<br />

behavi<strong>or</strong> is blocked by the sulfhydryl-specific reagent, PCMB (Rozental and N<strong>or</strong>ris 1973; N<strong>or</strong>ris 1979, 1981, t988).<br />

8. Sulfur, as in sulfhydryl / disulfide redox systems in proteins, is the critical dynamic elemental interface between responsive<br />

cells and the stimulating environment, whether biotic <strong>or</strong> abiotic.<br />

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