Physiology of digestion and the molecular characterization of the major digestive enzymes from Periplaneta americana

Tamaki, Fábio K.; Pimentel, André C.; Dias, Alcides B.; Cardoso, Christiane; Ribeiro, Alberto F.; Ferreira, Cristine Homsi Jorge; Terra, Walter R.

doi:10.1016/j.jinsphys.2014.08.007

Cited by 37 publications

(31 citation statements)

References 44 publications

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“…Allergens from groups 1, 2 and 10 are excreted into the feaces, which facilitates environmental exposure, while others are found predominantly in the bodies [24,39,55,56]. In fact, groups 10, 11 and 12 are digestive enzymes [57]. In contrast, Bla g 4 is expressed only in the adult male reproductive system and transferred to the female within the spermatophore [58].…”

Section: Cockroach Allergens: a Heterogeneous Group Of Proteinsmentioning

confidence: 99%

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New Insights into Cockroach Allergens

Pomés

Mueller

Randall

et al. 2017

Curr Allergy Asthma Rep

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Purpose of review This review addresses the most recent developments on cockroach allergen research in relation to allergic diseases, especially asthma. Recent findings The number of allergens relevant to cockroach allergy has recently expanded considerably up to 12 groups. New X-ray crystal structures of allergens from groups 1, 2 and 5 revealed interesting features with implications for allergen standardization, sensitization, diagnosis and therapy. Summary Cockroach allergy is strongly associated with asthma particularly among children and young adults living in inner-city environments, posing challenges for disease control. Environmental interventions targeted at reducing cockroach allergen exposure have provided conflicting results. Immunotherapy may be a way to modify the natural history of cockroach allergy and decrease symptoms and asthma severity among sensitized and exposed individuals. The new information on cockroach allergens is important for the assessment of allergen markers of exposure and disease, and for the design of immunotherapy trials.

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Section: Cockroach Allergens: a Heterogeneous Group Of Proteinsmentioning

confidence: 99%

“…These enzymes hydrolyze the N-acetyl-D-glucosamine 1,4-β-linkages of chitin polymers and are essential for digestion of chitin [63,111]. Chitinases, together with trypsins (group 10) and α-amylases (group 11), are part of the major digestive enzymes in cockroach [57]. …”

Section: Cockroach Allergens: a Heterogeneous Group Of Proteinsmentioning

confidence: 99%

New Insights into Cockroach Allergens

Pomés

Mueller

Randall

et al. 2017

Curr Allergy Asthma Rep

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“…Similarly, cDNA cloning and characterization of the amylase ( AMY ) gene have been reported in a number of insect species (reviewed in Bezerra et al ., ). Research focused specifically on insect gut AMY gene expression has centered around 4 species: Periplaneta americana (American cockroach: Tamaki et al ., ), Anthonomus grandis (cotton boll weevil: Oliveira‐Neto et al ., ), Drosophila melanogaster (fruit fly: Thompson et al ., ), and Bombyx mori (silkworm: Ngernyuang et al ., ). These studies have generally found that AMY expression is immediately dependent upon food accessibility.…”

Section: Introductionmentioning

confidence: 99%

“…In P. americana, amylase activity seems to be present throughout the alimentary tract, peaking in the crop (Tamaki et al, 2014). However, reverse transcription-PCR analyses have indicated that amylases are not expressed or synthesized in the crop, but in the salivary glands and midgut.…”

Section: Introductionmentioning

confidence: 99%

Adipokinetic hormones control amylase activity in the cockroach (Periplaneta americana) gut

Bodláková¹,

Jedlička

Kodrı́k

2016

Insect Science

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This study examined the biochemical characteristics of α-amylase and hormonal (adipokinetic hormone: AKH) stimulation of α-amylase activity in the cockroach (Periplaneta americana) midgut. We applied two AKHs in vivo and in vitro, then measured resultant amylase activity and gene expression, as well as the expression of AKH receptor (AKHR). The results revealed that optimal amylase activity is characterized by the following: pH: 5.7, temperature: 38.4 °C, K (Michaelis-Menten constant): 2.54 mg starch/mL, and V (maximum reaction velocity): 0.185 μmol maltose/mL/min. In vivo application of AKHs resulted in significant increase of amylase activity: by two-fold in the gastric caeca and 4-7 fold in the rest of the midgut. In vitro experiments supported results seen in vivo: a 24-h incubation with the hormones resulted in the increase of amylase activity by 1.4 times in the caeca and 4-9 times in the midgut. Further, gene expression analyses reveal that AKHR is expressed in both the caeca and the rest of the midgut, although expression levels in the former were 23 times higher than levels in the latter. A similar pattern was found for the amylase (AMY) gene. Hormonal treatment did not affect the expression of either gene. This study is the first to provide evidence indicating direct AKH stimulation of digestive enzyme activity in the insect midgut, supported by specific AKHR gene expression in this organ.

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“…Methylumbelliferyl-based substrates have been used for a wide range of enzyme activities, but the dependence of the fluorescence on ionization of the group at high pHs has led to obligatory discontinuous assays for the majority of cases (Yang and Hamaguchi, 1980; Hoppe, 1983). Particularly, most insect glycosidases have optimal activities in acidic pHs (Gontijo et al, 1998; Terra and Ferreira, 2005; Jacobson et al, 2007; Cançado et al, 2008; Moraes et al, 2012; Tamaki et al, 2014; Moreira et al, 2015). In this way, the development of substrates with groups that fluoresce in acidic pHs would be greatly beneficial for the study of those enzymes.…”

Section: Discussionmentioning

confidence: 99%

Standardization of a Continuous Assay for Glycosidases and Its Use for Screening Insect Gut Samples at Individual and Populational Levels

et al. 2017

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Glycoside Hydrolases (GHs) are enzymes able to recognize and cleave glycosidic bonds. Insect GHs play decisive roles in digestion, in plant-herbivore, and host-pathogen interactions. GH activity is normally measured by the detection of a release from the substrate of products as sugars units, colored, or fluorescent groups. In most cases, the conditions for product release and detection differ, resulting in discontinuous assays. The current protocols result in using large amounts of reaction mixtures for the obtainment of time points in each experimental replica. These procedures restrain the analysis of biological materials with limited amounts of protein and, in the case of studies regarding small insects, implies in the pooling of samples from several individuals. In this respect, most studies do not assess the variability of GH activities across the population of individuals from the same species. The aim of this work is to approach this technical problem and have a deeper understanding of the variation of GH activities in insect populations, using as models the disease vectors Rhodnius prolixus (Hemiptera: Triatominae) and Lutzomyia longipalpis (Diptera: Phlebotominae). Here we standardized continuous assays using 4-methylumbelliferyl derived substrates for the detection of α-Glucosidase, β-Glucosidase, α-Mannosidase, N-acetyl-hexosaminidase, β-Galactosidase, and α-Fucosidase in the midgut of R. prolixus and L. longipalpis with results similar to the traditional discontinuous protocol. The continuous assays allowed us to measure GH activities using minimal sample amounts with a higher number of measurements, resulting in data that are more reliable and less time and reagent consumption. The continuous assay also allows the high-throughput screening of GH activities in small insect samples, which would be not applicable to the previous discontinuous protocol. We applied continuous GH measurements to 90 individual samples of R. prolixus anterior midgut homogenates using a high-throughput protocol. α-Glucosidase and α-Mannosidase activities showed the normal distribution in the population. β-Glucosidase, β-Galactosidase, N-acetyl-hexosaminidase, and α-Fucosidase activities showed non-normal distributions. These results indicate that GHs fluorescent-based high-throughput assays apply to insect samples and that the frequency distribution of digestive activities should be considered in data analysis, especially if a small number of samples is used.

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Physiology of digestion and the molecular characterization of the major digestive enzymes from Periplaneta americana

Cited by 37 publications

References 44 publications

New Insights into Cockroach Allergens

New Insights into Cockroach Allergens

Adipokinetic hormones control amylase activity in the cockroach (Periplaneta americana) gut

Standardization of a Continuous Assay for Glycosidases and Its Use for Screening Insect Gut Samples at Individual and Populational Levels

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