Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster.

Chihara, Charles S.; Song, Chunyan; LaMonte, Greg; Fetalvero, Kristina M.; Hinchman, Kristy F.; Phan, Helen; Pineda, Mario Javier; Robinson, Kelly E.; Schneider, Gregory P.

doi:10.1093/jis/5.1.26

Cited by 10 publications

(11 citation statements)

References 33 publications

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“…On chromosome 3, we identified omega ( ome , P -value ≥ 1.38e-15) that encodes a dipeptidyl-peptidase and is also highly expressed in the midgut, Cadherin 87A ( Cad87A , P -value ≥ 2.01e-14) that is involved in calcium-dependent cell–cell adhesion and is a juvenile hormone-induced gene ( Li et al 2007 ), and Furin 1 ( Fur1 , P -value ≥ 9.10e-16) that exhibits serine-type endopeptidase activity. Interestingly, both ome and Cad87A function in the ovary ( Chihara et al 2005 ; Zartman et al 2009 ). Cad87A exhibits latitudinal differential expression in male D. melanogaster , possibly indicative of spatially varying selection (L. Zhao et al 2015 ).…”

Section: Resultsmentioning

confidence: 99%

Pool-GWAS on reproductive dormancy in Drosophila simulans suggests a polygenic architecture

Lirakis¹,

Nolte²,

Schlötterer³

2022

G3 Genes|Genomes|Genetics

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The genetic basis of adaptation to different environments has been of long-standing interest to evolutionary biologists. Dormancy is a well-studied adaptation to facilitate overwintering. In Drosophila melanogaster, a moderate number of genes with large effects have been described, which suggests a simple genetic basis of dormancy. On the other hand, genome-wide scans for dormancy suggest a polygenic architecture in insects. In D. melanogaster, the analysis of the genetic architecture of dormancy is complicated by the presence of cosmopolitan inversions. Here we performed a genome-wide scan to characterize the genetic basis of this ecologically extremely important trait in the sibling species of D. melanogaster, D. simulans that lacks cosmopolitan inversions. We performed Pool-GWAS in a South African D. simulans population for dormancy incidence at two temperature regimes (10 °C and 12 °C, LD 10:14). We identified several genes with SNPs that showed a significant association with dormancy (p-value < 1e-13), but the overall modest response suggests that dormancy is a polygenic trait with many loci of small effect. Our results shed light on controversies on reproductive dormancy in Drosophila and have important implications for the characterization of the genetic basis of this trait.

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Section: Resultsmentioning

confidence: 99%

Pool-GWAS on reproductive dormancy in Drosophila simulans suggests a polygenic architecture

Lirakis¹,

Nolte²,

Schlötterer³

2022

G3 Genes|Genomes|Genetics

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“…The enzyme was partially purified from the cockroach brain and intestine (Nassel et al, 2000). In addition, there is a report of a Drosophila melanogaster gene product, which was identified as DPP 4 (Chihara et al, 2005). However, these enzymes have not been characterized as to function or otherwise.…”

Section: Discussionmentioning

confidence: 99%

“…DPP 4 cleaves dipeptides from the N-terminus of a peptide chain of any length, and proline is the most preferred residue in the P1 position (David et al, 1993). DPP 4 has been found in mammals (Erickson et al, 1983), insects (Chihara et al, 2005), plants (Davy et al, 2000) and microorganisms (Gazi et al, 1995;Kabashima et al, 1995).…”

Section: Introductionmentioning

confidence: 99%

Dipeptidyl peptidase 4 – An important digestive peptidase in Tenebrio molitor larvae

Tereshchenkova

Goptar

Kulemzina

et al. 2016

Insect Biochemistry and Molecular Biology

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Dipeptidyl peptidase 4 (DPP 4) is a proline specific serine peptidase that plays an important role in different regulatory processes in mammals. In this report, we isolated and characterized a unique secreted digestive DPP 4 from the anterior midgut of a stored product pest, Tenebrio molitor larvae (TmDPP 4), with a biological function different than that of the well-studied mammalian DPP 4. The sequence of the purified enzyme was confirmed by mass-spectrometry, and was identical to the translated RNA sequence found in a gut EST database. The purified peptidase was characterized according to its localization in the midgut, and substrate specificity and inhibitor sensitivity were compared with those of human recombinant DPP 4 (rhDPP 4). The T. molitor enzyme was localized mainly in the anterior midgut of the larvae, and 81% of the activity was found in the fraction of soluble gut contents, while human DPP 4 is a membrane enzyme. TmDPP 4 was stable in the pH range 5.0-9.0, with an optimum activity at pH 7.9, similar to human DPP 4. Only specific inhibitors of serine peptidases, diisopropyl fluorophosphate and phenylmethylsulfonyl fluoride, suppressed TmDPP 4 activity, and the specific dipeptidyl peptidase inhibitor vildagliptin was most potent. The highest rate of TmDPP 4 hydrolysis was found for the synthetic substrate Arg-Pro-pNA, while Ala-Pro-pNA was a better substrate for rhDPP 4. Related to its function in the insect midgut, TmDPP 4 efficiently hydrolyzed the wheat storage proteins gliadins, which are major dietary proteins of T. molitor.

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“…RNAi knockdown of Slfc encoding a secreted serine protease causes male infertility ( 35 ). When a membrane serine protease encoded by ome was mutated, males became subfertile ( 36 ). RNAi knockdown of a secreted metalloprotease encoded by Mmp2 caused female subfertility because ovulation was blocked ( 37 ).…”

Section: Multicellular Organisms I: Invertebratesmentioning

confidence: 99%

Proteolysis in Reproduction: Lessons From Gene-Modified Organism Studies

Kiyozumi

Ikawa

2022

Front. Endocrinol.

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The physiological roles of proteolysis are not limited to degrading unnecessary proteins. Proteolysis plays pivotal roles in various biological processes through cleaving peptide bonds to activate and inactivate proteins including enzymes, transcription factors, and receptors. As a wide range of cellular processes is regulated by proteolysis, abnormalities or dysregulation of such proteolytic processes therefore often cause diseases. Recent genetic studies have clarified the inclusion of proteases and protease inhibitors in various reproductive processes such as development of gonads, generation and activation of gametes, and physical interaction between gametes in various species including yeast, animals, and plants. Such studies not only clarify proteolysis-related factors but the biological processes regulated by proteolysis for successful reproduction. Here the physiological roles of proteases and proteolysis in reproduction will be reviewed based on findings using gene-modified organisms.

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Identification and partial characterization of the enzyme of omega: one of five putative DPP IV genes in Drosophila melanogaster.

Cited by 10 publications

References 33 publications

Pool-GWAS on reproductive dormancy in Drosophila simulans suggests a polygenic architecture

Pool-GWAS on reproductive dormancy in Drosophila simulans suggests a polygenic architecture

Dipeptidyl peptidase 4 – An important digestive peptidase in Tenebrio molitor larvae

Proteolysis in Reproduction: Lessons From Gene-Modified Organism Studies

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