Transcriptome Sequencing and Developmental Regulation of Gene Expression in Anopheles aquasalis

Costa-da-Silva, André Luis; Marinotti, Osvaldo; Ribeiro, José M. C.; Silva, Maria C. P.; Lopes, Adriana Rios; Barros, Michele S.; Sá-Nunes, Anderson; Kojin, Bianca Burini; Carvalho, Enéas; Suesdek, Lincoln; Silva-Neto, Mário A.C.; James, Anthony A.; Capurro, Margareth Lara

doi:10.1371/journal.pntd.0003005

Cited by 10 publications

(7 citation statements)

References 91 publications

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“…This observation suggests the presence of a catalytic mechanism of AMPs such as serine protease-endopeptidase in the intestine of A. darlingi (Marinotti et al 2013). Transcriptome analysis of A. aquasalis females fed with sugar showed the expression of trypsin-type peptidases (Costa-da-Silva et al 2014). Muller et al (1995 reported that A. gambiae expressed a set of seven trypsin genes, including antryp1 and antryp2, which are induced after feeding w i t h blood, while antryp3, antryp4, and antryp7 are constitutively expressed and undetectable after feeding with blood (Borges-Veloso et al 2015).…”

Section: Discussionmentioning

confidence: 89%

Differential expression of trypsin-3 and phosrestin II genes in the main malaria vector, Anopheles darlingi, from the Brazilian Amazon region

Ohse¹,

Chi²,

Matiolli³

et al. 2017

gmr

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Anopheles darlingi is the most anthropophilic mosquito related to Plasmodium infection of malaria, causing significant morbidity and mortality in South America. Pyrethroid chemical has been used to control mosquitos. We analyzed the expression of trypsin-3 and phosrestin II genes implicated to feeding and resistance to insecticides, immune response and sensory antenna mechanisms, respectively, of larvae and adult of A. darlingi, through quantitative reverse transcription polymerase chain reaction (qRT-PCR). We aimed to validate the similarity in nucleotide sequences of A. darlingi RNA sequencing libraries by in silico, and qRT-PCR, owing to their possible effects on the ability to spread disease. The expression of trypsin-3 and phosrestin II was higher in the first and second instar larvae as compared with that in adults. These differentially expressed trypsin-3 and phosrestin II genes do not provide us evidence that both genes participate in pyrethroid resistance. The signaling pathway involving both genes requires further study. Preliminary phylogenetic relationships and the accumulation of mutations analysis in both genes were also compared with trypsin and phosrestin sequences of 15 and 17 other anopheline species, respectively, to obtain a mutational rate of 0.02 on phylogenetic trees. Trypsin gene of A. darlingi and A. albimanus clustered into the same group and was distinct from the species of A. gambiae complex and other anopheline. For phosrestin II, A. darlingi Rafael MS, et al. 2 Genetics and Molecular Research 16 (4): gmr16039852 was separated from the remaining species from Africa, Asia, and Europe. Although the groups showed low to moderate support, it is possible to infer that both genes may belong to two evolutionary groups: one presents in the anopheline species of New World and other in the anopheline species of Old World, and be useful for future studies.

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Section: Discussionmentioning

confidence: 89%

Differential expression of trypsin-3 and phosrestin II genes in the main malaria vector, Anopheles darlingi, from the Brazilian Amazon region

Ohse¹,

Chi²,

Matiolli³

et al. 2017

gmr

View full text Add to dashboard Cite

show abstract

“…Differences in the expression of distinct serine peptidase-coding transcripts during the different developmental stages of An. aquasalis and between sugar- and blood-feeding females have been described [ 46 ]. In this work, we demonstrated the activity of trypsin-like serine peptidases in the midgut of sugar-feeding females and identified, by MS/MS, peptidases with molecular masses similar to those observed in the zymography, which suggested that these peptidases could be responsible for some of the observed proteolytic bands.…”

Section: Discussionmentioning

confidence: 99%

“…aquasalis females revealed the expression of trypsin-like peptidases. These enzymes have been suggested to be involved in the initial steps of blood digestion or could be related to the regulation of other trypsin genes [ 46 ]. Similarly, early works showed that An.…”

Section: Discussionmentioning

confidence: 99%

Expression of active trypsin-like serine peptidases in the midgut of sugar-feeding female Anopheles aquasalis

et al. 2015

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BackgroundAnopheles aquasalis is a dipteran of the family Culicidae that is widely distributed in the coastal regions of South and Central America. This species acts as a vector of Plasmodium vivax, an important etiological agent of malaria, which represents a serious public health problem. In mosquitoes, trypsin-like serine proteases are important in blood meal digestion, immune responses and reproductive functions. The study of peptidases expressed in the mosquito midgut is essential to understanding the mechanisms of parasite-host interaction and the physiological process of nutrient digestion.MethodsOur study aimed to identify and characterize the proteolytic activities in the midgut of sugar-fed An. aquasalis females using zymographic analyses (substrate-SDS-PAGE), in-solution assays and mass spectrometry.ResultsHere, we used a zymographic analysis to further biochemically characterize the proteolytic profile of the midgut of sugar-feeding An. aquasalis females. The trypsin peptidases migrated between ~17 and ~76 kDa and displayed higher proteolytic activities between pH 7.5 and 10 and at temperatures between 37 °C and 50 °C. Four putative trypsin-like serine peptidases were identified using mass spectrometry and data mining. The molecular masses of these peptidases were similar to those observed using zymography, which suggested that these peptidases could be responsible for some of the observed proteolytic bands.ConclusionsTaken together, our results contribute to the gene annotation of the unknown genome of this species, to the tissue location of these peptidases, and to the functional prediction of these crucial enzymes, which all impact further studies of this species.

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“…Protein tyrosine phosphatase, non-receptor type 9 (PTPN9) is a soluble tyrosine phosphatase that attenuates prolactin- and EGF-mediated STAT5 activation, which regulates expression of genes that promote cell survival and proliferation in breast cancer cells [ 12 ]. The levels of phosphorylated EGF also are enhanced upon inhibition of PTPN9-mediated by MicroRNA miR-24 [ 80 ]. Studies have shown that PTPN9, in addition to other prototypical tyrosine phosphatases, can down regulate insulin and leptin signal transduction [ 80 ].…”

Section: Ptpn9mentioning

confidence: 99%

“…The levels of phosphorylated EGF also are enhanced upon inhibition of PTPN9-mediated by MicroRNA miR-24 [ 80 ]. Studies have shown that PTPN9, in addition to other prototypical tyrosine phosphatases, can down regulate insulin and leptin signal transduction [ 80 ].…”

Section: Ptpn9mentioning

confidence: 99%

Leptin-Induced JAK/STAT Signaling and Cancer Growth

2016

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Growth factor and cytokine signaling can influence the development of several cancer types. One of the key players in the development of cancer is the Janus kinas (JAK) signal transducer of activators of transcription (STAT) signaling pathway. The majority of growth factors and cytokine interactions with their membrane-bound receptors trigger JAK-STAT activation. The influential relationship between obesity and cancer is a fact. However, there is a complex sequence of events contributing to the regulation of this mechanism to promote tumor growth, yet to be fully elucidated. The JAK-STAT pathway is influenced by obesity-associated changes that have been shown to impact cancer growth and progression. This intricate process is highly regulated by a vast array of adipokines and cytokines that exert their pleiotropic effects on cancer cells to enhance metastasis to distant target sites. Leptin is a cytokine, or more precise, an adipokine secreted mainly by adipose tissue that requires JAK-STAT activation to exert its biological functions. Leptin is the central regulator of energy balance and appetite. Leptin binding to its receptor OB-R in turn activates JAK-STAT, which induces proliferation, angiogenesis, and anti-apoptotic events in normal cells and malignant cells expressing the receptor. Leptin also induces crosstalk with Notch and IL-1 (NILCO), which involves other angiogenic factors promoting tumor growth. Therefore, the existence of multiple novel classes of therapeutics that target the JAK/STAT pathway has significant clinical implications. Then, the identification of the signaling networks and factors that regulate the obesity-cancer link to which potential pharmacologic interventions can be implemented to inhibit tumor growth and metastasis. In this review, we will discuss the specific relationship between leptin-JAK-STAT signaling and cancer.

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Transcriptome Sequencing and Developmental Regulation of Gene Expression in Anopheles aquasalis

Cited by 10 publications

References 91 publications

Differential expression of trypsin-3 and phosrestin II genes in the main malaria vector, Anopheles darlingi, from the Brazilian Amazon region

Differential expression of trypsin-3 and phosrestin II genes in the main malaria vector, Anopheles darlingi, from the Brazilian Amazon region

Expression of active trypsin-like serine peptidases in the midgut of sugar-feeding female Anopheles aquasalis

Leptin-Induced JAK/STAT Signaling and Cancer Growth

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