Identification of Immune-Related Protein Kinases from Mosquitoes (Aedes aegypti)

Chiou, Jia-Yia; Huang, Shwu-Ju; Huang, Shiann-Tarng; Cho, Wen-Long

doi:10.1159/000025321

Cited by 12 publications

(10 citation statements)

References 28 publications

(41 reference statements)

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“…The confirmed VCB fragment was used to screen a mosquito vitellogenic fat body cDNA library which was constructed at the EcoRI site of the Zap II vector (Stratagene). The conditions for reverse transcription, PCR amplification, and cDNA cloning were previously described (53,54). The method of enzymatic sequencing utilized was that reported by Sanger et al (55).…”

Section: Methodsmentioning

confidence: 99%

Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor

Cho

Tsao

Hays

et al. 1999

Journal of Biological Chemistry

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185

126

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Here we report identification of a novel member of the thiol protease superfamily in the yellow fever mosquito, Aedes aegypti. It is synthesized and secreted as a latent proenzyme in a sex-, stage-, and tissue-specific manner by the fat body, an insect metabolic tissue, of female mosquitoes during vitellogenesis in response to blood feeding. The secreted, hemolymph form of the enzyme is a large molecule, likely a hexamer, consisting of 44-kDa subunits. The deduced amino acid sequence of this 44-kDa precursor shares high similarity with cathepsin B but not with other mammalian cathepsins. We have named this mosquito enzyme vitellogenic cathepsin B (VCB). VCB decreases to 42 kDa after internalization by oocytes. In mature yolk bodies, VCB is located in the matrix surrounding the crystalline yolk protein, vitellin. At the onset of embryogenesis, VCB is further processed to 33 kDa. The embryo extract containing the 33-kDa VCB is active toward benzoyloxycarbonyl-ArgArg-para-nitroanilide, a cathepsin B-specific substrate, and degrades vitellogenin, the vitellin precursor. Both of these enzymatic activities are prevented by transepoxysuccinyl-L-leucylamido-(4-guanidino)butane (E-64), a thiol protease inhibitor. Furthermore, addition of the anti-VCB antibody to the embryonic extract prevented cleavage of vitellogenin, strongly indicating that the activated VCB is involved in embryonic degradation of vitellin.Cathepsin B is a thiol (cysteine) protease with both endopeptidase and peptidyldipeptidase activities. Due to its broad specificity, cathepsin B plays a key role in intracellular protein catabolism in the lysosomal system (1). Cathepsin B has been well characterized both enzymatically and molecularly (2-10). The mammalian cathepsin B has been implicated in tumor invasion, progression, and metastasis (11-15). Tumor-specific cathepsin B is secreted by malignant cells as a latent high molecular weight precursor, presumably activated at cell contacts (16,17).In addition, cathepsins B, as well as the related cathepsins L, have been identified in numerous parasitic protozoa and helminthes, including prevalent pathogens of human and domestic animals (18 -26). In the blood-sucking bug, Rhodnius prolixus, cathepsin B is the major gut proteolytic enzyme (27). In these organisms, cathepsins B and L are presumably involved in the degradation of host hemoglobin.In insects and other arthropods, cathepsins B and L also participate in key developmental processes. In the flesh fly, Sarcophaga peregrina, hemocytes produce the extracellular form of a cathepsin B-like enzyme that participates in decomposition of the larval fat body during metamorphosis (28 -30). Moreover, cathepsins B and L have been implicated in degradation of yolk proteins during embryonic development (31-41).The elucidation of developmental mechanisms in the mosquito is important because this insect transmits the most devastating of vector-borne human diseases, including malaria, lymphatic filariasis, Dengue fever, and many others. Little is known, however, about t...

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Section: Methodsmentioning

confidence: 99%

Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor

Cho

Tsao

Hays

et al. 1999

Journal of Biological Chemistry

Self Cite

185

126

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“…Closely related homologs can be found in species ranging from the nematode [34], mosquito [3], fruit fly (GeneBank AF181637), zebrafish [Huang, pers. commun. ], plant [25] and mouse [28], to human [14,29,36].…”

Section: Introductionmentioning

confidence: 99%

Utilization of <i>Drosophila</i> Eye to Probe the Functions of Two Mammalian Serine/Threonine Kinases, Snk and HsHPK

Liu¹,

Huang²,

Chou³

et al. 2001

Journal of Biomedical Science

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Here we report a quick functional analysis of two mammalian serine/threonine kinases, a serum inducible kinase (Snk) and Homo sapiens hepatoma protein kinase (HsHPK), using Drosophila eye as a model system. We generated transgenic fly lines carrying constructs of both kinases under control of the GAL upstream activating sequence (UAS). Each UAS line was then crossed to a line in which GAL4 expression was driven by one of the following promoters, eyeless (ey),glass or decapentaplegic. Thus, different kinase mutants can be ectopically expressed in a promoter-dependent manner. We observed that the ectopic expression of either the wild-type or active form of Snk driven by the glass promoter resulted in a rough-eye phenotype. Nevertheless, the ectopic expression of HsHPK under the control of the ey promoter resulted in a small-eye phenotype. The results of this study demonstrated that ectopic expression of these two mammalian genes could be achieved by the regulation of Drosophila promoters. In addition, the effects of these ectopically expressed genes on eye development could be an implication of their functions with respect to cell proliferation and differentiation. Thus, Drosophila eye, with the powerful genetic tools and vast information on eye development available, can be a useful system to probe the functions of mammalian genes in the postgenome era.

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“…Among the human kinases, there are 18 receptor tyrosine kinases, 10 nonreceptor tyrosine kinases and 10 dual kinases. The profiles reported in this issue reveal the tyrosine kinases expressed in chicken erythroid progenitor cells and transformed erythroblasts [17], rat primary neurons derived from cerebral cortex, hippocampus and sympathetic ganglia [15], mosquito tissues with an without induced immunity [3], and in human gastric cancer cells and their non-cancerous counterparts [14]. Tyrosine kinases specific to these tissues were identified; for instance, c-kit is found in chicken erythroid cells [17] and Eph A3 and 4 receptors in rat neurons [15].…”

Section: Tyrosine Kinase Profilementioning

confidence: 99%

“…Tyrosine kinases specific to these tissues were identified; for instance, c-kit is found in chicken erythroid cells [17] and Eph A3 and 4 receptors in rat neurons [15]. Several novel kinases, mostly serine/threonine kinases, were identified in this process such as HsHPK [9], KFC, a STE20-like kinase [17], CaMKK [8], and AaCHED [3]. The information generated will be useful in the future identification of tumorspecific markers and in setting up a more complete database for tyrosine kinases and serine kinases.…”

Section: Tyrosine Kinase Profilementioning

confidence: 99%

Molecular Profiling of Tyrosine Kinases in Normal and Cancer Cells

Kung

Chen²,

Robinson

1998

J Biomed Sci

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As the post-genome era is approaching, with vast amount of sequence information available and new technology developed, scientists are presented with opportunities to explore in simple analysis the structure and expression pattern of not just a single gene, but of an entire family of genes, if not the entire genome. The concept of ‘molecular profiling’ or ‘expression array’ has thus emerged. The need to simultaneously ‘see’ all genes in the same family is obvious under the precept of the combinatorial process being an underlying principle of complex biological systems: no gene exists in isolation, for virtually every molecule participates in intermolecular interactions. The activation of receptor tyrosine kinases through homo or hetero-dimerization is the prototypic example. In this review, a tyrosine kinase profile technique and its application to studying the expression of tyrosine kinases and the identification of novel kinases will be discussed. This serves as an introduction to the several interesting papers published in this special ‘kinase’ issue of the Journal of Biomedical Sciences, using this technique. A new simplified approach, kinase display, which is an extension of the profiling method and requires only restriction digestion and gel analysis will also be introduced.

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Identification of Immune-Related Protein Kinases from Mosquitoes (Aedes aegypti)

Cited by 12 publications

References 28 publications

Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor

Mosquito Cathepsin B-like Protease Involved in Embryonic Degradation of Vitellin Is Produced as a Latent Extraovarian Precursor

Utilization of <i>Drosophila</i> Eye to Probe the Functions of Two Mammalian Serine/Threonine Kinases, Snk and HsHPK

Molecular Profiling of Tyrosine Kinases in Normal and Cancer Cells

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