• International Journal of Industrial Entomology and Biomaterials
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• v.45 no.1
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• pp.17-21
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• 2022

The present study aimed to determine whether a hemolymph prepared from Antheraea yamamai larvae had the same biological activities using a Bombyx mori hemolymph prior to exposure to lipopolysaccharide (LPS) in order to induce an inflammatory response. The effects of the hemolymph were determined using a reverse transcription-quantitative polymerase chain reaction to assess the expression of pro-inflammatory molecules. The A. yamamai hemolymph exerted anti-inflammatory effects on LPS-activated human monocytic leukemia cells via Toll-like receptor (TLR) 4-mediated suppression, similar to the B. mori hemocyte extract. Treatment with the A. yamamai hemolymph significantly suppressed LPS-induced upregulated inducible nitric oxide synthase (iNOS) and cyclooxygenase-2 (COX-2) mRNA expression at all tested concentrations compared with the control, similar to the B. mori immune-challenged hemolymph. Finally, the A. yamamai hemolymph, like the B. mori immune-challenged hemolymph, suppressed all of these concentrations in a dose-independent manner. These results demonstrate that the hemolymph of A. yamamai exhibited important biologically active substances. Further in-depth functional studies are required to fully understand the mechanisms underlying the biological activities of wild-type silkworm hemolymphs.

• International Journal of Industrial Entomology and Biomaterials
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• v.31 no.2
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• pp.127-131
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• 2015

Oak silkworm, Antheraea yamamai (A. yamamai), has been used for clothing and surgical suture and considered as biomaterial due to RGD tripeptide. This paper reported the degumming conditions of A. yamamai using sodium oleate, high pressure and temperature, and sodium carbonate. Degumming ratio of A. yamamai cocoon using sodium oleate was less than 10%. High pressure and temperature treatment induced 30% weight loss of A. yamamai cocoon. The concentration, treatment temperature and time using sodium carbonate was examined and revealed the following conditions for degumming; 5% owf, 60 min at 100℃. The degummed solution was confirmed using UV and FT-IR spectrometer. Our results can be used to handle A. yamamai silkworm cocoon for further application including material processing.

• International Journal of Industrial Entomology and Biomaterials
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• v.21 no.2
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• pp.163-167
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• 2010

[ $\alpha$ ]Glucosidase (EC 3.2.1.20) is a glycosidase that hydrolyzes disaccharides, oligosaccharides, and polysaccharides resulting in the release of α-D-glucose. In this study, $\alpha$-glucosidase activity in the hemolymph and midgut of the mulberry silkworm Bombyx mori and Japanese oak silkmoth Antheraea yamamai was measured using maltose, sucrose, trehalose, and p-nitrophenyl $\alpha$-D-glucopyranoside as substrates. In general, hemolymph $\alpha$-glucosidase activity was higher in B. mori than in A. yamamai. In contrast, midgut $\alpha$-glucosidase activity was higher in A. yamamai than in B. mori for all of the substrates tested. $\alpha$-Glucosidase activity in the midgut of both B. mori and A. yamamai showed similar responses to changes in pH and temperature for all of the substrates tested. Native (7.5%) PAGE of hemolymph and midgut proteins from B. mori and A. yamamai followed by staining with 4-methylumbelliferyl $\alpha$-D-glucoside (MUG) indicated that the $\alpha$-glucosidases of these related lepidopterans are functionally similar but structurally different. In comparison to $\alpha$-glucosidase activity from A. yamamai, $\alpha$-glucosidase activity from B. mori was generally less sensitive to the $\alpha$-glucosidase inhibitors, 1-deoxynojirimycin (DNJ), acarbose, and voglibose when the activity was determined using maltose, sucrose, and trehalose.

• Journal of Life Science
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• v.10 no.1
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• pp.10-13
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• 2000

To develope the genetic source of oak wild silkworm, Antheraea yamamai, the cDNA library was constructed with poly A+ mRNA isolated from posterial silk gland of fifth instar larvae. Titer of the cDNA library was about 5.1$\times$105 pfu in total. We presumed that the titer covered almost all transcripts existed in Antherea yamamai. From cDNA library of Antheraea yamamai, fibroin heavy chain gene, which is specifically expressed from posterial silk gland of Antheraea yamamai, was screened using oligonuclotide probe specific to alanine rich motif of fibrin heavy chain gene of Antheraea pernyi. As a result, fibroin clones isolated from 5$\times$104 plaques showed the highest homolgy (95%) with that of Antherea pernyi in nucleotide of Anthereaea yamamai and Bombyx mori shows that there is no homologous sequence in the 3+ partial 채야후 region Genomic southern hybridization suggested that one copy is present. Northern hybridization showed that fibroin transcript was approximateely 9 kb in length.

• International Journal of Industrial Entomology and Biomaterials
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• v.34 no.1
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• pp.6-10
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• 2017

Dissolution of Antheraea yamamai silkworm cocoon was carried out in various solvent systems with various dissolving conditions including dissolution salts, salt concentration, dissolving temperature, and time. General chaotropic salt for Bombyx mori silk fibroin does not work for A. yamamai silkworm cocoon. Lithium bromide 9.3 M at $100^{\circ}C$ also does not work to dissolve wild silkworm cocoon. However, 9 M of lithium thiocyanate treatment at $100^{\circ}C$ induced 100% dissolution of wild silkworm cocoon. But it could not be dissolved lower than $60^{\circ}C$. Like lithium thiocyanate, less than $60^{\circ}C$ treatment with molten calcium nitrate 4 hydrate could not dissolve wild silkworm cocoon. As the dissolution temperature increased up to $100^{\circ}C$, the solubility of wild one was reached over 90%. SDS-PAGE showed broad tailing stream pattern that means the molecule of wild silk was depolymerized with dissolution temperature and time. From the above results, the best chaotropic salt for A.yamamai silkworm cocoon is calcium nitrate 4 hydrate.

• Journal of Life Science
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• v.9 no.1
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• pp.84-89
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• 1999

To determine phylogenetic relatedness of four silk-producing silkmoths (B. mori, B. mandarina, A. yamamai and A. pernyi), internal coding region of arylphorin which is a storage protein in hemolymph protein of insects were amplified by polymerase chain reaction and then sequenced and compared each other. The nucleotide composition was biased toward adenine and thymine(59% A+T) and a strong bias for use of C in the third position of codons was found for Phe and Tyr. Together TTC(Phe) and TAC(Tyr) account for about 16.8% (10 for TTC and 8 for TAC) of all codon usage. The nucleotide similarity of arylphorin gene from B. mori showed 99%, 98% and 97% homology with those of B. mandarina, A. yamamai and A. pernyi, respectively. Also, the nucleotide sequence of arylphorin gene from B. mandarina showed 98% and 97% homology with those of A. yamamai and A.pernyi, respectively. Between A. yamamai and A. pernyi, the sequence homology was 97%. The deduced amino acid sequences in B. mori, B. mandarina and A. yamamai showed almost 99% homology. Although the aryphorin gene provided insufficient variability among the four insect species, A UPGMA tree is generated that supported the monophyly of silk-producing insects, with M. sexta placed basal to it. It is suggest that silk-producing insects have a close relationship and a homogeneous genetic background from comparison with those of other insects.

• Journal of Sericultural and Entomological Science
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• v.48 no.1
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• pp.11-15
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• 2006

Antheraea yamamai silk fibroin powder was prepared by treatment with HCl. The prepared A. yamamai fibroin hydrolysate was characterized by gel filtration chromatography, amino acid analysis, X-ray diffractometry, circular dichroism analysis, differential thermal analysis, and thermogravimetry. The average molecular weight of A. yamamai powder was about 430 and the major amino acids composed of the powder were Ala and Ser. According to XRD analysis, A. yamamai silk powder showed sharp diffraction peaks at $2{\theta}=20.34^{\circ}\;and\;31.5^{\circ}$. CD spectrum showed a peak around 220 nm and a should 215 nm, assigned to ${\alpha}-helix\;and\;{\beta}-sheet$ structure, respectively. DSC and TGA showed that the maximum degradation temperature of powder was around $250{\sim}270^{\circ}C$. Moreover, no harmful heavy metal was contained in the A. yamamai silk fibroin hydrolysate.

• International Journal of Industrial Entomology and Biomaterials
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• v.1 no.2
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• pp.171-175
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• 2000

Determined sequences of 384 randomly selected clones in a PCR-based cDNA library of Antheraea yamamai could identify expressed sequence tags (ESTs) of highly expressed gene. One EST (fibroin) appeared 15 times, one EST (40S ribosomal protein S18) twelve times, one EST (ribosomal protein S24a) eleven times, ten times (ribosomal protein S8), nine times (60S ribosomal protein L10A), seven times (60S ribosomal protein S15A, S17, S17 and seroin), six times (ribosomal protein S8), five times (ribosomal protein S24, mariner transposase and P8 protein), four times (serpin 2), three times (heat shock protein 70 and poly A binding protein), and the remaining 6 ESTs twice (amylase, KIAA1006, elongation factor-1, transposon mag, translation initiation factor 4C, QM protein, transposase). Therefore, the 94 EST make it possible to identify 24 redundant clones that are candidates for highly expressed genes in posterior silk gland of this insect. The 24 redundant EST clones were identified in GenBank, but none of them was related to A. yamamai, suggesting that there are many unidentified genes which are highly expressed in the A. yamamai genome.

• Journal of Sericultural and Entomological Science
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• v.31 no.2
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• pp.72-81
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• 1989

Antheraea yamamai vitellin was purified from matured eggs by polyacryamide gel electrophoresis, also stage dependent appearance, immunological comparison and relative content of the protein were investigated. 1. Vitellogenin, the precursor of vitellin, was first detected in the larval hemolymph at the late spinning stage by polyacrylamide gel electrophoresis and immunoelectrophoresis. 2. The electrophoretic mobility of the vitellin was identical with that of Bombyx mori and of Bombyx mandarina. However, the specific antiserum against A. uamamai vitellin did not react with either that of Bombyx mori or Bombyx mandarina in immumo-diffusion test. 3. Relative content of A. yamamai vitellin to the total soluble egg protein was 46.0 percent and did not change till eight days after oviposition. But the content started to decline from ten days after oviposition and was negligible in the five or serventeen month old eggs.

• International Journal of Industrial Entomology and Biomaterials
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• v.44 no.2
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• pp.65-71
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• 2022

The wild silkmoth Antheraea yamamai Guérin-Méneville, 1861 (Lepidoptera: Saturniidae) is an important producer of silk that is superior to the silk produced by traditional domesticated silkworm. In this study, we sequenced the complete mitochondrial genome (mitogenome) of An. yamamai collected from Jeju Island, which is the southernmost island approximately 100 km offshore southward from the Korean Peninsula. Determining this sequence will be necessary for tracing the biogeographic history of the species and developing molecular markers for identifying the origin of commercial products. Comparison of the sequence divergence among two available and the current mitogenomes revealed a low but substantial number of substitutions, totaling 23 nucleotides in the whole genome. CytB and ND5 showed the highest variability with five and four variations, respectively, suggesting that these regions will be prior regions to target for subsequent biogeographic and diagnosis study. Phylogenetic reconstruction based on all available sequences of Saturniidae showed that An. yamamai is a sister to the congeneric species An. pernyi, corroborating that Antheraea is a highly supported monophyletic group. The tribe Saturniini was clearly non-monophyletic and interrupted by Attacini and Bunaeini.