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碩士 === 國立中央大學 === 生命科學研究所 === 92 === Galectin-1 (GAL1), a β-galactosyl binding lectins, has been shown to modulate cell adhesion, cell-matrix interaction, cell proliferation and some immune functions. GAL1 is an extracellular proteins act to cross-linking cell surface and substrate glycoconjugates....

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Main Authors: Zuo-Ping Ye, 葉佐平
Other Authors: Rong-Nan Huang
Format: Others
Language:zh-TW
Published: 2004
Online Access:http://ndltd.ncl.edu.tw/handle/96652964545453930242
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spelling ndltd-TW-092NCU051050182015-10-13T13:04:43Z http://ndltd.ncl.edu.tw/handle/96652964545453930242 none Galectin-1蛋白對昆蟲生長的影響 Zuo-Ping Ye 葉佐平 碩士 國立中央大學 生命科學研究所 92 Galectin-1 (GAL1), a β-galactosyl binding lectins, has been shown to modulate cell adhesion, cell-matrix interaction, cell proliferation and some immune functions. GAL1 is an extracellular proteins act to cross-linking cell surface and substrate glycoconjugates. It is proposed that GAL1, having a single CRD domain recognized the structural motif Galβ1-4GlcNAc that is similar to that of chitosan membrane (β-1, 4 N-acetyl-D-glucosamine). In an earlier work, we have found that GAL1-coated chitosan membrane could support 3T3 cells proliferation. These studies further investigate 1) the interaction of GAL1 and chitosan in vitro; 2) the effect of GAL1 on insect larvae development. These results showed that GAL1 dose-dependently bind with chitosan in vitro. These results suggested that chitosan could be a nature ligand of GAL1. Furthermore, GAL1 was found to be toxic to some insects, such as the dipteran of Drosophila melanogaster and the lepidoptera of Plutella xylostella. The development of diamondback moth (P. xylostella) larvae were significantly disturbed when feeded with GAL1 extract and/or recombinant GAL1 proteins purified from GAL1 over-expressed E. coli. The development of D. melanogaster larvae were also significantly delayed when feeded with 200-1000µg/ml GAL1; These results indicate the recombiant GAL1 exhibites high insecticidal activity and may be a candidate for bio-insecticide. However, the mechanism of insecticidal toxicity of GAL1 still has to be elucidated Rong-Nan Huang 黃容南 2004 學位論文 ; thesis 66 zh-TW
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language zh-TW
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description 碩士 === 國立中央大學 === 生命科學研究所 === 92 === Galectin-1 (GAL1), a β-galactosyl binding lectins, has been shown to modulate cell adhesion, cell-matrix interaction, cell proliferation and some immune functions. GAL1 is an extracellular proteins act to cross-linking cell surface and substrate glycoconjugates. It is proposed that GAL1, having a single CRD domain recognized the structural motif Galβ1-4GlcNAc that is similar to that of chitosan membrane (β-1, 4 N-acetyl-D-glucosamine). In an earlier work, we have found that GAL1-coated chitosan membrane could support 3T3 cells proliferation. These studies further investigate 1) the interaction of GAL1 and chitosan in vitro; 2) the effect of GAL1 on insect larvae development. These results showed that GAL1 dose-dependently bind with chitosan in vitro. These results suggested that chitosan could be a nature ligand of GAL1. Furthermore, GAL1 was found to be toxic to some insects, such as the dipteran of Drosophila melanogaster and the lepidoptera of Plutella xylostella. The development of diamondback moth (P. xylostella) larvae were significantly disturbed when feeded with GAL1 extract and/or recombinant GAL1 proteins purified from GAL1 over-expressed E. coli. The development of D. melanogaster larvae were also significantly delayed when feeded with 200-1000µg/ml GAL1; These results indicate the recombiant GAL1 exhibites high insecticidal activity and may be a candidate for bio-insecticide. However, the mechanism of insecticidal toxicity of GAL1 still has to be elucidated
author2 Rong-Nan Huang
author_facet Rong-Nan Huang
Zuo-Ping Ye
葉佐平
author Zuo-Ping Ye
葉佐平
spellingShingle Zuo-Ping Ye
葉佐平
none
author_sort Zuo-Ping Ye
title none
title_short none
title_full none
title_fullStr none
title_full_unstemmed none
title_sort none
publishDate 2004
url http://ndltd.ncl.edu.tw/handle/96652964545453930242
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AT yèzuǒpíng galectin1dànbáiduìkūnchóngshēngzhǎngdeyǐngxiǎng
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