19G1-30 kDa proteins in the membrane of the pupal fat body of Bombyx mori interact with a hemolymph chymotrypsin inhibitor
In the silkworm, Bombyx mori, there are 30 kDa proteins that are expressed in the fat body and secreted into the hemolymph. A 19G1-30 kDa protein in the membrane fraction of the late larval midgut is a probable receptor for the hemolymph chymotrypsin inhibitor CI-8. Take-up of CI-8 into the pupal pe...
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| Veröffentlicht in: | Journal of Insect Biotechnology and Sericology 2022, Vol.91(3), pp.3_033-3_039 |
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| container_title | Journal of Insect Biotechnology and Sericology |
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| creator | Ueno, Yoshinori Okada, Taro He, Ningjia Ujita, Minoru Banno, Yutaka Kajiura, Zenta |
| description | In the silkworm, Bombyx mori, there are 30 kDa proteins that are expressed in the fat body and secreted into the hemolymph. A 19G1-30 kDa protein in the membrane fraction of the late larval midgut is a probable receptor for the hemolymph chymotrypsin inhibitor CI-8. Take-up of CI-8 into the pupal perivisceral fat body suggests that the 19G1-30 kDa proteins function as a receptor in the fat body. We used biochemical assays to investigate whether the 19G1-30 kDa proteins were the receptor for CI-8 in the pupal fat body. The results of affinity purification, far western blotting, and western blotting suggested that the 19G1-30 kDa proteins are the interacting factors of the membrane fraction of the pupal fat body. Tissue surface analysis indicated that these proteins were the canonical tissue-surface proteins. Immunological analysis showed that, after the take-up of CI-8 into the fat body, dissociation of the 19G1-30 kDa protein and CI-8 occurred followed by aggregation of the 19G1-30 kDa proteins to form protein granules. The results showed that the 19G1-30 kDa protein is a receptor of CI-8. |
| doi_str_mv | 10.11416/jibs.91.3_033 |
| format | Article |
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A 19G1-30 kDa protein in the membrane fraction of the late larval midgut is a probable receptor for the hemolymph chymotrypsin inhibitor CI-8. Take-up of CI-8 into the pupal perivisceral fat body suggests that the 19G1-30 kDa proteins function as a receptor in the fat body. We used biochemical assays to investigate whether the 19G1-30 kDa proteins were the receptor for CI-8 in the pupal fat body. The results of affinity purification, far western blotting, and western blotting suggested that the 19G1-30 kDa proteins are the interacting factors of the membrane fraction of the pupal fat body. Tissue surface analysis indicated that these proteins were the canonical tissue-surface proteins. Immunological analysis showed that, after the take-up of CI-8 into the fat body, dissociation of the 19G1-30 kDa protein and CI-8 occurred followed by aggregation of the 19G1-30 kDa proteins to form protein granules. The results showed that the 19G1-30 kDa protein is a receptor of CI-8.</description><identifier>ISSN: 1346-8073</identifier><identifier>EISSN: 1884-7978</identifier><identifier>DOI: 10.11416/jibs.91.3_033</identifier><language>eng</language><publisher>Ibaraki: The Japanese Society of Sericultural Science</publisher><subject>Bombyx mori ; Chymotrypsin ; chymotrypsin inhibitor ; Fat body ; Hemolymph ; Immunology ; Inhibitors ; Membrane proteins ; Membranes ; metamorphosis ; Midgut ; Proteins ; receptor ; Receptors ; Silkworms ; Surface analysis (chemical) ; Tissue analysis ; Western blotting</subject><ispartof>Journal of Insect Biotechnology and Sericology, 2022, Vol.91(3), pp.3_033-3_039</ispartof><rights>2022 by Japan Academic Association for Copyright Clearance (Except in the USA), Copyright Clearance Center, Inc. (In the USA)</rights><rights>Copyright Japan Science and Technology Agency 2022</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><link.rule.ids>314,780,784,1881,4022,27922,27923,27924</link.rule.ids></links><search><creatorcontrib>Ueno, Yoshinori</creatorcontrib><creatorcontrib>Okada, Taro</creatorcontrib><creatorcontrib>He, Ningjia</creatorcontrib><creatorcontrib>Ujita, Minoru</creatorcontrib><creatorcontrib>Banno, Yutaka</creatorcontrib><creatorcontrib>Kajiura, Zenta</creatorcontrib><title>19G1-30 kDa proteins in the membrane of the pupal fat body of Bombyx mori interact with a hemolymph chymotrypsin inhibitor</title><title>Journal of Insect Biotechnology and Sericology</title><addtitle>J. Insect Biotechnol. Sericol.</addtitle><description>In the silkworm, Bombyx mori, there are 30 kDa proteins that are expressed in the fat body and secreted into the hemolymph. A 19G1-30 kDa protein in the membrane fraction of the late larval midgut is a probable receptor for the hemolymph chymotrypsin inhibitor CI-8. Take-up of CI-8 into the pupal perivisceral fat body suggests that the 19G1-30 kDa proteins function as a receptor in the fat body. We used biochemical assays to investigate whether the 19G1-30 kDa proteins were the receptor for CI-8 in the pupal fat body. The results of affinity purification, far western blotting, and western blotting suggested that the 19G1-30 kDa proteins are the interacting factors of the membrane fraction of the pupal fat body. Tissue surface analysis indicated that these proteins were the canonical tissue-surface proteins. Immunological analysis showed that, after the take-up of CI-8 into the fat body, dissociation of the 19G1-30 kDa protein and CI-8 occurred followed by aggregation of the 19G1-30 kDa proteins to form protein granules. The results showed that the 19G1-30 kDa protein is a receptor of CI-8.</description><subject>Bombyx mori</subject><subject>Chymotrypsin</subject><subject>chymotrypsin inhibitor</subject><subject>Fat body</subject><subject>Hemolymph</subject><subject>Immunology</subject><subject>Inhibitors</subject><subject>Membrane proteins</subject><subject>Membranes</subject><subject>metamorphosis</subject><subject>Midgut</subject><subject>Proteins</subject><subject>receptor</subject><subject>Receptors</subject><subject>Silkworms</subject><subject>Surface analysis (chemical)</subject><subject>Tissue analysis</subject><subject>Western blotting</subject><issn>1346-8073</issn><issn>1884-7978</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2022</creationdate><recordtype>article</recordtype><recordid>eNo9UE1PxCAUbIwmrqtXzySeu_JKaeHm92qyiRc9EyjUUttSKRutv17WNV7e58y8vEmSc8ArgByKy9aqacVhRQQm5CBZAGN5WvKSHcaa5EXKcEmOk5NpanFEUJovkm_ga0gJRu93Eo3eBWOHCdkBhcag3vTKy8EgV__243aUHaplQMrpeTe9cb2av1DvvI2kYLysAvq0oUESNaZ33dyPDaqauXfBz-MUhe3QWGWD86fJUS27yZz95WXy-nD_cvuYbp7XT7fXm7QFCjStixqAachwTpXSVaGJlkArnBOqSg0Ga84YJ1JrxUvIoK4p4RWRec2KjJVkmVzsdeN7H1szBdG6rR_iSZGx6AvjFNOIutqj2inINyNGb3vpZyF9sFVnxM5cwUGQfYj-_a-qRnphBvIDl6F3Gg</recordid><startdate>2022</startdate><enddate>2022</enddate><creator>Ueno, Yoshinori</creator><creator>Okada, Taro</creator><creator>He, Ningjia</creator><creator>Ujita, Minoru</creator><creator>Banno, Yutaka</creator><creator>Kajiura, Zenta</creator><general>The Japanese Society of Sericultural Science</general><general>Japan Science and Technology Agency</general><scope>7QO</scope><scope>7SS</scope><scope>8FD</scope><scope>FR3</scope><scope>P64</scope></search><sort><creationdate>2022</creationdate><title>19G1-30 kDa proteins in the membrane of the pupal fat body of Bombyx mori interact with a hemolymph chymotrypsin inhibitor</title><author>Ueno, Yoshinori ; Okada, Taro ; He, Ningjia ; Ujita, Minoru ; Banno, Yutaka ; Kajiura, Zenta</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-j1515-f6f118d12045bbdc6d3da15c0435b7d1e0d98893addb97121ff539c3a4f862873</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2022</creationdate><topic>Bombyx mori</topic><topic>Chymotrypsin</topic><topic>chymotrypsin inhibitor</topic><topic>Fat body</topic><topic>Hemolymph</topic><topic>Immunology</topic><topic>Inhibitors</topic><topic>Membrane proteins</topic><topic>Membranes</topic><topic>metamorphosis</topic><topic>Midgut</topic><topic>Proteins</topic><topic>receptor</topic><topic>Receptors</topic><topic>Silkworms</topic><topic>Surface analysis (chemical)</topic><topic>Tissue analysis</topic><topic>Western blotting</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Ueno, Yoshinori</creatorcontrib><creatorcontrib>Okada, Taro</creatorcontrib><creatorcontrib>He, Ningjia</creatorcontrib><creatorcontrib>Ujita, Minoru</creatorcontrib><creatorcontrib>Banno, Yutaka</creatorcontrib><creatorcontrib>Kajiura, Zenta</creatorcontrib><collection>Biotechnology Research Abstracts</collection><collection>Entomology Abstracts (Full archive)</collection><collection>Technology Research Database</collection><collection>Engineering Research Database</collection><collection>Biotechnology and BioEngineering Abstracts</collection><jtitle>Journal of Insect Biotechnology and Sericology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Ueno, Yoshinori</au><au>Okada, Taro</au><au>He, Ningjia</au><au>Ujita, Minoru</au><au>Banno, Yutaka</au><au>Kajiura, Zenta</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>19G1-30 kDa proteins in the membrane of the pupal fat body of Bombyx mori interact with a hemolymph chymotrypsin inhibitor</atitle><jtitle>Journal of Insect Biotechnology and Sericology</jtitle><addtitle>J. Insect Biotechnol. Sericol.</addtitle><date>2022</date><risdate>2022</risdate><volume>91</volume><issue>3</issue><spage>3_033</spage><epage>3_039</epage><pages>3_033-3_039</pages><issn>1346-8073</issn><eissn>1884-7978</eissn><abstract>In the silkworm, Bombyx mori, there are 30 kDa proteins that are expressed in the fat body and secreted into the hemolymph. A 19G1-30 kDa protein in the membrane fraction of the late larval midgut is a probable receptor for the hemolymph chymotrypsin inhibitor CI-8. Take-up of CI-8 into the pupal perivisceral fat body suggests that the 19G1-30 kDa proteins function as a receptor in the fat body. We used biochemical assays to investigate whether the 19G1-30 kDa proteins were the receptor for CI-8 in the pupal fat body. The results of affinity purification, far western blotting, and western blotting suggested that the 19G1-30 kDa proteins are the interacting factors of the membrane fraction of the pupal fat body. Tissue surface analysis indicated that these proteins were the canonical tissue-surface proteins. Immunological analysis showed that, after the take-up of CI-8 into the fat body, dissociation of the 19G1-30 kDa protein and CI-8 occurred followed by aggregation of the 19G1-30 kDa proteins to form protein granules. The results showed that the 19G1-30 kDa protein is a receptor of CI-8.</abstract><cop>Ibaraki</cop><pub>The Japanese Society of Sericultural Science</pub><doi>10.11416/jibs.91.3_033</doi><oa>free_for_read</oa></addata></record> |
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| subjects | Bombyx mori Chymotrypsin chymotrypsin inhibitor Fat body Hemolymph Immunology Inhibitors Membrane proteins Membranes metamorphosis Midgut Proteins receptor Receptors Silkworms Surface analysis (chemical) Tissue analysis Western blotting |
| title | 19G1-30 kDa proteins in the membrane of the pupal fat body of Bombyx mori interact with a hemolymph chymotrypsin inhibitor |
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