Are insects resistant to plant proteinase inhibitors?
Six species of Lepidoptera were evaluated for their susceptibility to serine proteinase inhibitors from cabbage. Trypsin and chymotrypsin activity from larval Pieris rapae and Pieris napi were not significantly inhibited (0–18%), in vitro, by cabbage proteinase inhibitors, while the serine proteinas...
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Veröffentlicht in: | Journal of insect physiology 1995, Vol.41 (2), p.107-116 |
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description | Six species of Lepidoptera were evaluated for their susceptibility to serine proteinase inhibitors from cabbage. Trypsin and chymotrypsin activity from larval
Pieris rapae and
Pieris napi were not significantly inhibited (0–18%),
in vitro, by cabbage proteinase inhibitors, while the serine proteinase activity in the midguts of larval
Plutella xylostella was moderately inhibited (40–50%), and
Trichoplusia ni, Lymantria dispar, and
Helicoverpa zea were substantially inhibited (55–85%) by cabbage proteinase inhibitors. These results suggest that the growth and development of the latter three species should be reduced following ingestion of these inhibitors. However, chronic ingestion of cabbage proteinase inhibitors only reduced the growth and development of
T. ni. This lack of biological activity of the proteinase inhibitors against the other two species was explained by a shift in the relative proportion of digestive enzymes in response to ingestion of proteinase inhibitors. Following ingestion of cabbage proteinase inhibitors, the predominant trypsin-like enzyme(s) in the midgut of larval
L. dispar and
H. zea were resistant to inhibition by cabbage trypsin inhibitors (13–18% inhibited), while the trypsin(s) in
T. ni was moderately susceptible (37% inhibited). These results were confirmed for
H. zea and
T. ni feeding on proteinase inhibitors in tomato foliage. This is the first demonstration of adaptation to proteinase inhibitors, and has important implications for gene regulation and physiological plasticity. |
doi_str_mv | 10.1016/0022-1910(94)00101-L |
format | Article |
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Pieris rapae and
Pieris napi were not significantly inhibited (0–18%),
in vitro, by cabbage proteinase inhibitors, while the serine proteinase activity in the midguts of larval
Plutella xylostella was moderately inhibited (40–50%), and
Trichoplusia ni, Lymantria dispar, and
Helicoverpa zea were substantially inhibited (55–85%) by cabbage proteinase inhibitors. These results suggest that the growth and development of the latter three species should be reduced following ingestion of these inhibitors. However, chronic ingestion of cabbage proteinase inhibitors only reduced the growth and development of
T. ni. This lack of biological activity of the proteinase inhibitors against the other two species was explained by a shift in the relative proportion of digestive enzymes in response to ingestion of proteinase inhibitors. Following ingestion of cabbage proteinase inhibitors, the predominant trypsin-like enzyme(s) in the midgut of larval
L. dispar and
H. zea were resistant to inhibition by cabbage trypsin inhibitors (13–18% inhibited), while the trypsin(s) in
T. ni was moderately susceptible (37% inhibited). These results were confirmed for
H. zea and
T. ni feeding on proteinase inhibitors in tomato foliage. This is the first demonstration of adaptation to proteinase inhibitors, and has important implications for gene regulation and physiological plasticity.</description><identifier>ISSN: 0022-1910</identifier><identifier>EISSN: 1879-1611</identifier><identifier>DOI: 10.1016/0022-1910(94)00101-L</identifier><language>eng</language><publisher>Elsevier Ltd</publisher><subject>Cabbage ; Chymotrypsin ; Digestive enzymes ; Helicoverpa zea ; Lepidoptera ; Lymantria dispar ; Noctuidae ; Pieridae ; Pieris rapae ; Plutella xylostella ; Plutellidae ; Regulation ; Tomato ; Trichoplusia ni ; Trypsin</subject><ispartof>Journal of insect physiology, 1995, Vol.41 (2), p.107-116</ispartof><rights>1995</rights><lds50>peer_reviewed</lds50><oa>free_for_read</oa><woscitedreferencessubscribed>false</woscitedreferencessubscribed><citedby>FETCH-LOGICAL-c381t-2ec19a097217e0d510304bc73f2065ccaed075b70ba8e52f9696a258f29de0103</citedby><cites>FETCH-LOGICAL-c381t-2ec19a097217e0d510304bc73f2065ccaed075b70ba8e52f9696a258f29de0103</cites></display><links><openurl>$$Topenurl_article</openurl><openurlfulltext>$$Topenurlfull_article</openurlfulltext><thumbnail>$$Tsyndetics_thumb_exl</thumbnail><linktohtml>$$Uhttps://dx.doi.org/10.1016/0022-1910(94)00101-L$$EHTML$$P50$$Gelsevier$$H</linktohtml><link.rule.ids>314,780,784,3550,4024,27923,27924,27925,45995</link.rule.ids></links><search><creatorcontrib>Broadway, Roxanne M.</creatorcontrib><title>Are insects resistant to plant proteinase inhibitors?</title><title>Journal of insect physiology</title><description>Six species of Lepidoptera were evaluated for their susceptibility to serine proteinase inhibitors from cabbage. Trypsin and chymotrypsin activity from larval
Pieris rapae and
Pieris napi were not significantly inhibited (0–18%),
in vitro, by cabbage proteinase inhibitors, while the serine proteinase activity in the midguts of larval
Plutella xylostella was moderately inhibited (40–50%), and
Trichoplusia ni, Lymantria dispar, and
Helicoverpa zea were substantially inhibited (55–85%) by cabbage proteinase inhibitors. These results suggest that the growth and development of the latter three species should be reduced following ingestion of these inhibitors. However, chronic ingestion of cabbage proteinase inhibitors only reduced the growth and development of
T. ni. This lack of biological activity of the proteinase inhibitors against the other two species was explained by a shift in the relative proportion of digestive enzymes in response to ingestion of proteinase inhibitors. Following ingestion of cabbage proteinase inhibitors, the predominant trypsin-like enzyme(s) in the midgut of larval
L. dispar and
H. zea were resistant to inhibition by cabbage trypsin inhibitors (13–18% inhibited), while the trypsin(s) in
T. ni was moderately susceptible (37% inhibited). These results were confirmed for
H. zea and
T. ni feeding on proteinase inhibitors in tomato foliage. This is the first demonstration of adaptation to proteinase inhibitors, and has important implications for gene regulation and physiological plasticity.</description><subject>Cabbage</subject><subject>Chymotrypsin</subject><subject>Digestive enzymes</subject><subject>Helicoverpa zea</subject><subject>Lepidoptera</subject><subject>Lymantria dispar</subject><subject>Noctuidae</subject><subject>Pieridae</subject><subject>Pieris rapae</subject><subject>Plutella xylostella</subject><subject>Plutellidae</subject><subject>Regulation</subject><subject>Tomato</subject><subject>Trichoplusia ni</subject><subject>Trypsin</subject><issn>0022-1910</issn><issn>1879-1611</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>1995</creationdate><recordtype>article</recordtype><recordid>eNp9kM1LxDAQxYMouH78Bx56Ej1UZ9KmbS7KsvgFBS96Dmk6xcjuds1kBf97U1c8eppheO8x7yfEGcIVAlbXAFLmqBEudHkJkG55uydm2NQ6xwpxX8z-JIfiiPkdAFTVqJlQ80CZXzO5yFkg9hztOmZxzDbLadmEMZJfW55Ub77zcQx8eyIOBrtkOv2dx-L1_u5l8Zi3zw9Pi3mbu6LBmEtyqC3oWmJN0CuEAsrO1cUgoVLOWeqhVl0NnW1IyUFXurJSNYPUPaUaxbE43-WmNz62xNGsPDtaptdo3LLBqkFUoJKw3AldGJkDDWYT_MqGL4NgJkZmAmAmAEaX5oeRaZPtZmejVOLTUzDsPK0d9T4kIqYf_f8B343fbKs</recordid><startdate>1995</startdate><enddate>1995</enddate><creator>Broadway, Roxanne M.</creator><general>Elsevier Ltd</general><scope>AAYXX</scope><scope>CITATION</scope><scope>7SS</scope></search><sort><creationdate>1995</creationdate><title>Are insects resistant to plant proteinase inhibitors?</title><author>Broadway, Roxanne M.</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c381t-2ec19a097217e0d510304bc73f2065ccaed075b70ba8e52f9696a258f29de0103</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>1995</creationdate><topic>Cabbage</topic><topic>Chymotrypsin</topic><topic>Digestive enzymes</topic><topic>Helicoverpa zea</topic><topic>Lepidoptera</topic><topic>Lymantria dispar</topic><topic>Noctuidae</topic><topic>Pieridae</topic><topic>Pieris rapae</topic><topic>Plutella xylostella</topic><topic>Plutellidae</topic><topic>Regulation</topic><topic>Tomato</topic><topic>Trichoplusia ni</topic><topic>Trypsin</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Broadway, Roxanne M.</creatorcontrib><collection>CrossRef</collection><collection>Entomology Abstracts (Full archive)</collection><jtitle>Journal of insect physiology</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Broadway, Roxanne M.</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Are insects resistant to plant proteinase inhibitors?</atitle><jtitle>Journal of insect physiology</jtitle><date>1995</date><risdate>1995</risdate><volume>41</volume><issue>2</issue><spage>107</spage><epage>116</epage><pages>107-116</pages><issn>0022-1910</issn><eissn>1879-1611</eissn><abstract>Six species of Lepidoptera were evaluated for their susceptibility to serine proteinase inhibitors from cabbage. Trypsin and chymotrypsin activity from larval
Pieris rapae and
Pieris napi were not significantly inhibited (0–18%),
in vitro, by cabbage proteinase inhibitors, while the serine proteinase activity in the midguts of larval
Plutella xylostella was moderately inhibited (40–50%), and
Trichoplusia ni, Lymantria dispar, and
Helicoverpa zea were substantially inhibited (55–85%) by cabbage proteinase inhibitors. These results suggest that the growth and development of the latter three species should be reduced following ingestion of these inhibitors. However, chronic ingestion of cabbage proteinase inhibitors only reduced the growth and development of
T. ni. This lack of biological activity of the proteinase inhibitors against the other two species was explained by a shift in the relative proportion of digestive enzymes in response to ingestion of proteinase inhibitors. Following ingestion of cabbage proteinase inhibitors, the predominant trypsin-like enzyme(s) in the midgut of larval
L. dispar and
H. zea were resistant to inhibition by cabbage trypsin inhibitors (13–18% inhibited), while the trypsin(s) in
T. ni was moderately susceptible (37% inhibited). These results were confirmed for
H. zea and
T. ni feeding on proteinase inhibitors in tomato foliage. This is the first demonstration of adaptation to proteinase inhibitors, and has important implications for gene regulation and physiological plasticity.</abstract><pub>Elsevier Ltd</pub><doi>10.1016/0022-1910(94)00101-L</doi><tpages>10</tpages><oa>free_for_read</oa></addata></record> |
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language | eng |
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source | Access via ScienceDirect (Elsevier) |
subjects | Cabbage Chymotrypsin Digestive enzymes Helicoverpa zea Lepidoptera Lymantria dispar Noctuidae Pieridae Pieris rapae Plutella xylostella Plutellidae Regulation Tomato Trichoplusia ni Trypsin |
title | Are insects resistant to plant proteinase inhibitors? |
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