TY - JOUR
T1 - 19G1-30 kDa proteins in the membrane of the pupal fat body of Bombyx mori interact with a hemolymph chymotrypsin inhibitor
AU - Ueno, Yoshinori
AU - Okada, Taro
AU - He, Ningjia
AU - Ujita, Minoru
AU - Banno, Yutaka
AU - Kajiura, Zenta
N1 - Funding Information:
This work was supported in part by the National Biore-source Project (Silkworm) from the Ministry of Education, Science and Culture of Japan.
Funding Information:
This work was supported in part by the National Biore-source Project (Silkworm) from the Ministry of Educa-tion, Science and Culture of Japan.
Publisher Copyright:
© 2022, Japanese Society of Sericultural Sciences. All rights reserved.
PY - 2022
Y1 - 2022
N2 - 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 investi-gate 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.
AB - 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 investi-gate 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.
UR - http://www.scopus.com/inward/record.url?scp=85144321933&partnerID=8YFLogxK
UR - http://www.scopus.com/inward/citedby.url?scp=85144321933&partnerID=8YFLogxK
U2 - 10.11416/jibs.91.3_033
DO - 10.11416/jibs.91.3_033
M3 - Article
AN - SCOPUS:85144321933
VL - 91
SP - 33
EP - 39
JO - Journal of Insect Biotechnology and Sericology
JF - Journal of Insect Biotechnology and Sericology
SN - 1346-8073
IS - 3
ER -