Neurosecretory Cells Expressing the Gene for Common Precursor for Diapause Hormone and Pheromone Biosynthesis-Activating Neuropeptide in the Suboesophageal Ganglion of the Silkworm, Bombyx mori

1994 ◽  
Vol 96 (1) ◽  
pp. 27-36 ◽  
Author(s):  
Y. Sato ◽  
M. Ikeda ◽  
O. Yamashita
1963 ◽  
Vol 40 (3) ◽  
pp. 517-530
Author(s):  
KINSAKU HASEGAWA

1. The action of the diapause hormone has been studied by injecting extracts of the heads of male moths or of the brain-suboesophageal ganglion complexes of pupae into pupae expected to produce non-diapause eggs. 2. The effect of the injection of hormone upon young oocytes is to make them develop into diapause eggs. Older oocytes, which have already acquired non-diapause characters, are not affected. 3. The hormone is almost completely inactivated when injected on the day of pupation. The hormone is most effective when injected into pupae 2-3 days old, at which stage the ovarioles have started to grow vigorously. It is ineffective 1-2 days before adult emergence, by which time all the oocytes have acquired non-diapause characters. 4. The hormone is inactivated in all pupae irrespective of whether they are destined to produce diapause eggs or non-diapause eggs. Inactivation of diapause hormone (in contrast to that of juvenile hormone) is partially relieved by exposure to low temperature or by simultaneous injection of indian ink. 5. The extracts prepared as in (1) above do not serve as a stimulant for the brain causing the suboesophageal ganglion to produce diapause hormone. The action of the extract faithfully reflects the function of the diapause hormone which originates in the suboesophageal ganglion.


1964 ◽  
Vol 41 (4) ◽  
pp. 855-863
Author(s):  
KINSAKU HASEGAWA

1. The susceptibility of ‘non-diapause’ pupae to diapause hormone, the sexual difference in production of diapause hormone in the suboesophageal ganglion (SG), the changes in diapause hormone content of the SG during larval-pupal-adult development, and the hormone production in polyvoltine race, were studied by injecting diapause hormone extracts into pupae expected to produce non-diapause eggs. 2. The susceptibility of ‘non-diapause’ pupae of a bivoltine race (Daizo) was very low, or the hormone injected was almost inactivated. The susceptibility of ‘non-diapause’ race to diapause hormone is different in different races. 3. As for sexual differences in content of diapause hormone in moth heads, males are superior to females, which was further substantiated by injecting extracts from the SG of both sexes. 4. From the activity of diapause hormone extracts derived from larval, pupal and adult SG, the hormone production in SG is raised during the late pupal stage, especially in males. It is also observed that larval SG produces the hormone, and the hormone production in the SG of male moths after mating becomes weak. 5. Male moth heads of ‘non-diapause’ worms (polyvoltine race), as well as of ‘diapause’ worms, contain diapause hormone; though activity is less than in ‘diapause’ worms, which reflects the occurrence of diapause eggs caused by SG-transplantation. 6. It is highly probable that the bioassay by injecting diapause hormone extracts reveals the activity of the SG in the silkworm. 7. The activity of the SG in the polyvoltine race has been discussed from standpoint of diapause determination in the silkworm.


1995 ◽  
Vol 65 (2) ◽  
pp. 105-111 ◽  
Author(s):  
Waraporn Pinyarat ◽  
Toru Shimada ◽  
Wei-Hua Xu ◽  
Yukihiro Sato ◽  
Okitsugu Yamashita ◽  
...  

SummaryWe have determined the map position of the gene encoding a common precursor protein for diapause hormone and pheromone biosynthesis-activating neuropeptide (the DH-PBAN gene, Dh)in the silkmoth, Bombyx mori. First we compared the structure of introns in the DH-PBAN gene by the polymerase chain reaction, and found that the Dh locus carried three alleles, DhA1, DhA2 and DhB. The DhA1 and DhA2 alleles contained a fourth intron consisting of 740 bp, whereas DhB had a longer fourth intron of 770 bp. DhA1 and DhA2 contained a fifth intron consisting of 940 bp, whereas the fifth intron in DhB was much longer and consisted of 1700 bp. DhA1 was distinguished from DhA2 by an RFLP in the fifth intron after digestion with Rsa I. Linkage analyses using these polymorphisms showed that Dh was linked to the bp gene on chromosome 11, and independent of markers on chromosomes 1, 2, 3, 4, 5, 6, 7 and 13. To determine the map position, we obtained F1 hybrids between the n501 strain (K DhA1) and the w30 strain ( + KDhB), and backcrossed the F1 hybrid to females of the w30 strain. From the segregation of K and Dh in 864 individuals in the next generation, the recombination value was calculated as 25·5 % between K and Dh. Similarly we obtained backcross progeny between the No. 744 strain (BuDhA1) and the w30 strain ( + BuDhB), and calculated the recombination value between Bu and Dh as 30·4% from 487 progeny. Because k and Bu had already been mapped at positions 11–23·2 cM and 11–28·7 cM, respectively, we mapped Dh at 11--2·2 cM. The Dh locus is different from any loci which are known to control diapause, development or growth.


2004 ◽  
Vol 380 (1) ◽  
pp. 255-263 ◽  
Author(s):  
Tian-Yi ZHANG ◽  
Le KANG ◽  
Zhi-Fang ZHANG ◽  
Wei-Hua XU

Diapause hormone (DH) and PBAN (pheromone biosynthesis-activating neuropeptide) are two important insect neuropeptides regulating development and reproduction respectively. In the present study, we report two Bombyx mori transcription factors interacting specifically with the promoter of Bom-DH-PBAN (where Bom-DH stands for B. mori DH); we named them DHMBP-1 and -2 (DH-modulator-binding proteins 1 and 2). The developmental changes of DHMBP-1/-2 are closely correlated with that of Bom-DH-PBAN mRNA throughout the pupal stage. Competition assays indicate that DHMBP-1 from Chinese B. mori possesses binding characteristics similar to those of the POU-M1 protein from Japanese B. mori. POU-M1 cDNAs were cloned from various tissues of Chinese B. mori and were found to be distinct from the previously published POU-M1 in amino acid residues 108–136 because of insertion mutations. Owing to this difference in amino acid residues, we named this cDNA POU-M2. Even though POU-M2 differs from POU-M1 at the N-terminal, the POU domain and the binding properties of both POU-M1 and -M2 are the same. Functional analysis showed that overexpression of POU-M2 in the Bombyx cell line BmN activated the promoter of Bom-DH-PBAN, but failed to activate a promoter in which the POU-binding element was mutated. The transcriptional activity of POU-M2 is probably regulated by other factors binding to the upstream of the promoter sequence. We show that the POU-M2-binding site was able to activate the transcription of a heterologous promoter of the gene encoding B. mori larval serum protein. POU-M1 was found to exhibit the same transcriptional activities as POU-M2. Taken together, these results demonstrate that POU-M2 plays an important role in the transcriptional regulation of the Bom-DH-PBAN gene.


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