Biomedical subjects

Y J Hua

Publications and source records attributed to Y J Hua.

6 recordsLinked to original sources

PubMed2001

[A study on breeding of "Ganzaoxian 47" from dry seeds of rice carried by recoverable satellite].

OBJECTIVE: To observe and investigate the variation and heredity of the offspring of dry seeds of rice carried by satellite, hence to select early maturing mutants, and to cultivate directly "Ganzaoxian 47" new varieties for production application. Isozymes analyses and studies of the new varieties and its original CK varieties were made. METHOD: Dry seeds of rice restorer line were carried to the space on board a recoverable satellite for 7 d in 1992. After recovery the seeds were planted in the field to study the agricultural characters, yield, disease resistance, rice quality and peroxidase isozymes change. RESULT: Its agricultural characters, yield, disease resistance, rice quality and peroxidase isozymes all showed distinct changes, and new varieties were cultivate directively for production application. CONCLUSION: It could be considered that certain variations of the rice seeds induced by the space conditions were heritable to the offspring's, and directive cultivation of new varieties is possible for production application. It could be used as a new method for mutagenic seed breeding.

Biomass↗

PubMed1999

Identification of a prothoracicostatic peptide in the larval brain of the silkworm, Bombyx mori.

Prothoracicotropic hormone (PTTH) stimulates ecdysteroid biosynthesis in the prothoracic gland (PG) of insects. A peptide inhibiting ecdysteroid biosynthesis in the PG was isolated from the extracts of 2,000 larval brains of the silkworm, Bombyx mori, using a protocol that included four reversed-phase high performance liquid chromatography procedures. The primary structure of this prothoracicostatic peptide (Bom-PTSP) was determined to be H-Ala-Trp-Gln-Asp-Leu-Asn-Ser-Ala-Trp-NH(2). This neuropeptide has the same sequence as Mas-MIP-I, a myoinhibitory peptide previously isolated from the ventral nerve cord of the tobacco hornworm, Manduca sexta, and is highly homologous with the N-terminal portion of vertebrate peptides of the galanin family. This peptide inhibited PTTH-stimulated ecdysteroidogenesis in the PG at both the spinning and feeding stages, which indicates that Bom-PTSP interferes with PTTH-stimulated ecdysteroidogenesis.

Amino Acid Sequence↗

PubMed1995

An ecdysiostatin from flies.

A bioassay for compounds with ecdysiostatic activity ('ecdysiostatins') was developed in order to prove the existence of an ecdysiostatin in blowfly larvae. The factor eluted by HPLC like Neb-TMOF (trypsin modulating oostatic factor), a hexapeptide that inhibits ecdysone biosynthesis. The ecdysiostatic activity of Neb-TMOF is specific, related peptides were less active or inactive. TMOF inhibits ecdysone biosynthesis rather than its secretion. It increases the cAMP level of ring glands. Effectors that elevate the intracellular cAMP can mimic the inhibitory effect of the ecdysiostatin. This suggests that cAMP may control steroidogenesis in fly larvae by shutting ecdysone biosynthesis. Thus, the hexapeptide acts as a prothoracicostatic hormone (PTSH) that controls ecdysone biosynthesis.

Amino Acid Sequence↗

PubMed1995

Folliculostatins, gonadotropins and a model for control of growth in the grey fleshfly, Neobellieria (sarcophaga) bullata.

The sequences of two folliculostatic peptides of the fleshfly Neobellieria bullata have been determined recently. The first peptide (Neb-TMOF: H-NPTNLH-OH), originates from a 75 kDa precursor protein found in vitellogenic oocytes. The hexapeptide directly inhibits the synthesis of trypsin-like enzymes in the gut, and thus lowers the concentration of yolk polypeptides in the hemolymph. It also inhibits the biosynthesis of ecdysone in the larval ring gland. Therefore, it could also be named prothoracicostatic hormone (Neb-PTSH). The second peptide (Neb-colloostatin: H-SIV-PLGLPVPIGPIVVGPR-OH) acts on previtellogenic follicles and is a cleaved product of a collagen-like precursor molecule. Our results indicate that peptides that are cleaved from matrix proteins could act as growth-inhibiting factors. Gonadotropin releasing hormone (GnRH)-immunolike peptides were not identified, but progress is being made in the isolation and characterization of factors which stimulate cAMP production by the ovary. Using these results, a novel model of growth control in which matrix proteins play an important role as a potential source of growth regulators has been developed.

Amino Acid Sequence↗

PubMed1994

Inhibition of ecdysone biosynthesis in flies by a hexapeptide isolated from vitellogenic ovaries.

The only identified insect peptides known to be involved in controlling the biosynthesis of ecdysone, the steroid moulting hormone of arthropods, are the prothoracicotropic hormones (PTTH). These neuropeptides stimulate ecdysone biosynthesis. Recently, a hexapeptide (NPTNLH) with folliculostatic and trypsin modulating activity was isolated from vitellogenic ovaries of the fleshfly Neobellieria bullata. Here we report that the hexapeptide, when tested in vitro on the isolated ring gland of flies, inhibited ecdysone biosynthesis immediately and completely (EC50 = 5 nM). The hexapeptide is the first known factor with 'prothoracicostatic activity' and may form part of the endocrine system that controls ecdysone biosynthesis in vivo.

Animals↗

PubMedDate not supplied

Quantification of ecdysteroids by immunoassay: comparison of enzyme immunoassay and radioimmunoassay.

The performance of enzyme immunoassay (EIA) and radioimmunoassay (RIA) in the quantitative analysis of ecdysteroids was compared. The EIA was found to be at least equivalent to the RIA with respect to analytical range and sensitivity and to be more comfortable with respect to safety and time saving. When biological samples were analyzed by both assays a good correlation (r = 0.83) was found. Since the EIA has certain advantages over the RIA, we now recommend the use of the former assay for the quantification of ecdysteroids.

Animals↗