Faculty of Science - Mahidol University

Mahidol University Annual Research Abstracts, Vol. 33 275
HIGH DOSE PSEUDOEPHEDRINE ADMINIS-
TRATION CAN INDUCE APOPTOSIS IN
SEMINIFEROUS TUBULES ON MALE RATS
S. Nudmamud-Thanoi, Thanoi, S. and Sobhon, P.
(NO. 706)
Department of Anatomy, Faculty of Science, Mahidol University,
Bangkok, Thailand.
Objective : The present study is aimed to investigate the
effects of pseudoephedrine, a sympathomimetic drug, on the
reproductive system for understanding the mechanisms and
increasing the knowledge of using the drug.
Materials and Methods : Sprague Dawley male rats (250-
280g) were divided into 3 groups as acute, chronic, and control
groups with 10 animals each. To examine an acute, effect of
pseudoephedrine, amimals were administered intragastically at the
dose of 120mg/kg. The chronic effect was examined by treated
pseudoephedrine intragastically at the dose of 80 mg/kg, once daily
for 15 days. The animals in control group were administered
intragastically with vehicle. After treatment, animals were sacrificed
and apoptotic activites within the seminiferous tubules were studied
using the TUNEL (TdT-mediated dUTP Nick End Labeling) assay.
Results : The present study showed that acute
administration of high dose pseudoephedrine can induce apoptotic
activites within seminiferous tubules. In contrast, animals treated
with lower dose of pseudophedrine chronically showed a small
amount of apoptotic cells inside the seminiferous tubules.
Qualitatively, the apoptotic actiivites were involved in every stage
of sperm development inside the seminiferous tubules especially
the spermatogonia. These results indicate that acute administration
of high dose pseudoephedrine could induce apoptosis within the
seminiferous tubules of male rats. Apoptosis that caused by
pseudoephedrine may be due to a sudden increased adrenergic
vasoconstriction after a single high dose administration.
(Poster presentation at the 28 th Annual Meeting of the Society of
Anatomy. April, 2005. Ubonratchatani, Thailand.)
CHANGES IN EPIDERMAL STRUCTURE AND
PROTEIN EXPRESSION DURING MOLTING
CYCLE OF THE BLACK TIGER SHRIMP
(Penaeus monodon) (NO. 707)
Promwikorn W., Khunthongpan S., Kirirat P. Intasaro, P.
Thaweethasewee P. and Withyachmunarnkul B.
Department of Anatomy, Faculty of Science, Mahidol University,
Bangkok, Thailand
Background : In shrimp, the cycle of post-embryonic
growth and development is characterized by a unique molting
process. Epidermis plays an important role in the molting process.
Although it has long been studied over seventy years, the regulatory
mechanism of the molting cycle of the black tiger shrimp (Penaeus
monodon), which is well-known as an important agricultural export
product of Thailand, is far from attention. We therefore have been
investigating regulatory mechanism of the molting cycle in the black
tiger shrimp.
Objective: To investgate changes in epidermal structure
and protein expression during molting cycle of the black tiger shrimp
by histochemistry and two dimension gel electrophoresis.
Materials and methods: Healthy black tiger shrimps
(Penaeus monodon), 10-20 g body-weight, were transferred from
natural farms to culture in aquariums at Dept. Anatomy, PSU., where
they were fed three times a day with commercial food. Eachshrimp
were examined for molting stages at least once a day. Epidermal
and sub-epidermis morphology of each molting stage were
histologically investigates by staining with Masson’s trichromes,
and periodic acid Schiff’s reagents, respectively. Epidermal protein
expression was analysed by two dimension gel electrophoresis and
silver stained.
Results and discussions: It was found that the height of
epidermis increases during the period of mid-premolt throughout
early-postmolt stages. Glycoprotein deposition in sub-epidermis
region is also increase corresponding to the above period.
(Poster presentation at the 28 th Annual Meeting of the Society of
Anatomy. April, 2005. Ubonratchatani, Thailand.)
STRUCTURE AND PROTEIN PROFILES OF THE
ANTENNAL GLAND OF THE BLACK TIGER
SHRIMP (Penaeus monodon). (NO. 708)
Asuvapongpatana S, Wongprasert K, Buranajitpirom D,
Namwong W, Weerchatyanukul W., Apisawetakan S.,
Sritunyalucksana K, Withayachumnarnkul B.
Department of Anatomy, Faculty of Science, Mahidol University,
Bangkok, Thailand.
Objective : To study the structure and protein profiles of
the antennal gland of the black tiger shrimp (Penaeus monodon)
Materials and Methods : Juvenile shrimp, 20-25 g, were
anesthetized on ice. Their anternnal glands were removed and divided
into 2 groups. The first group was for studying under light
microscopy, and sections were for studying the protein profile. The
antennal glands were homogenized with lysis buffer (20 mM Tris,
pH 7.4 and 100 mM NaCl). The homogenate was centrifuged at
800xg, at 4 °c for 20 min, to pellet the muclei. The supernate was
centrifuged at 100,000xg for 1 h, and the antennal gland lysate was
collected. The pellet was incubated on ice with detergent (NaCl/Pi,
1% triton X-100, 2mm EDTA, 1mM PMSF) for 30 min to solubileze
the muclear membrane. The membrane solution was centrifuged at
100,000xg, at 4 °c for 1 h, and the supernate (solubilized membrane
lysate) was collected. The antennal gland lysate and solubilized
membrane lysate were run on 12.5% SDSPAGE followed by staining
with Coomassie blue or silver.
Results : The antennal gland of P. monodon comprised 3
parts: coelomosac, labyrinth and bladder. The coelomosac is
surrounded by the lavyrinth and are supplied by the antennal artery.
The coelomosac cells were similar to podocytes of mammalian
kidney, having a large nucleus with abundant vacuoles in the
cytoplasm. The labyrinth cell is cuboidal with concentric nycleus
and brush border at the apical end of the cell. The labyrinth cells
might be divided into two stages: the secretory and non secretory
secretory stages. In the secretory stage, the cell is cuboid with the
nucleus closed to the apical surface and the brush border is slough
off. In the non-secretory stage, the cuboidal cell is covered with
brush border and the nucleus was at the center of the cell. The
proteins of the antennal gland were distributed between 10-150 kDa,
with main components were proteins at molecular weights of 53,
40, 30, 22 kDa.
(Poster presentation at the 28 th Annual Meeting of the Society of
Anatomy. April, 2005. Ubonratchatani, Thailand.)
PDF created with FinePrint pdfFactory Pro trial version http://www.pdffactory.com