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evaluate <strong>the</strong> effect of single or combination of crude
extracts from Poria cocos <strong>and</strong> Dioscorea opposite on renal
advanced glycation end products (AGEs) formation in
pre‐diabetic rats. After induced with 20 mg/kg
strep<strong>to</strong>zo<strong>to</strong>cin, <strong>the</strong> blood sugar levels of rats remained
mimic prediabetes status (140‐200 mg/dL). Then, single
dose of Poria cocos crude extracts (0.14 g/kg/day) <strong>and</strong>
Dioscorea opposite crude extracts (0.35 g/kg/day),
combination of both, or vehicle were administered for 8
weeks. Blood <strong>and</strong> selected organ samples were collected
during <strong>the</strong> study. The results showed 8‐week
administration of single or combination of <strong>the</strong>se crude
extracts could significantly reduce <strong>the</strong> fasting blood
glucose level (p 0.05) <strong>and</strong> delay <strong>the</strong> progress <strong>to</strong> overt
diabetes. The levels of tumor necrosis fac<strong>to</strong>r‐α (TNF‐α)
<strong>and</strong> interleukin‐6 (IL‐6) concentrations in plasma <strong>and</strong>
liver were significantly decreased in administered
groups compared <strong>to</strong> control group (p 0.05). Such
founding are highly correlated with <strong>the</strong> thickness of
glomerular basement membrane. The
immunohis<strong>to</strong>chemistry stain showed that <strong>the</strong> expression
of AGEs <strong>and</strong> <strong>the</strong> recep<strong>to</strong>r for advanced glycation end
products (RAGE) in kidney mainly accumulated in
afferent arteriole <strong>and</strong> <strong>the</strong> proximal area of renal vessel.
These results suggest that administration of Poria cocos
or Dioscorea opposite crude extracts could exert an
anti‐inflamma<strong>to</strong>ry effect by reducing AGEs formation
<strong>and</strong> prevent <strong>the</strong> process of diabetes in pre‐diabetic rats.
Discussion on reduction treatment suitable
for allergenicity of Penaeus vannameimajor
allergen tropomyosin
Jiayi SUN, Xichang WANG, Yuan LIU <strong>and</strong> Ying LU
College of Food Science <strong>and</strong> Technology, Shanghai Ocean
University, Shanghai, China. Email: Tears123123@126.com
In this study, ultrasound(300 W, 3 min),
enzymolysis(35 °C, 10 min) <strong>and</strong> ultrasound(300 W, 3 min)
combining with enzymolysis(35 °C, 10 min) treatment
were individually used <strong>to</strong> reduce shrimp major allergen
tropomyosin (Tm). The reduction degree was evaluated
by Tricine‐SDS‐PAGE, Western blot <strong>and</strong> S<strong>and</strong>wich ELISA.
Based on <strong>the</strong> data, a protein b<strong>and</strong> with molecular weight
about 35 kDa was reduced remarkably after treated by
enzymolysis <strong>and</strong> ultrasound combining with enzymolysis.
Western blot data showed that <strong>the</strong> 35kDa protein was
shrimp allergen Tm. S<strong>and</strong>wich ELISA results appeared
that <strong>the</strong> Tm protein treated by enzymolysis with ficin <strong>and</strong>
alcalase lost <strong>the</strong> immunological activity. The amount of Tm
treated with ‐chymotrypsin <strong>and</strong> bromelian was
reduced, however, according <strong>to</strong> <strong>the</strong> s<strong>and</strong>wich ELISA, it
still showed weak immunological activity. Ultrasound
treatment showed <strong>the</strong> worst reduction effect. Enzyme
digestion sites analysis of every enzyme for Tm implied
that appropriate digestion temperature <strong>and</strong> <strong>the</strong> amount
of digestion sites were important for <strong>the</strong> reduction effect.
Their roles are necessary <strong>to</strong> pay attention when reducing
<strong>the</strong> allergenicity of shrimp allergen Tm.
Distribution <strong>and</strong> expression studies on
aquaporin­1 (AQP­1) <strong>and</strong> <strong>the</strong> cystic fibrosis
transmembrane regula<strong>to</strong>r (CFTR) in silver
sea bream
Norman YS WOO, Eddie E DEANE, James CY
LUK, Anna KY KWONG <strong>and</strong> Teresa WS YUEN
School of Life Sciences, The Chinese University of Hong Kong,
Shatin, NT, Hong Kong SAR, China. Email:
normanwoo@cuhk.edu.hk
Aquaporins have been implicated <strong>to</strong> play a role in water
transport in various osmoregula<strong>to</strong>ry epi<strong>the</strong>lia of teleosts.
Using immunolocalization pro<strong>to</strong>cols we studied <strong>the</strong>
spatial distribution of aquaporin‐1 (AQP1) in <strong>the</strong> gill,
intestine <strong>and</strong> kidney of silver sea bream (Sparus sarba)
that were acclimated <strong>to</strong> seawater (SW) or freshwater
(FW). In <strong>the</strong> gill, immunoreactivity of AQP1 was mainly
detected at <strong>the</strong> primary <strong>and</strong> secondary lamellae junctions
<strong>and</strong> found <strong>to</strong> co‐localize with Na + ‐K + ‐ATPase reactivity
mainly within <strong>the</strong> region of <strong>the</strong> chloride cells. For
intestine it was found that AQP1 was localized at <strong>the</strong>
basal side of villi epi<strong>the</strong>lial cells for both SW‐<strong>and</strong> FWacclimated
sea bream. However in SW‐acclimated fish,
AQP1 was observed <strong>to</strong> be scattered amongst <strong>the</strong>
intestinal goblet cells. In kidney, AQP1 immunoreactivity
was restricted <strong>to</strong> <strong>the</strong> apical membranes of some renal
tubular cells for both SW‐ <strong>and</strong> FW‐acclimated silver sea
bream. RT‐PCR analysis was used <strong>to</strong> measure AQP1
transcript abundance in salinity acclimated sea bream
<strong>and</strong> it was found that expression was highest in gill tissue
taken from fish that were acclimated <strong>to</strong> low salinity
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