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123 results on '"Chen, Yee Hsiung"'

38. Demonstration of a Glycoprotein Derived From the Ceacam10Gene in Mouse Seminal Vesicle Secretions1

Author

Li, Sheng-Hsiang, Lee, Robert Kuo-Kuang, Hsiao, Ya-Ling, and Chen, Yee-Hsiung

Abstract

CEACAM10 was purified from mouse seminal vesicle secretions by a series of purification steps that included ion exchange chromatography on a DEAE-Sephacel column and ion exchange high-performance liquid chromatography on a sulfopropyl column. It was shown to be a 36-kDa glycoprotein with an N-linked carbohydrate moiety. The circular dichromoism spectrum of CEACAM10 in 50 mM phosphate buffer at pH 7.4 appeared as one negative band arising from the β form at 217 nm. CEACAM10 was expressed predominantly in seminal vesicles of adult mice. Both CEACAM10 and its mRNA were demonstrated on the luminal epithelium of the mucosal folds in the seminal vesicle. The amount of Ceacam10mRNA in the seminal vesicle was correlated with the stage of animal maturation. Castration of adult mice resulted in cessation of Ceacam10expression, while treatment of castrated mice with testosterone propionate in corn oil restored Ceacam10expression in the seminal vesicle. During the entire course of pregnancy, Ceacam10might be silent in the embryo. A cytochemical study illustrated the presence of the CEACAM10 binding region on the entire surface of mouse sperm. CEACAM10-sperm binding greatly enhanced sperm motility in vitro.

Published
2005
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39. Developmental Profile of a Caltrin-Like Protease Inhibitor, P12, in Mouse Seminal Vesicle and Characterization of Its Binding Sites on Sperm Surface1

Author

Chen, Li-Yuan, Lin, Yen-Hui, Lai, Ming-Long, and Chen, Yee-Hsiung

Abstract

We examined the developmental profile of a kazal-type trypsin inhibitor (P12) of Mr6126 in mouse seminal vesicle, characterized its binding sites on the surface of sperm, and assessed its effect on Ca2+uptake by spermatozoa. Among the genital tracts of adult mice, P12 was found only in the male accessory glands including seminal vesicle, coagulating gland, and prostate. It was immunolocalized on the luminal epithelium of the primary and secondary folds in both the seminal vesicle and coagulating gland, and on the folds projecting into the lumen of the glandular alveolus in the prostate. The protein and its RNA message in seminal vesicle did not appear in the prepubertal period, but expression coincided with maturation. Castration of adult mice resulted in cessation of P12 expression. Treatment of the castrated mice with testosterone propionate in corn oil restored the protein expression in the seminal vesicle. Spermatozoa collected from caudal epididymis were devoid of P12. Cytochemical study illustrated a P12-binding region on the anterior acrosomes of cells preincubated with P12. Analysis of equilibrium data from the binding assay using 125I-P12 with a Scatchard plot showed a single type of P12-binding sites on sperm, with an apparent dissociation constant of 70.15 ± 5.25 nM and the capacity of 1.49 ± 0.06 × 106binding sites/cell. The protein could serve as a calcium transport inhibitor to suppress a great extent of Ca2+uptake by spermatozoa. The immunohistochemical staining patterns of testis revealed that the P12-binding sites appeared on postmeiotic cells such as spermatids and spermatozoa, but were absent in Leydig cells, Sertoli cells, spermatogonia, and spermatocytes in seminiferous tubules.

Published
1998
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40. Diversity of the ß-Bungarotoxin Family

Author

Chu, Chen-Chung, Chiang, Shang-Wen, Liau, Ming-Yi, and Chen, Yee-Hsiung

Abstract

We had applied an h.p.l.c. method to make an effective resolution of the isotoxins (P3-P18) of ß-bungarotoxin family in one batch of Formosan krait (Bungarus multicinctus) venom from commercial source. The functional characteristics of P4-5, P8-9, P11, P13 and P15-18 were compared. They showed a great difference in their ability to hydrolyze phospholipid and to cause neurotoxic effect. P11 had the phospholipase activity of 373 unit/mg of protein and its LD50 was 0.012 mg/g body weight of mice. P4 and P5 showed 18 and 34% of the phospholipase activity of P11, and the other isotoxins had the enzyme activity comparable to that of P11. The lethal potency based on the LD50 values was in the order P15-18>P11>P9>P8>P5>P4. The LD50 of P4 was about 150 or 1100 times as large as that of LD50 of P11 or P16. We applied also our h.p.l.c. method to examine the distribution of ß-bungarotoxin in two batches of Formosan krait venom collected separately from south China and Taiwan. The h.p.l.c. pattern of the isotoxins in Taiwan krait venom differed remarkably from that in the south China krait venom. At least 5 isotoxins were identified in Taiwan krait venom. They were distinct from more than 11 isotoxins identified in south China krait venom. Apparently, ß-bungarotoxins in Formosan krait venom can show a great deal of geographical variation.

Published
1996
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