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체외수정 환자에서의 난포액 및 혈중 혈관 내피 성장인자
박성재 ( Sung Jae Park ),기경도 ( Kyung Do Ki ),이효원 ( Hyo Won Lee ),이보연 ( Bo Yon Lee ),이선경 ( Seon Kyung Lee ),허주엽 ( Chu Yeop Huh ),김승보 ( Seung Bo Kim ) 대한산부인과학회 2006 Obstetrics & Gynecology Science Vol.49 No.9
목적: 난포생성에서 황체기능의 작용까지 여성생식과정의 여러 단계가 혈관생성에 관련되어 있다. 본 연구는 체외수정을 시행하는 환자에서 혈액 및 난포액내 VEGF (Vascular endothelial growth factor) 농도를 측정하고자 하였다. 연구 방법: 2003년 8월부터 2005년 7월까지 본원 불임클리닉에서 체외수정시술을 받은 29명의 환자를 대상으로 하였으며 과배란 유도는 GnRH agonist를 이용한 단기투여법 (short protocol)을 사용하였다. 난자 채취시에 혈액과 난포액을 채취하여 -60℃에서 보관하였다가 효소면역 정량법 (ELISA, enzyme-linked immunosorbent assay)으로 혈청과 난포액의 VEGF 농도를 측정하였다. 결과: 총 29명의 환자중 10명의 환자에서 임신이 되었다 (34.5%). 난포액내 VEGF 농도와 혈청내 VEGF 농도 및 연령 사이에는 상관계수 0.428로 유의한 양의 상관관계를 보였고, 난포액내 VEGF 농도와 난포수 및 채취된 난자수 사이에는 상관계수 -0.493로 유의한 음의 상관관계가 나타냈다. 하지만 난포액내 VEGF 농도와 혈청내 VEGF 농도는 상관관계를 보이지 않았다. 대상 여성 중 임신군과 비임신군을 비교하였을 때 난포액내 VEGF 농도는 비임신군에서 1468.38±727.33으로 임신군의 676.48±542.07에 비해 유의하게 높게 나타났다. 결론: 본 연구의 결과를 바탕으로 황체기에서의 호르몬 생성부전이나 난포액내 부적절한 환경으로 인하여 상승된 VEGF의 농도가 체외수정 (IVF-ET)의 결과와 연관되어 있는 것으로 사료된다. Objective: Several aspects of female reproduction, from folliculogenesis to corpus luteum function, are related to angiogenesis. The purpose of this study is to measure the concentrations of vascular endothelial growth factor (VEGF) in follicular fluid and serum in patients during In Vitro Fertilization - Embryo Transfer (IVF-ET) cycles. Methods: In our prospective study, twenty-nine patients who underwent in vitro fertilization by GnRH agonist short protocol were assessed at the our infertility clinic from Aug. 2003 to July 2005. Serum VEGF and follicular fluid VEGF levels were measured in all patients at the time of oocytes retrieval. The assay technique used in this study was ELISA for serum and follicular fluid VEGF. Results: Of 29 cycles, 10 cycles were pregnant (34.5%). A positive correlation existed for follicular fluid VEGF and chronologic age (r=0.428, p-value=0.021). Follicular fluid VEGF concentration showed an inverse relationship with the total number of oocytes retrieved and follicles (r=-0.493, p-value=0.007; r=-0.474, p-value=0.009). But there was no statistically significant relationship between follicular fluid VEGF concentration and serum VEGF concentration (ρ=0.347). Follicular fluid VEGF concentration was significantly higher in the non-pregnant group (1468.38±727.33 pg/mL) compared to the pregnant group (676.48±542.07 pg/mL) (p-value=0.003). Conclusion: Our data provide some of the evidences that elevated VEGF concentrations in the follicular fluid are associated with poor conception rates in the IVF-ET cycles.
Antimicrobial Activity of a Honeybee (Apis cerana) Venom Kazal-Type Serine Protease Inhibitor
Bo Yeon Kim,Kwang Sik Lee,Feng Ming Zou,Hu Wan,Yong Soo Choi,Hyung Joo Yoon,Hyung Wook Kwon,Yeon Ho Je,Byung Rae Jin 한국응용곤충학회 2013 한국응용곤충학회 학술대회논문집 Vol.2013 No.10
Insect-derived Kazal-type serine protease inhibitors exhibit thrombin, elastase, plasmin, proteinase K, or subtilisin A inhibition activity, but so far, no functional roles for bee-derived Kazal-type serine protease inhibitors have been identified. In this study, a bee (Apis cerana) venom Kazal-type serine protease inhibitor (AcKTSPI) that acts as a microbial serine protease inhibitor was identified. AcKTSPI contained a single Kazal domain that displayed six conserved cysteine residues and a P1 threonine residue. AcKTSPI was expressed in the venom gland and was present as a 10-kDa peptide in bee venom. Recombinant AcKTSPI Kazal domain (AcKTSPI-Kd) expressed in baculovirus-infected insect cells demonstrated inhibitory activity against subtilisin A (Ki 67.03 nM) and proteinase K (Ki 91.53 nM), but not against α-chymotrypsin or typsin, which implies a role for AcKTSPI as a microbial serine protease inhibitor. However, AcKTSPI-Kd exhibited no detectable inhibitory effects on factor Xa, thrombin, tissue plasminogen activator, or elastase. Additionally, AcKTSPI-Kd bound directly to Bacillus subtilis, B. thuringiensis, Beauveria bassiana, and Fusarium graminearum but not to Escherichia coli. Consistent with these findings, AcKTSPI-Kd showed antibacterial activity against Gram-positive bacteria and antifungal activity against both plant-pathogenic and entomopathogenic fungi. These findings constitute molecular evidence that AcKTSPI acts as an inhibitor of microbial serine proteases. This paper provides a novel view of the antimicrobial functions of a bee venom Kazal-type serine protease inhibitor.
Lee, Seung-Jae,Kim, Yon-Suk,Kim, Seong-Eun,Kim, Eun-Kyung,Hwang, Jin-Woo,Park, Tae-Kyu,Kim, Bo Kyung,Moon, Sang-Ho,Jeon, Byong-Tae,Jeon, You-Jin,Ahn, Chang-Bum,Je, Jae-Young,Park, Pyo-Jam American Chemical Society 2012 Journal of agricultural and food chemistry Vol.60 No.40
<P>An angiotensin I-converting enzyme (ACE) inhibitory peptide was isolated and identified from hydrolysates of duck skin byproducts. Duck skin byproducts were hydrolyzed using nine proteases (Alcalase, Collagenase, Flavourzyme, Neutrase, papain, pepsin, Protamex, trypsin, and α-chymotrypsin) to produce an antihypertensive peptide. Of the various hydrolysates produced, the α-chymotrypsin hydrolysate exhibited the highest ACE inhibitory activity. The hydrolysate was purified using fast protein liquid chromatography (FPLC) and high-performance liquid chromatography (HPLC). The amino acid sequence of the ACE inhibitory peptide was identified as a hexapeptide Trp-Tyr-Pro-Ala-Ala-Pro, with a molecular weight of 693.90 Da. The peptide had an IC<SUB>50</SUB> value of 137 μM, and the inhibitory pattern of the purified ACE inhibitor from duck skin byproducts was determined to be competitive by Lineweaver–Burk plots. In addition, the peptide was synthesized and the ACE inhibitory activity was verified in vivo. Spontaneously hypertensive rats (SHR) exhibited significantly decreased blood pressure and heart rate after peptide injection. Taken together, the results suggest that Trp-Tyr-Pro-Ala-Ala-Pro may be useful as a new antihypertensive agent.</P><P><B>Graphic Abstract</B> <IMG SRC='http://pubs.acs.org/appl/literatum/publisher/achs/journals/content/jafcau/2012/jafcau.2012.60.issue-40/jf3023172/production/images/medium/jf-2012-023172_0009.gif'></P>