大阪大学 · Medicine
마사히토 이카와 교수의 연구실은 생식생물학과 유전자 조작 기술을 융합한 연구를 주도하고 있습니다. 특히 생애 초기 단계의 배아에서 유전자 발현을 비침습적으로 모니터링할 수 있는 GFP를 활용한 전신 전달형 레트로바이러스 벡터 기반 유전자 노크다운 기술과, 정자 운동 및 수정 과정에서 핵심적인 역할을 하는 단백질(예: ADAM3, PDILT)의 분자 기전을 규명하고 있습니다. 이는 생리적 수정 과정과 in vitro 수정 간의 차이를 밝혀내는 데 기여하며, 생식 능력 유지 및 유전자 기반 생식 기술 개발에 기여하고 있습니다.
표시된 성과는 수집된 데이터 기준으로 산출되며, 일부 차이가 있을 수 있습니다.
We describe the use of lentiviral vectors expressing small interfering RNAs (siRNAs) to knock down the expression of specific genes in vitro and in vivo. A lentiviral vector capable of generating siRNA specific for GFP after transduction of 293T-GFP cell lines showed no GFP fluorescence. Furthermore, no GFP-specific RNA could be detected. When eggs from GFP-positive transgenic mice were transduced with lentivirus-expressing siGFP virus, reduced fluorescence could be seen in blastocysts. More int
Mammalian fertilization comprises sperm migration through the female reproductive tract, biochemical and morphological changes to sperm, and sperm-egg interaction in the oviduct. Recent gene knockout approaches in mice have revealed that many factors previously considered important for fertilization are largely dispensable, or if they are essential, they have an unexpected function. These results indicate that what has been observed in in vitro fertilization (IVF) differs significantly from what
Non-invasive selection of transgenic mice was performed at the stage of preimplantation embryos. The morulae collected from wild female mated with hemizygous transgenic male expressing Aequorea victoria green fluorescent protein (GFP) under chicken beta-actin promoter could be classified as green or non-green under a fluorescent microscope. All the green embryos were shown to carry the transgene by PCR analysis. Taking advantage of the detection of GFP expression can be done non-invasively, the
A disintegrin and metalloproteinase 3 (ADAM3) is a sperm membrane protein critical for both sperm migration from the uterus into the oviduct and sperm primary binding to the zona pellucida (ZP). Here we show that the testis-specific protein disulfide isomerase homolog (PDILT) cooperates with the testis-specific calreticulin-like chaperone, calsperin (CALR3), in the endoplasmic reticulum and plays an indispensable role in the disulfide-bond formation and folding of ADAM3. Pdilt(-/-) mice were mal
