The University of Osaka · Biochemistry, Genetics and Molecular Biology
칸아 요시카츠 교수의 연구실은 신경전달물질인 글루타메이트의 신호 전달 기능을 조절하는 수송체, 특히 글루타메이트 수송체와 중성아미노산 수송체(LAT1)의 분자 기전을 중심으로 연구를 진행하고 있습니다. 신경세포와 지지세포 간의 신호 조절 메커니즘을 밝혀내며 뇌의 신호 전달 균형과 신경독성 방어 기전을 규명하고자 합니다. 특히, 신경전달물질의 빠른 제거와 세포막 수송체의 이온 의존성 기전에 초점을 맞추고 있습니다.
Figures are computed from collected data and may differ slightly.
A cDNA was isolated from rat C6 glioma cells by expression cloning which encodes a novel Na+-independent neutral amino acid transporter designated LAT1. For functional expression in Xenopus oocytes, LAT1 required the heavy chain of 4F2 cell surface antigen (CD98), a type II membrane glycoprotein. When co-expressed with 4F2 heavy chain, LAT1 transported neutral amino acids with branched or aromatic side chains and did not accept basic amino acids or acidic amino acids. The transport via LAT1 was
An essential component of the transmission process at glutamatergic synapses is the removal of glutamate from the synaptic cleft. This is achieved by powerful transport systems which have a high affinity for glutamate and exhibit a novel coupling to inorganic ions. Transporters situated on presynaptic termini sequester glutamate directly from the synaptic cleft. In concert, transporters situated on glial cells maintain a low extracellular glutamate concentration, thereby establishing a diffusion
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