ライフサイエンスコーパス: 4F2hc

1 4F2hc increases the stability of the light subunit LAT2

2 n obtained by co-expression of b(0, +)AT and 4F2hc or b(0,+)AT and rBAT in human retinal pigment epit

3 in the kidney is identical for b(0,+)AT and 4F2hc.

4 is different from that of b(0,+)AT mRNA and 4F2hc mRNA, but there are regions in the kidney where b(

5 increases in the levels of mRNAs for xCT and 4F2hc and in corresponding protein levels.

6 The expression pattern of xCT and 4F2hc in the mouse retina was analyzed by immunofluoresc

7 mRNA levels for xCT and 4F2hc, the two subunits of system xc-, were monitored by

8 that interfacial PE binding is regulated by 4F2hc-R183 and is critical for regulation of palmitoylat

9 fication of the LAT1 with its chaperon CD98 (4F2hc,SLC3A2) and that this stabilised complex retained

10 d heterodimer with CD98 heavy chain (CD98hc, 4F2hc or SLC3A2), but the mechanism of assembly and amin

11 These cells express the heavy chain 4F2hc as evidenced from RT-PCR analysis.

12 (-) (the light chain xCT and the heavy chain 4F2hc) as is evident from functional and molecular studi

13 (b(0, +)AT) interacts with 4F2 heavy chain (4F2hc) as well as with the protein related to b(0,+) ami

14 , when coexpressed with the 4F2 heavy chain (4F2hc) in mammalian cells, induces a b(0,+)-like amino a

15 d with bovine BBB LAT1 mRNA and the mRNA for 4F2hc, which encodes the heavy chain of the heterodimer.

16 to the other type II membrane glycoprotein, 4F2hc (4F2 heavy chain).

17 the light chain with the heavy chain (human 4F2hc) in HeLa cells.

18 d single-particle analysis of purified human 4F2hc/L-type amino acid transporter 2 (LAT2) heterodimer

19 n increase in xCT mRNA but with no change in 4F2hc mRNA.

20 vide evidence of super-dimer formation (LAT1-4F2hc)(2).

21 ther validate the dynamic assemblies of LAT1-4F2hc on plasma membrane and in the lysosome.

22 The LAT1-4F2hc complex (SLC7A5-SLC3A2) facilitates uptake of esse

23 with regulation and localisation of the LAT1-4F2hc super-dimer.

24 5, which encode the heterodimeric CD98 (LAT1/4F2hc) amino acid transporter and regulate the intracell

25 The system L LAT1/4F2hc amino acid transporter was examined through uptake

26 nts, reveal that the extracellular domain of 4F2hc interacts with LAT2, almost completely covering th

27 Moreover, the extracellular domain of 4F2hc suffices to stabilize solubilized LAT2.

28 th no detectable change in the expression of 4F2hc.

29 The interaction of 4F2hc with LAT2 gives insights into the structural bases

30 The "rBAT/4F2hc family" of proteins induce both neutral and cation

31 SLC3A2 (4F2hc, CD98) plays a role as a disulfide-linked adaptor

32 SLC7A11 (xCT), together with SLC3A2 (4F2hc), encodes the heterodimeric amino acid transport s

33 The 4F2hc x b(0,+)AT complex has higher substrate affinity t

34 The 4F2hc/4F2-lc6 complex-mediated transport process is Na(+

35 higher than that of transcripts such as the 4F2hc antigen, actin, or the Glut1 glucose transporter.

36 Even though both the 4F2hc x b(0,+)AT complex and the rBAT x b(0,+)AT complex

37 ics of the transport process mediated by the 4F2hc/4F2-lc6 complex and the expression pattern of 4F2-

38 H, and modulated by complex N-glycans on the 4F2hc subunit.

39 ps with rBAT mRNA expression as well as with 4F2hc mRNA expression.

40 The ability to interact with 4F2hc and rBAT is demonstrable with mouse b(0,+)AT as we

41 essed in COS-7 cells with rBAT, but not with 4F2hc, BAT1 exhibited a Na(+)-independent transport of c

42 Coexpression of human xCT with 4F2hc in HeLa cells leads to the induction of cystine an