High impact information on Txndc5

• Using cDNA subtraction we have identified a previously unknown cDNA, termed plasma cell thioredoxin-related protein (PC-TRP), which was overexpressed in plasma cells in vitro [1].
• Identification of a novel thioredoxin-related protein, PC-TRP, which is preferentially expressed in plasma cells [1].
• The full-length 2636-bp PC-TRP cDNA contained an open reading frame coding for 417 amino acids [1].
• The cDNA sequence was mapped to a region on mouse chromosome 13 and the PC-TRP gene consists of ten exons distributed over a 28-kb region [1].
• Immunohistological analysis revealed that PC-TRP was expressed at high levels in all plasma cells isolated from bone marrow or lamina propria, irrespective of their Ig isotype [1].

Anatomical context of Txndc5

• A more detailed analysis revealed that PC-TRP was expressed at a high level in plasma cells, both at the mRNA and protein level, while present at very low levels in all other cells and tissues examined [1].
• ERp19 and ERp46, new members of the thioredoxin family of endoplasmic reticulum proteins [2].

Associations of Txndc5 with chemical compounds

• Two newly discovered ER luminal proteins, designated ERp19 and ERp46, are related to protein disulphide isomerase [2].
• As a result, we were able to identify alternative splice variants of Thioredoxin domain containing 5, Interleukin1beta, Interleukin 1 family 6 and glutamine-rich hypothetical protein [3].

Analytical, diagnostic and therapeutic context of Txndc5

• Western and Northern blot analyses revealed that both ERp19 and ERp46 and their respective mRNAs are highly expressed in the liver as compared with other tissues [2].

References