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Gene Review:

TXNDC2 - thioredoxin domain containing 2 (spermatozoa)

Homo sapiens

Synonyms: SPTRX, SPTRX1, Spermatid-specific thioredoxin-1, Sptrx-1, Thioredoxin domain-containing protein 2

Miranda-Vizuete, A. et al., Jiménez, A. et al.

Miranda-Vizuete, Ljung, Damdimopoulos, Gustafsson, Oko, Pelto-Huikko, Spyrou,

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High impact information on TXNDC2

We report here the identification and characterization of a novel member of the thioredoxin family in humans, named Sptrx (sperm-specific trx), the first with a tissue-specific distribution, located exclusively in spermatozoa [1].
Immunostaining of human testis sections identified Sptrx protein in spermatids, while immunofluorescence and immunogold electron microscopy analysis demonstrated Sptrx localization in the cytoplasmic droplet of ejaculated sperm [1].
Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa [1].
Northern analysis and in situ hybridization shows that Sptrx mRNA is only expressed in human testis, specifically in round and elongating spermatids [1].
The identification of Sptrx with an expression pattern restricted to the postmeiotic phase of spermatogenesis, when the sperm tail is organized, suggests that Sptrx might be an important factor in regulating critical steps of human spermiogenesis [1].

Biological context of TXNDC2

Sptrx open reading frame encodes for a protein of 486 amino acids composed of two clear domains: an N-terminal domain consisting of 23 highly conserved repetitions of a 15-residue motif and a C-terminal domain typical of thioredoxins [1].

Associations of TXNDC2 with chemical compounds

Functionally, Sptrx-1 behaves as an oxidant in vitro when using selenite, but not oxidized glutathione, as electron acceptor [2].

Other interactions of TXNDC2

Analysis of circular dichroism spectra of fragments 1-360 and 361-469 and comparison to spectra of full-length Sptrx-1 supports a two-domain organization with a largely unstructured N-terminal domain and a folded thioredoxin-like C-terminal domain [2].

Analytical, diagnostic and therapeutic context of TXNDC2

In gel filtration chromatography human Sptrx-1 eluates as a 400 kDa protein consistent with either an oligomeric form, not maintained by intermolecular disulfide bonding, and/or a highly asymmetrical structure [2].

References

Characterization of Sptrx, a novel member of the thioredoxin family specifically expressed in human spermatozoa. Miranda-Vizuete, A., Ljung, J., Damdimopoulos, A.E., Gustafsson, J.A., Oko, R., Pelto-Huikko, M., Spyrou, G. J. Biol. Chem. (2001) [Pubmed]
Human spermatid-specific thioredoxin-1 (Sptrx-1) is a two-domain protein with oxidizing activity. Jiménez, A., Johansson, C., Ljung, J., Sagemark, J., Berndt, K.D., Ren, B., Tibbelin, G., Ladenstein, R., Kieselbach, T., Holmgren, A., Gustafsson, J.A., Miranda-Vizuete, A. FEBS Lett. (2002) [Pubmed]

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