Disease relevance of PTGDS

• Lipocalin-type prostaglandin D synthase in milk: a new biomarker for bovine mastitis [1].

High impact information on PTGDS

• The accumulation of PGDS, a KSPG that does not interact with collagen, was not affected by ascorbate [2].
• However, compared with the keratocytes, the fibroblasts possessed no aldehyde dehydrogenase and synthesized significantly higher levels of decorin and significantly lower levels of prostaglandin D synthase (PGDS) and keratan sulfate [3].
• OBJECTIVE : We examined the role of prostaglandin D2 (PGD2) in the formation of plasminogen activator inhibitor (PAI)-1 following interleukin-1beta (IL-1) stimulation in bovine endothelial cells (EC) transfected with lipocaline-type PGD2 synthase (L-PGDS) genes [4].
• Additionally, these cells produce PGDS, a known retinoid transporter, as a KSPG [5].
• PGDS isolated from corneal extracts was not keratanase sensitive but was susceptible to endo-beta-galactosidase, suggesting that it contains unsulfated polylactosamine chains in native tissue and is therefore present as a glycoprotein [5].

Biological context of PTGDS

• Mapping the prostaglandin-D synthase gene (PTGDS ) to bovine chromosome 1 [6].
• Expression of lipocalin-type prostaglandin D synthase was not uniform in the seven epididymal subsegments, suggesting a possible role in sperm maturation [7].

Anatomical context of PTGDS

• Previously, we identified a 26-kDa fertility-associated protein in bull seminal plasma as lipocalin-type prostaglandin D synthase [7].
• Lipocalin-type prostaglandin D synthase was strikingly localized in the caput epididymidis, while moderate to weak staining was observed in the remainder of the epididymis [7].
• Immunocytochemical localization of lipocalin-type prostaglandin D synthase in the bull testis and epididymis and on ejaculated sperm [7].
• Using fluorescence microscopy, we also localized lipocalin-type prostaglandin D synthase to the apical ridge of the acrosome on ejaculated sperm [7].

Associations of PTGDS with chemical compounds

• Prostaglandin (PG) D2 represented approximately 10% of the PGs produced in the lumen, irrespective of the presence or absence of luminal PGDS, suggesting that this protein is not involved in PGD2 biosynthesis [8].
• The enzymatic activity of PGDS was estimated in the ram by in vitro incubation of epididymal-isolated tubules with radioactive arachidonic acid [8].
• In the ram and stallion, cDNA and deduced protein sequences of PGDS were obtained by reverse transcription-polymerase chain reaction and showed that PGDS possessed the sequences involved in the three-dimensional folding characteristic of the lipocalin family and a cysteine at position 65 that is involved in the enzymatic activity [8].
• It is likely that PGDS, which has a structure similar to that of lipocalin, functions as a lipophilic carrier protein, because we have shown that epididymal PGDS binds retinoic acid and testosterone in vitro [8].
• Subsequent culture of the fibroblasts in serum-free medium did not restore aldehyde dehydrogenase to keratocyte levels but did restore the cell morphology to a more dendritic appearance and returned the synthesis of decorin, PGDS, and keratan sulfate to keratocyte levels [3].

Analytical, diagnostic and therapeutic context of PTGDS

• Identity was confirmed by Western blot analysis using antisera to recombinant PGDS [5].

References