NCBI Summary:
The protein encoded by this gene is a glycoprotein, belonging to the pentraxin family of proteins, which has a characteristic pentameric organization. These family members have considerable sequence homology which is thought to be the result of gene duplication. The binding of the encoded protein to proteins in the pathological amyloid cross-beta fold suggests its possible role as a chaperone. This protein is also thought to control the degradation of chromatin. It has been demonstrated that this protein binds to apoptotic cells at an early stage, which raises the possibility that it is involved in dealing with apoptotic cells in vivo. [provided by RefSeq]
General function
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Cellular localization
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Ovarian function
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Identification of differentially expressed proteins in the ovaries of menopausal women. Zhang LQ 2014 et al.
PURPOSE
This study investigated proteins differentially expressed in the ovaries of menopausal women in comparison to childbearing women.
METHODS
Differential protein expression was screened by difference gel electrophoresis and 2-D SDS-PAGE. Four differentially expressed proteins were excised manually, identified by mass spectrometry and confirmed by immunoblot and immunohistochemistry.
RESULTS
The four proteins were identified as serum amyloid P, heat shock protein 27, Glyoxalase I and Ubiquitin carboxy-terminal hydrolase. Serum amyloid P expression was significantly up-regulated in the ovaries of menopausal women by immunoblot analysis (p<0.05), Glyoxalase I and Ubiquitin carboxy-terminal hydrolase displayed an altered expression pattern, with higher expression in the atretic follicles of menopausal women. Weak Glyoxalase I and Ubiquitin carboxy-terminal hydrolase were observed in the granulosa and theca cells of the follicles of childbearing women. Heat shock protein 27 and serum amyloid P were clearly observed in the atretic follicles of menopausal women, while their expression was restricted to the theca cells and cytoplasm of primordial follicles in the ovaries of childbearing women. All four proteins were predominantly expressed in the atretic follicles of menopausal women.
CONCLUSIONS
These data suggest that the identified proteins may play a role in the regulation of follicle atresia in menopausal women, although their functions and mechanism warrant further investigation.
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Expression regulated by
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Ovarian localization
, Follicular Fluid
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Proteome mining of human follicular fluid reveals a crutial role of complement cascade and key biological pathways in women undergoing in vitro fertilisation. Jarkovska K et al. In vitro fertilisation (IVF) is fraught with problems and currently proteomics approaches are being tried out to examine the microenvironment of the follicle in order to assess biological and immunological parameters that may affect its development. Additionaly, better understanding of reproductive process may help increase IVF birth rate per embryo transfer and at the same time avoid spontaneous miscarriages or life threatening conditions such as ovarian hyperstimulation syndrom. The primary aim of this study was to search for specific differences in protein composition of human follicular fluid (HFF) and plasma in order to identify proteins that accumulate or are absent in HFF. Depletion of abundant proteins combined with multi-dimensional protein fractionation allowed the study of middle and lower abundant proteins. Paired comparison study examining HFF with plasma/serum from women undergoing successful IVF revealed important differences in the protein composition which may improve our knowledge of the follicular microenvironment and its biological role. This study showed involvement of innate immune function of complement cascade in HFF. Complement inhibition and the presence of C-terminal fragment of perlecan suggested possible links to angiogenesis which is a vital process in folliculogenesis and placental development. Differences in proteins associated with blood coagulation were also found in the follicular milieu. Several specific proteins were observed, many of which have not yet been associated with follicle/oocyte maturation. These proteins together with their regulatory pathways may play a vital role in the reproductive process. Serum amyloid P componet is 2.6 fold higher in plasma than FF.