A New Scalable Purification Procedure for Prostatic Secretory Protein (PSP94) from Human Seminal Plasma

Baijal-Gupta, Madhulika; Fraser, Jennifer E.; Clarke, Michael W.; Xuan, Jim W.; Finkelman, Malcolm

doi:10.1006/prep.1996.0128

Cited by 13 publications

(11 citation statements)

References 0 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…Prior to FFE separation, IGFBP-1 in AF was isolated using a salting out procedure (26) by adding solid ammonium sulfate (0 -75% saturation) to the clarified AF sample. The sample was then centrifuged at 13,000 rpm for 1 h (Beckman model J2-21 centrifuge, JA 20 rotor).…”

Section: Sample Preparation For Ffe Separationmentioning

confidence: 99%

Functional and Complementary Phosphorylation State Attributes of Human Insulin-like Growth Factor-Binding Protein-1 (IGFBP-1) Isoforms Resolved by Free Flow Electrophoresis

Nissum

Shehab²,

Sukop

et al. 2009

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

Fetal growth restriction (FGR) is a common disorder in119 . Our data demonstrate that phosphorylation at Ser 119 plays a significant role in modulating affinity of IGFBP-1 for IGF-I. In addition, an altered profile of IGFBP-1 phosphoisoforms was revealed between FGR and healthy pregnancies that may result from potential site-specific phosphorylation. This study provides a strong basis for use of this novel approach in establishing the linkage between phosphorylation of IGFBP-1 and FGR. This overall strategy will also be broadly applicable to other phosphoproteins with clinical and functional significance.

show abstract

Section: Sample Preparation For Ffe Separationmentioning

confidence: 99%

Functional and Complementary Phosphorylation State Attributes of Human Insulin-like Growth Factor-Binding Protein-1 (IGFBP-1) Isoforms Resolved by Free Flow Electrophoresis

Nissum

Shehab²,

Sukop

et al. 2009

Molecular & Cellular Proteomics

View full text Add to dashboard Cite

show abstract

“…PSP94 was purified to homogeneity from pooled human seminal plasma, using a three-step procedure [10]. Briefly, human seminal fluid obtained from the Fertility Clinic at University Hospital (London, Ontario, Canada) underwent three consecutive steps of purification: ammonium sulfate fractionation followed by a Macro-Prep S support (cation) flowthrough process and final Macro-Prep high Q support (anion exchange) chromatography, using twogradient elution [10].…”

Section: Preparation Of Psp94mentioning

confidence: 99%

Prostate secretory protein (PSP94) suppresses the growth of androgen-independent prostate cancer cell line (PC3) and xenografts by inducing apoptosis

Garde

Basrur

Li³

et al. 1999

Prostate

Self Cite

View full text Add to dashboard Cite

“…The slides were baked for 3-4 days at 45 C. Adjacent serial sections were used for IHC using rabbit polyclonal anti PSP94 (Baijal-Gupta et al 1996), raised against native PSP94 or PSP57 antiserum against a synthetic 41-mer peptide (Xuan et al 1995) or for ISH, as described below.…”

Section: Preparation Of Tissue Sectionsmentioning

confidence: 99%

“…PSP94, also known as microseminoprotein (MSP), an abundant human seminal plasma protein (Lilja & Abrahamsson 1988, Green et al 1990, Liang et al 1991, has been purified from human (Wright et al 1990, Baijal-Gupta et al 1996 and porcine (Fernlund et al 1994) seminal plasma. The protein has been detected in significantly reduced levels in other human tissues (Johansson et al 1984, Brar et al 1988, Lilja & Abrahamsson 1988, Ulvsback et al 1989, Weiber et al 1990, Teni et al 1992, Xuan et al 1995 and in mucous glands and various secretions (Weiber et al 1990).…”

Section: Introductionmentioning

confidence: 99%

Prostatic secretory protein (PSP94) expression in human female reproductive tissues, breast and in endometrial cancer cell lines

Baijal-Gupta¹,

Clarke²,

Finkelman³

et al. 2000

Journal of Endocrinology

View full text Add to dashboard Cite

PSP94 ( microseminoprotein,MSP) is one of the three major proteins secreted by the normal human prostate gland. Using reverse transcriptase polymerase chain reaction (RT-PCR) and Southern blotting, PSP94 transcripts were shown in human endometrium, myometrium, ovary, breast, placenta and in the human endometrial cancer cell lines KLE and AN3 CA. Primers used in these studies were specific for human prostate PSP94, and were derived from its flanking non-coding regions. The results were confirmed by sequence analysis of two independently derived clones from normal human breast tissues and the other two from KLE cells respectively. The sequences were identical with the coding sequence of human prostate PSP94 cDNA. Using RNA from the endometrial tissues, two different transcripts of 487 bp, equivalent to prostate PSP94 and 381 bp, corresponding to prostate PSP57, its alternately spliced form, were amplified by RT-PCR. Human ovary, breast, placenta and endometrial cancer cell lines (KLE, AN3 CA), however, showed only the full length, 487 bp, PSP94 transcript. We further demonstrated by in situ hybridization that PSP94 mRNA is expressed specifically in the glandular epithelial cells, and not in the stroma of both the human endometrial and breast tissues. Further, using image analysis of in situ hybridization data, the levels of PSP94 mRNA in the cycling endometrial tissues and in breast confirmed the differential levels of expression in the cycling endometrium (P<0·005). This study distinctly demonstrated significant expression of PSP94 mRNA in human uterine, breast and other female reproductive tissues as well in the endometrial cancer cell lines, suggesting that it may have a role in these tissues as a local autocrine paracrine factor.

show abstract

A New Scalable Purification Procedure for Prostatic Secretory Protein (PSP94) from Human Seminal Plasma

Cited by 13 publications

References 0 publications

Functional and Complementary Phosphorylation State Attributes of Human Insulin-like Growth Factor-Binding Protein-1 (IGFBP-1) Isoforms Resolved by Free Flow Electrophoresis

Functional and Complementary Phosphorylation State Attributes of Human Insulin-like Growth Factor-Binding Protein-1 (IGFBP-1) Isoforms Resolved by Free Flow Electrophoresis

Prostate secretory protein (PSP94) suppresses the growth of androgen-independent prostate cancer cell line (PC3) and xenografts by inducing apoptosis

Prostatic secretory protein (PSP94) expression in human female reproductive tissues, breast and in endometrial cancer cell lines

Contact Info

Product

Resources

About