2025
DSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress
Alim S, Cheppali S, Pawar S, Swamy M. DSP-1, the major fibronectin type-II protein of donkey seminal plasma is a small heat-shock protein and exhibits chaperone-like activity against thermal and oxidative stress. Biochimica Et Biophysica Acta (BBA) - Proteins And Proteomics 2025, 1873: 141064. PMID: 39956303, DOI: 10.1016/j.bbapap.2025.141064.Peer-Reviewed Original ResearchConceptsChaperone-like activitySeminal plasmaFibronectin type IITetramer to monomersSperm capacitationSurface hydrophobicityMolecular chaperonesClient proteinsHeat shock proteinsBiophysical studiesAlcohol dehydrogenaseOxidative stressPhysiological ligandsShock proteinsProteinHead group moietySHspsBinding of phosphorylcholineCholine phospholipidsBindingFibronectinDehydrogenaseChaperoneSpermMammals
2023
Contrasting effects of molecular crowding on the membrane-perturbing and chaperone-like activities of major bovine seminal plasma protein, PDC-109
Singh B, Cheppali S, Saha I, Swamy M. Contrasting effects of molecular crowding on the membrane-perturbing and chaperone-like activities of major bovine seminal plasma protein, PDC-109. International Journal Of Biological Macromolecules 2023, 254: 127573. PMID: 37923045, DOI: 10.1016/j.ijbiomac.2023.127573.Peer-Reviewed Original ResearchConceptsChaperone-like activityPDC-109Effects of molecular crowdingMembrane destabilizationMolecular crowdingBovine seminal plasma proteinSperm cell surfaceSeminal plasma proteinsBovine seminal plasmaAcrosome reactionClient proteinsProtein stabilityMicroenvironment of proteinsSeminal plasmaMembrane-perturbingProtein oligomersReduced surface hydrophobicityOligomeric proteinsLipid effluxCell surfaceCrowding agentsProteinIsothermal titration calorimetric studiesTitration calorimetric studiesFunctional activity
2021
Purification, molecular characterization and ligand binding properties of the major donkey seminal plasma protein DSP-1
Alim S, Cheppali S, Laitaoja M, Talluri T, Jänis J, Swamy M. Purification, molecular characterization and ligand binding properties of the major donkey seminal plasma protein DSP-1. International Journal Of Biological Macromolecules 2021, 194: 213-222. PMID: 34863837, DOI: 10.1016/j.ijbiomac.2021.11.177.Peer-Reviewed Original ResearchConceptsSperm plasma membraneSeminal plasma proteinsFibronectin type IIAmino acid sequenceIntrinsic fluorescence titrationBind to phosphorylcholineHSP-1/2PDC-109Family proteinsAcid sequenceCholine phospholipidsLigand binding propertiesEquus hemionusMultiple acetylationsSeminal plasmaPlasma membraneMolecular characterizationMammalian speciesMembrane perturbationProteinHigh-resolution LC-MS analysisProtein 1Head group moietyBinding propertiesCell membrane
1999
Seminal plasma biochemical markers and their association with semen analysis findings
Diamandis E, Arnett W, Foussias G, Pappas H, Ghandi S, Melegos D, Mullen B, Yu H, Srigley J, Jarvi K. Seminal plasma biochemical markers and their association with semen analysis findings. Urology 1999, 53: 596-603. PMID: 10096390, DOI: 10.1016/s0090-4295(98)00550-0.Peer-Reviewed Original ResearchConceptsVasectomy patientsProstaglandin D synthaseDifferential diagnosisBiochemical markersInsulin-like growth factorPlasma biochemical markersProstate-specific antigenSemen analysis findingsPercentage of motilityPGDS concentrationSeminal plasmaNormal morphologySperm qualitySeminal plasma correlatesPatient ageClinical valueNormal subjectsNonobstructive azoospermiaPatientsClinical groupsBiochemical parametersPlasma correlateProtein 3Immunofluorometric procedureGrowth factor
1997
NONPROSTATIC SOURCES OF PROSTATE-SPECIFIC ANTIGEN
Diamandis E, Yu H. NONPROSTATIC SOURCES OF PROSTATE-SPECIFIC ANTIGEN. Urologic Clinics Of North America 1997, 24: 275-282. PMID: 9126224, DOI: 10.1016/s0094-0143(05)70373-6.Peer-Reviewed Original ResearchConceptsNonprostatic tissuesProstate-specific antigenBreast nipple aspirate fluidBreast cancer risk assessmentPSA gene expressionBreast cancer cytosolsHigher PSA concentrationsBreast cancer prognosisRegulation of PSAPotential clinical utilityCancer risk assessmentMicrograms/LNonprostatic sourcesPSA regulationAndrogen excessSerum PSAMicrograms/L.Breast secretionsAspirate fluidSeminal plasmaPSA productionPSA-ACT complexClinical utilityCancer cytosolsProstatic tissue
1992
Human seminal relaxin is a product of the same gene as human luteal relaxin.
Winslow J, Shih A, Bourell J, Weiss G, Reed B, Stults J, Goldsmith L. Human seminal relaxin is a product of the same gene as human luteal relaxin. Endocrinology 1992, 130: 2660-2668. DOI: 10.1210/en.130.5.2660.Peer-Reviewed Original ResearchH2 geneC4 reverse-phase columnAmino acid sequencePooled human seminal plasmaB-chainA-chainGas-phase sequencingHuman seminal plasmaHuman genomeAcid sequenceGene H1Ion-exchange chromatographyC-terminusNonallelic genesSeminal plasmaB-chain C-terminusSemen plasmaGene expressionGenesB-26Immunoaffinity chromatographyH1 relaxinPurification stepsRelaxin peptidesHPLC steps
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