Studies on mitogen regulated protein (proliferin) during murine development

dc.contributor.advisor Marit Nilsen-Hamilton
dc.contributor.author Mubaidin, Adnan
dc.contributor.department Biochemistry, Biophysics and Molecular Biology
dc.date 2018-08-17T09:52:12.000
dc.date.accessioned 2020-07-02T06:09:45Z
dc.date.available 2020-07-02T06:09:45Z
dc.date.copyright Fri Jan 01 00:00:00 UTC 1988
dc.date.issued 1988
dc.description.abstract <p>Mitogen regulated protein/proliferin (MRP/PLF) is a glycoprotein with a significant percentage of positional identity in sequence with the prolactin-growth hormone family of proteins. MRP/PLF is secreted by proliferating mouse embryo cell lines and by the mouse placenta.;I developed a radioimmunoassay to examine the temporal and the spatial distribution of MRP/PLF throughout the pregnancy of CF-1 mice. The results revealed the appearance of MRP/PLF in mouse maternal plasma on the eighth day of gestation. The concentration of MRP/PLF in mouse maternal plasma reached a peak (8-10 [mu]g/ml) between the tenth and eleventh days of gestation (mid-pregnancy) and declined thereafter. Examination of various pregnant mouse tissue extracts obtained at different days in gestation revealed the presence of MRP/PLF in the placenta at a peak level (40-50 pg/[mu]g protein) between the ninth and thirteenth days of gestation; this level declined thereafter. The temporal distribution of MRP/PLF was associated with placental growth.;Other investigators have shown that MRP/PLF secreted by a cultured Chinese hamster ovary (CHO) cell line transformed with an expression vector containing mouse MRP/PLF cDNA binds the mannose 6-phosphate receptor. To examine whether MRP/PLF is cleared from maternal plasma via the mannose 6-phosphate receptors, and to gain some understanding of the structure of the carbohydrate chain on MRP/PLF, we examined the ability of MRP/PLF from maternal CF-1 mouse blood to bind to the mannose 6-phosphate receptor.;The similarity of MRP/PLF structure with prolactin and with placental lactogens, together with the temporal distribution of MRP/PLF in mouse maternal blood, allows us to propose MRP/PLF as a placental hormone. The results in this dissertation also suggest that the rate of MRP/PLF clearance from the maternal circulation via the mannose 6-phosphate receptor is developmentally regulated, and the levels of MRP/PLF are not regulated by testosterone.</p>
dc.format.mimetype application/pdf
dc.identifier archive/lib.dr.iastate.edu/rtd/8874/
dc.identifier.articleid 9873
dc.identifier.contextkey 6344763
dc.identifier.doi https://doi.org/10.31274/rtd-180813-11669
dc.identifier.s3bucket isulib-bepress-aws-west
dc.identifier.submissionpath rtd/8874
dc.identifier.uri https://dr.lib.iastate.edu/handle/20.500.12876/81910
dc.language.iso en
dc.source.bitstream archive/lib.dr.iastate.edu/rtd/8874/r_8909176.pdf|||Sat Jan 15 02:18:05 UTC 2022
dc.subject.disciplines Biochemistry
dc.subject.keywords Biochemistry and biophysics
dc.subject.keywords Biochemistry
dc.title Studies on mitogen regulated protein (proliferin) during murine development
dc.type article
dc.type.genre dissertation
dspace.entity.type Publication
relation.isOrgUnitOfPublication faf0a6cb-16ca-421c-8f48-9fbbd7bc3747
thesis.degree.level dissertation
thesis.degree.name Doctor of Philosophy
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