Studies on mitogen regulated protein (proliferin) during murine development

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1988
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Mubaidin, Adnan
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Marit Nilsen-Hamilton
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Biochemistry, Biophysics and Molecular Biology

The Department of Biochemistry, Biophysics, and Molecular Biology was founded to give students an understanding of life principles through the understanding of chemical and physical principles. Among these principles are frontiers of biotechnology such as metabolic networking, the structure of hormones and proteins, genomics, and the like.

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The Department of Biochemistry and Biophysics was founded in 1959, and was administered by the College of Sciences and Humanities (later, College of Liberal Arts & Sciences). In 1979 it became co-administered by the Department of Agriculture (later, College of Agriculture and Life Sciences). In 1998 its name changed to the Department of Biochemistry, Biophysics, and Molecular Biology.

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1959–present

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  • Department of Biochemistry and Biophysics (1959–1998)

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Abstract

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.

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Fri Jan 01 00:00:00 UTC 1988