PMID: 36062Oct 1, 1978

The binding of rat liver cell multiplication-stimulating activity (MSA) to human placenta and serum proteins

The Australian Journal of Experimental Biology and Medical Science
M W Brinsmead, G C Liggins

Abstract

Multiplication-stimulation activity (MSA) from the medium of BRL-3A rat liver cells in culture binds to cell membrane and cytosol receptors from human placenta and to serum proteins. The binding of MSA to placental cell membranes is dependent on time, temperature, pH and divalent ion concentration. MSA bound to placental cytosol receptor and serum is not displaced by insulin, whereas that bound to placental cell membranes is displaced by insulin and insulin-like peptides. The affinity of the three receptors for MSA is similar [approximately 10(8) M(-1)]. An assay using 125I-MSA and placental membrane receptor detects somatomedin-like receoptor activity (SmLRA) in unextracted sera from man and animals. A binding protein in serum that competes for 125I-MSA with receptor could not be completely separated from SmLRA by heating, acidification, charcoal treatment and gel chromatography of the serum. The relative activities of SmLRA and serum binding protein remained constant in three disorders of human growth (acromegaly, growth hormone deficiency and Laron's dwarfism) in which values of SmLRA varied widely. However, the binding protein is only partly responsible for the apparent SmLRA of unextracted serum. It is concluded that MSA i...Continue Reading

References

Nov 22, 1979·The New England Journal of Medicine·W H Daughaday
Mar 1, 1984·Clinics in Endocrinology and Metabolism
Aug 1, 1979·The Australian & New Zealand Journal of Obstetrics & Gynaecology·M W Brinsmead, G C Liggins

Related Concepts

Somatotropin Deficiency
Placenta Specimen
Recombinant Insulin-Like Growth Factor
Somatomedin Assay
Acromegaly
Somatomedins
Placenta
Serum Proteins
Acidification - ActCode
Charcoal

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