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Membrane-associated insulin-like growth factor (IGF) binding structures in placental cells
- Source :
- Journal of the Serbian Chemical Society, Vol 68, Iss 11, Pp 811-818 (2003), Scopus-Elsevier
- Publication Year :
- 2003
- Publisher :
- National Library of Serbia, 2003.
-
Abstract
- The biological activities of IGF-I and ?II are mediated mainly by the type 1 IGF receptor (IGF 1R) and controlled by their interaction with soluble proteins, the IGF binding proteins (IGFBPs). Although there is a growing body of evidence that some IGFBPs may be cell surface-bound, published data concerning cell association of IGFBP-1 are scarce and none of them concern placental cells. The cell membranes used in this study were isolated from term human placenta. Detergent-solubilized membranes were shown to contain two types of IGF binding structures that were separated by gel filtration on a Sephadex G-100 column. Proteins in the first peak were eluted at V0(Mr>100 kD) and they bound IGF-I with greater specificity and affinity than IGF-II and insulin. Most likely, they represented the IGF 1R. Small proteins (Mr?45 kD) were eluted with the membrane proteins in the second maximum. They were able to bind IGF-I and IGF-II, but not insulin. The identity of these proteins was shown to be IGFBP-1 on the basis of their reaction with specific anti-IGFBP-1 antibodies. To the best of our knowledge, the existence of IGFBP-1 associated with human placental cell membranes has not been reported in the literature before. Colocalisation of IGFBP-1 with IGF 1R in cell membranes could provide efficient modulation of IGF 1R receptor-ligand interactions.
- Subjects :
- placental cell membranes
medicine.medical_treatment
Cell
Size-exclusion chromatography
lcsh:Chemistry
Insulin-like growth factor
medicine
IGF-II
gel filtration
biology
Chemistry
Insulin
General Chemistry
IGFBP-1
Molecular biology
IGF-I
medicine.anatomical_structure
Membrane
IGF 1R
lcsh:QD1-999
Membrane protein
Biochemistry
Sephadex
biology.protein
Antibody
Subjects
Details
- ISSN :
- 18207421 and 03525139
- Volume :
- 68
- Database :
- OpenAIRE
- Journal :
- Journal of the Serbian Chemical Society
- Accession number :
- edsair.doi.dedup.....3cafb01133cc32ab10b92561057558cc