Abstract
| Originalsprog | Engelsk |
|---|---|
| Tidsskrift | Journal of Biological Chemistry |
| Vol/bind | 270 |
| Udgave nummer | 31 |
| Sider (fra-til) | 18219-26 |
| Antal sider | 7 |
| ISSN | 0021-9258 |
| Status | Udgivet - 1995 |
| Udgivet eksternt | Ja |
Bibliografisk note
Keywords: Amino Acid Sequence; Animals; Binding, Competitive; Blotting, Western; Chickens; Egg Proteins; Endosomes; Female; Heymann Nephritis Antigenic Complex; Humans; LDL-Receptor Related Protein 1; Lactoferrin; Lipoproteins, LDL; Liver; Membrane Glycoproteins; Molecular Sequence Data; Oocytes; Protein Precursors; Rats; Receptors, Cell Surface; Receptors, Immunologic; Receptors, LDL; Recombinant Fusion Proteins; Tissue Distribution; alpha-MacroglobulinsBiblioteksadgang?
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I: Journal of Biological Chemistry, Bind 270, Nr. 31, 1995, s. 18219-26.
Publikation: Bidrag til tidsskrift › Tidsskriftartikel › Forskning › peer review
}
TY - JOUR
T1 - The chicken oocyte receptor for yolk precursors as a model for studying the action of receptor-associated protein and lactoferrin.
AU - Hiesberger, T
AU - Hermann, M
AU - Jacobsen, Linda
AU - Novak, S
AU - Hodits, R A
AU - Bujo, H
AU - Meilinger, M
AU - Hüttinger, M
AU - Schneider, W J
AU - Nimpf, J
N1 - Keywords: Amino Acid Sequence; Animals; Binding, Competitive; Blotting, Western; Chickens; Egg Proteins; Endosomes; Female; Heymann Nephritis Antigenic Complex; Humans; LDL-Receptor Related Protein 1; Lactoferrin; Lipoproteins, LDL; Liver; Membrane Glycoproteins; Molecular Sequence Data; Oocytes; Protein Precursors; Rats; Receptors, Cell Surface; Receptors, Immunologic; Receptors, LDL; Recombinant Fusion Proteins; Tissue Distribution; alpha-Macroglobulins
PY - 1995
Y1 - 1995
N2 - Receptor-associated protein (RAP) was originally described as a 39-kDa intracellular protein copurifying with mammalian low density lipoprotein (LDL) receptor-related protein/alpha 2-macroglobulin receptor (LRP/alpha 2MR). RAP has a high affinity for LRP/alpha 2MR and interferes with the receptor's ability to bind a variety of ligands. The laying hen expresses, in a tissue-specific manner, at least four different proteins which belong to the same family of receptors as LRP/alpha 2MR. Here we show that the chicken also produces RAP, so far thought to be expressed only in mammals. Studies on the interaction of recombinant human RAP with the LDL receptor family in the chicken revealed that RAP binds with high affinity to the abundant oocyte receptor for yolk precursors (OVR) as well as to the somatic cell-specific LRP/alpha 2MR. Significantly, RAP interacts with a lower affinity with the LDL receptor, but does not bind to the oocyte-specific form of LRP. Binding of RAP to OVR inhibits the interaction of the receptor with all known physiological ligands, i.e. the yolk precursors very low density lipoprotein, vitellogenin, and alpha 2-macroglobulin. In COS cells transfected with OVR, RAP is internalized and degraded in a concentration-dependent and saturable manner. Lactoferrin, another protein with a high affinity for mammalian LRP/alpha 2MR, also binds to OVR and abolishes its interaction with yolk precursors. Cross-competition experiments show that RAP and lactoferrin recognize sites different from those involved in yolk precursor binding. The availability of pure OVR and LDLR enable us to determine kinetic parameters for the binding of RAP and lactoferrin to these receptors by surface plasmon resonance. Taken together, our results strongly suggest that chicken OVR, which is easily accessible and highly abundant in growing oocytes, represents a superior system for studying mechanistic and structural aspects of the interaction of ligands and modulating proteins with members of the LDL receptor gene family.
AB - Receptor-associated protein (RAP) was originally described as a 39-kDa intracellular protein copurifying with mammalian low density lipoprotein (LDL) receptor-related protein/alpha 2-macroglobulin receptor (LRP/alpha 2MR). RAP has a high affinity for LRP/alpha 2MR and interferes with the receptor's ability to bind a variety of ligands. The laying hen expresses, in a tissue-specific manner, at least four different proteins which belong to the same family of receptors as LRP/alpha 2MR. Here we show that the chicken also produces RAP, so far thought to be expressed only in mammals. Studies on the interaction of recombinant human RAP with the LDL receptor family in the chicken revealed that RAP binds with high affinity to the abundant oocyte receptor for yolk precursors (OVR) as well as to the somatic cell-specific LRP/alpha 2MR. Significantly, RAP interacts with a lower affinity with the LDL receptor, but does not bind to the oocyte-specific form of LRP. Binding of RAP to OVR inhibits the interaction of the receptor with all known physiological ligands, i.e. the yolk precursors very low density lipoprotein, vitellogenin, and alpha 2-macroglobulin. In COS cells transfected with OVR, RAP is internalized and degraded in a concentration-dependent and saturable manner. Lactoferrin, another protein with a high affinity for mammalian LRP/alpha 2MR, also binds to OVR and abolishes its interaction with yolk precursors. Cross-competition experiments show that RAP and lactoferrin recognize sites different from those involved in yolk precursor binding. The availability of pure OVR and LDLR enable us to determine kinetic parameters for the binding of RAP and lactoferrin to these receptors by surface plasmon resonance. Taken together, our results strongly suggest that chicken OVR, which is easily accessible and highly abundant in growing oocytes, represents a superior system for studying mechanistic and structural aspects of the interaction of ligands and modulating proteins with members of the LDL receptor gene family.
M3 - Journal article
C2 - 7543099
SN - 0021-9258
VL - 270
SP - 18219
EP - 18226
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 31
ER -