Biomaterial Database

Characterization of insulin-like growth factor receptors in human thyroid tissue. 1992

K Cissewski, and M Wolf, and A C Moses

Charles A. Dana Research Laboratories, Department of Medicine, Beth Israel Hospital, Boston, MA.

We have characterized the binding of 125I-IGF-I and 125I-IGF-II to plasma membranes purified from human thyroid tissue. IGF binding was time- and temperature-dependent. At 4 degrees C, maximal specific binding of 125I-IGF-I was 17.3 +/- 2.5% and of 125I-IGF-II was 8.8 +/- 2.0% (mean +/- SD/60 micrograms membrane protein). 125I-IGF-I binding was inhibited completely by unlabeled IGF-I, IGF-II, insulin, and the type-I IGF receptor monoclonal antibody, alpha IR-3. 125I-IGF-II was inhibited completely by unlabeled IGF-II and nearly completely by IGF-I. 125I-IGF-II binding also was inhibited significantly by insulin, suggesting that much or all of the IGF-II was bound to the type-I IGF receptor. Scatchard analysis revealed a single class of binding sites with a Kd of 6.0 +/- 4.2 x 10(-10) M for IGF-I binding and 5.7 +/- 1.3 x 10(-10) M for IGF-II binding. IGF-I binding was inhibited by a variety of salts in a dose-dependent manner, calcium and magnesium salts being more effective than sodium or potassium salts. Affinity crosslinking of 125I-IGF-I and -II showed clear evidence only for type-I IGF receptors. Thus, a crude plasma membrane fraction of human thyroid tissue expresses predominantly type-I IGF receptors.

UI	MeSH Term	Description	Entries
D007700	Kinetics	The rate dynamics in chemical or physical systems.
D002462	Cell Membrane	The lipid- and protein-containing, selectively permeable membrane that surrounds the cytoplasm in prokaryotic and eukaryotic cells.	Plasma Membrane,Cytoplasmic Membrane,Cell Membranes,Cytoplasmic Membranes,Membrane, Cell,Membrane, Cytoplasmic,Membrane, Plasma,Membranes, Cell,Membranes, Cytoplasmic,Membranes, Plasma,Plasma Membranes
D003432	Cross-Linking Reagents	Reagents with two reactive groups, usually at opposite ends of the molecule, that are capable of reacting with and thereby forming bridges between side chains of amino acids in proteins; the locations of naturally reactive areas within proteins can thereby be identified; may also be used for other macromolecules, like glycoproteins, nucleic acids, or other.	Bifunctional Reagent,Bifunctional Reagents,Cross Linking Reagent,Crosslinking Reagent,Cross Linking Reagents,Crosslinking Reagents,Linking Reagent, Cross,Linking Reagents, Cross,Reagent, Bifunctional,Reagent, Cross Linking,Reagent, Crosslinking,Reagents, Bifunctional,Reagents, Cross Linking,Reagents, Cross-Linking,Reagents, Crosslinking
D006801	Humans	Members of the species Homo sapiens.	Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
D000345	Affinity Labels	Analogs of those substrates or compounds which bind naturally at the active sites of proteins, enzymes, antibodies, steroids, or physiological receptors. These analogs form a stable covalent bond at the binding site, thereby acting as inhibitors of the proteins or steroids.	Affinity Labeling Reagents,Labeling Reagents, Affinity,Labels, Affinity,Reagents, Affinity Labeling
D013388	Succinimides	A subclass of IMIDES with the general structure of pyrrolidinedione. They are prepared by the distillation of ammonium succinate. They are sweet-tasting compounds that are used as chemical intermediates and plant growth stimulants.	Butanimides,Pyrrolidinediones
D013961	Thyroid Gland	A highly vascularized endocrine gland consisting of two lobes joined by a thin band of tissue with one lobe on each side of the TRACHEA. It secretes THYROID HORMONES from the follicular cells and CALCITONIN from the parafollicular cells thereby regulating METABOLISM and CALCIUM level in blood, respectively.	Thyroid,Gland, Thyroid,Glands, Thyroid,Thyroid Glands,Thyroids
D017526	Receptor, IGF Type 1	A protein-tyrosine kinase receptor that is closely related in structure to the INSULIN RECEPTOR. Although commonly referred to as the IGF-I receptor, it binds both IGF-I and IGF-II with high affinity. It is comprised of a tetramer of two alpha and two beta subunits which are derived from cleavage of a single precursor protein. The beta subunit contains an intrinsic tyrosine kinase domain.	IGF Type 1 Receptor,IGF-I Receptor,Receptor, IGF-I,Receptor, Insulin-Like Growth Factor I,Receptor, Insulin-Like Growth Factor Type 1,IGF-1 Receptor,Insulin-Like-Growth Factor I Receptor,Receptor, IGF Type 1 alpha Subunit,Receptor, IGF Type 1 beta Subunit,Receptors, IGF-1,Receptors, Insulin-Like-Growth Factor I,IGF 1 Receptor,IGF I Receptor,IGF-1 Receptors,Insulin Like Growth Factor I Receptor,Receptor, IGF I,Receptor, IGF-1,Receptors, IGF 1
D017527	Receptor, IGF Type 2	A receptor that is specific for IGF-II and mannose-6-phosphate. The receptor is a 250-kDa single chain polypeptide which is unrelated in structure to the type 1 IGF receptor (RECEPTOR, IGF TYPE 1) and does not have a tyrosine kinase domain.	IGF Type 2 Receptor,IGF-II Receptor,Receptor, IGF-II,Receptor, Insulin-Like Growth Factor II,Receptor, Insulin-Like Growth Factor Type 2,Receptor, Mannose-6-Phosphate,IGF-2 Receptor,Insulin-Like-Growth-Factor II Receptor,Mannose-6-Phosphate Receptor,Receptors, IGF-2,Receptors, Insulin-Like Growth Factor II,IGF 2 Receptor,IGF II Receptor,IGF-2 Receptors,Insulin Like Growth Factor II Receptor,Mannose 6 Phosphate Receptor,Receptor, IGF II,Receptor, IGF-2,Receptor, Insulin Like Growth Factor II,Receptor, Insulin Like Growth Factor Type 2,Receptor, Insulin-Like-Growth-Factor II,Receptor, Mannose 6 Phosphate,Receptors, IGF 2,Receptors, Insulin Like Growth Factor II
D066298	In Vitro Techniques	Methods to study reactions or processes taking place in an artificial environment outside the living organism.	In Vitro Test,In Vitro Testing,In Vitro Tests,In Vitro as Topic,In Vitro,In Vitro Technique,In Vitro Testings,Technique, In Vitro,Techniques, In Vitro,Test, In Vitro,Testing, In Vitro,Testings, In Vitro,Tests, In Vitro,Vitro Testing, In