The Elastin Receptor: A Galactoside-Binding Protein

The Elastin Receptor: A Galactoside-Binding Protein

The elastin receptor complex contains a component of 67 kilodaltons that binds to a glycoconjugate affinity column containing $\beta $-galactoside residues and is eluted from this column with lactose. This protein component is also released from the surface of cultured chondroblasts by incubation wi...

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Veröffentlicht in:Science (American Association for the Advancement of Science) 1988-03, Vol.239 (4847), p.1539-1541
Hauptverfasser: Hinek, Aleksander, Wrenn, David S., Mecham, Robert P., Barondes, Samuel H.
Format: Artikel
Sprache:eng
Schlagworte:
Amino acids
Anatomy & physiology
Animals
Antigens
Biochemistry
Biological and medical sciences
Cartilage - analysis
Cattle
Cell receptors
Cell structures and functions
Cells, Cultured
Chondrocytes
Chromatography, Affinity
Elastic tissue
Elastin
Elastin - metabolism
Extracellular Matrix - drug effects
Extracellular Matrix - metabolism
fetuses
Fundamental and applied biological sciences. Psychology
Galactosides - metabolism
Glycoconjugates - metabolism
Glycosides - metabolism
Immunoassay
Immunohistochemistry
Lactose - pharmacology
Lectins
lung
Lung - analysis
Lungs
Microscopy, Electron
Molecular and cellular biology
Protein research
Receptors
Receptors, Cell Surface - drug effects
Receptors, Cell Surface - isolation & purification
Receptors, Cell Surface - metabolism
T cell antigen receptors
T lymphocytes
Ungulates
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Beschreibung
Zusammenfassung:The elastin receptor complex contains a component of 67 kilodaltons that binds to a glycoconjugate affinity column containing $\beta $-galactoside residues and is eluted from this column with lactose. This protein component is also released from the surface of cultured chondroblasts by incubation with lactose, and its association with immobilized elastin is inhibited by lactose. Since lactose also blocks elastic fiber formation by cultured chondroblasts, the galactoside-binding property of the elastin receptor is implicated in this process.
ISSN:0036-8075
1095-9203
DOI:10.1126/science.2832941