Hyaluronic acid binding, endocytosis and degradation by sinusoidal liver endothelial cells
The binding, endocytosis, and degradation of {sup 125}I-hyaluronic acid ({sup 125}I-HA) by liver endothelial cells (LEC) was studied under several conditions. The dissociation of receptor-bound {sup 125}I-HA was rapid, with a half time of {approx}31 min and a K{sub off} of 6.3 {times} 10{sup {minus}4}/sec. A large reversible increase in {sup 125}I-HA binding to LEC at pH 5.0 was due to an increase in the observed affinity of the binding interaction. Pronase digestion suggested the protein nature of the receptor and the intracellular location of the digitonin exposed binding activity. Binding and endocytosis occur in the presence of 10 mM EGTA indicating that divalent cations are not required for receptor function. To study the degradation of {sup 125}I-HA by LEC, a cetylpyridinium chloride (CPC) precipitation assay was characterized. The minimum HA length required for precipitation was elucidated. The fate of the LEC HA receptor after endocytosis was examined.
- Research Organization:
- Texas Univ., Houston, TX (USA). Graduate School of Biomedical Sciences
- OSTI ID:
- 6983895
- Country of Publication:
- United States
- Language:
- English
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59 BASIC BIOLOGICAL SCIENCES
ALCOHOLS
AMINES
ANIMAL TISSUES
BETA DECAY RADIOISOTOPES
BIOASSAY
BIOCHEMICAL REACTION KINETICS
BIOLOGICAL HALF-LIFE
BODY
CARBOHYDRATES
CARBOXYLIC ACIDS
CHELATING AGENTS
DAYS LIVING RADIOISOTOPES
DIGESTIVE SYSTEM
EGTA
ELECTRON CAPTURE RADIOISOTOPES
ENDOTHELIUM
GLANDS
GLYCOLS
HYALURONIC ACID
HYDROXY COMPOUNDS
IMMUNOASSAY
INTERMEDIATE MASS NUCLEI
IODINE 125
IODINE ISOTOPES
ISOTOPE APPLICATIONS
ISOTOPES
KINETICS
LIVER
MEMBRANE PROTEINS
METABOLISM
MUCOPOLYSACCHARIDES
NUCLEI
ODD-EVEN NUCLEI
ORGANIC ACIDS
ORGANIC COMPOUNDS
ORGANS
POLYSACCHARIDES
PROTEINS
RADIOISOTOPES
REACTION KINETICS
RECEPTORS
SACCHARIDES
TISSUES
TRACER TECHNIQUES