Binding of uteroglobin to microsomes and plasmatic membranes

FEBS Lett. 1995 Mar 20;361(2-3):255-8. doi: 10.1016/0014-5793(95)00167-8.

Abstract

Microsomes and plasmatic membranes from rat liver bind radioactive uteroglobin (UG) in vitro with high affinity (Kd = 1.7 x 10(-10) M. The binding is saturable and specific and dependent on previous reduction of UG with dithiothreitol. Microsomes from rat spleen or lung or from rabbit endometrium also possess a similar ability. Binding capacity is not affected by previous treatment of microsomes with phospholipase A2 or peptide-N-glycosidase F but is lost after brief treatment with trypsin. The complex formed between UG and the binding component can be solubilized from microsomes with 5 mM CHAPS and it elutes with an apparent Mr of 90,000 in a Sephacryl 200 column. The complex is resistant to 8 M urea but is completely dissociated by Triton X-100. The UG-binding protein(s) has been partially purified from solubilized microsomes and membranes by affinity chromatography. The results are discussed in relation to a possible physiological effect of UG on cellular membranes.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Carrier Proteins / isolation & purification
  • Carrier Proteins / metabolism*
  • Cell Membrane / metabolism*
  • Cholic Acids
  • Chromatography, Affinity
  • Chromatography, Gel
  • Detergents
  • Electrophoresis, Polyacrylamide Gel
  • Endometrium / metabolism
  • Female
  • Intracellular Membranes / metabolism
  • Kinetics
  • Lung / metabolism
  • Microsomes / metabolism*
  • Octoxynol / pharmacology
  • Phospholipases A / pharmacology
  • Phospholipases A2
  • Protein Binding
  • Rabbits
  • Rats
  • Spleen / metabolism
  • Trypsin / pharmacology
  • Urea / pharmacology
  • Uteroglobin / metabolism*

Substances

  • Carrier Proteins
  • Cholic Acids
  • Detergents
  • Urea
  • Octoxynol
  • Uteroglobin
  • Phospholipases A
  • Phospholipases A2
  • Trypsin
  • 3-((3-cholamidopropyl)dimethylammonium)-1-propanesulfonate