The characterization and molecular structure of hepatoproliferin: a liver regeneration factor from rat hepatocytes

Biofactors. 2007;30(1):49-65. doi: 10.1002/biof.5520300106.

Abstract

Hepatoproliferin (HPF) was purified from regenerating rat livers as an oligomeric entity (big-HPF) from which the monomeric form (small-HPF) could be obtained using disaggregating conditions. By using a solid-phase ion-exchange method, small-HPF was forced to dissociate into two charged ionic species, namely norepinephrine (NE) and a sulfonated disaccharide with a molecular structure consisting of D-glucuronic acid bound to glucosamine 2,6-disulfate by a beta-glycosidic linkage having a beta, 1 --> 4 configuration. Monomeric HPF stemmed from the formation of three electrostatic bonds between the protonated amine groups of three norepinephrines, of which two bind to the deprotonated sulfonic groups of glucosamine 2,6-disulfate and one to the deprotonated carboxylic group of glucuronic acid, to constitute a tightly associated complex with a molecular mass of 1046 Da. This represents one of the two purified isoforms of small-HPF. The other isoform, which has a lower molecular mass of 877 Da, lack one NE, leaving the weaker carboxylic group of glucuronic acid unoccupied, to constitute a more acidic form of HPF.

Publication types

  • Research Support, Non-U.S. Gov't

MeSH terms

  • Animals
  • Arylsulfatases / metabolism
  • Chromatography, High Pressure Liquid
  • Chromatography, Ion Exchange
  • Disaccharides / analysis
  • Disaccharides / pharmacology
  • Glucuronidase / metabolism
  • Hexosamines / chemistry*
  • Hexosamines / isolation & purification
  • Hexosamines / pharmacology
  • Liver Regeneration* / drug effects
  • Male
  • Molecular Structure
  • Norepinephrine / analysis
  • Rats
  • Rats, Sprague-Dawley

Substances

  • Disaccharides
  • Hexosamines
  • hepatoproliferin, rat
  • Arylsulfatases
  • Glucuronidase
  • Norepinephrine