Maintenance of primary murine hepatocyte functions in multicomponent polymer capsules--in vitro cryopreservation studies.
OBJECTIVE
The potential of a new encapsulation system has been evaluated as an artificial housing for liver cells.


METHODS
Murine hepatocytes were encapsulated in specially designed multicomponent capsules formed by polyelectrolyte complexation of sodium alginate, cellulose sulphate and poly(methylene-co-guanidine) hydrochloride, the permeability of which has previously been characterised.


RESULTS
We demonstrate here the absence of cytotoxicity and the excellent biocompatibility of these capsules towards primary culture of murine hepatocytes. Experimental results demonstrated that the encapsulated hepatocytes retained their specific functions--transaminase activity, urea synthesis and protein secretion--over the first 4 days of culture in minimum medium. The cryopreservation of encapsulated hepatocytes, for periods of up to 4 months, did not alter their functional capacities, as no major differences were observed between unfrozen and frozen encapsulated cells for the functions tested.


CONCLUSIONS
Because of the absence of cytotoxicity, and the ease of handling and cryopreservation, while maintaining liver specific functions, the described system appears to be valuable for murine liver cell encapsulation. It is also a promising tool for fundamental research into drug metabolism, intercellular regulation, metabolic pathways, and the establishment of banks for the supply and storage of murine hepatocytes.
Canaple
L
L
Institute of Animal Biology, University of Lausanne, Switzerland.
Nurdin
N
N
Angelova
N
N
Saugy
D
D
Hunkeler
D
D
Desvergne
B
B
D000818:Animals; D001219:Aspartate Aminotransferases / Q000378:metabolism; D002470:Cell Survival; D002478:Cells, Cultured; D015925:Cryopreservation; D022781:Hepatocytes / Q000502:physiology*; D019164:Liver, Artificial; D008297:Male; D051379:Mice; D011108:Polymers; D014508:Urea / Q000378:metabolism
D011108:Polymers; D014508:Urea; D001219:Aspartate Aminotransferases