The predicted proteinase furin is not the hepatic proalbumin convertase.
Rat and chicken liver microsomal membranes were used to investigate the relationship between proalbumin processing activity and the predicted proteinase furin. Two polyclonal antisera directed against the predicted catalytic domain of furin showed the highest level of immunoreactivity in a microsomal fraction that had minimal proalbumin converting activity. Extracts of the fraction containing most converting activity lacked detectable furin. In addition, the proalbumin convertase was not inhibited by the anti-furin antisera. These results strongly suggest that furin is not responsible for the in vivo cleavage of proalbumin.
Ledgerwood
E C
EC
Molecular Pathology Laboratory, Christchurch Hospital, New Zealand.
George
P M
PM
Bathurst
I C
IC
Brennan
S O
SO
D000595:Amino Acid Sequence; D000818:Animals; D002645:Chickens; D045683:Furin; D008862:Microsomes, Liver / Q000201:enzymology; D008969:Molecular Sequence Data; D011228:Prealbumin / Q000378:metabolism*; D011499:Protein Processing, Post-Translational; D013379:Substrate Specificity; D013381:Subtilisins / Q000737:chemistry / Q000378:metabolism*
D011228:Prealbumin; D013381:Subtilisins; D045683:Furin