Modification of the intramolecular turnover of terminal carbohydrates of dipeptidylaminopeptidase IV isolated from rat-liver plasma membrane during liver regeneration
- PMID: 6363072
- DOI: 10.1111/j.1432-1033.1984.tb07934.x
Modification of the intramolecular turnover of terminal carbohydrates of dipeptidylaminopeptidase IV isolated from rat-liver plasma membrane during liver regeneration
Abstract
An intramolecular turnover of the terminal carbohydrates L-fucose, N-acetylneuraminic acid and D-galactose is a characteristic property of several liver plasma membrane glycoproteins, first demonstrated for dipeptidylaminopeptidase IV (EC 3.4.14.5., DPP IV). The core carbohydrates D-mannose and N-acetyl-D-glucosamine turn over like the polypeptide chain. The ratio of apparent half-lives of L-fucose and L-methionine of DPP IV is shifted from 0.17 in normal liver to 0.60 in regenerating liver. The ratio of half-lives of N-acetylneuraminic acid and L-methionine is only slightly changed from 0.43 in normal liver to 0.61 in regenerating liver. The ratio of apparent half-lives of D-mannose and L-methionine amounts to 0.80 in normal liver and 0.71 after partial hepatectomy. From this a drastic reduction of the intramolecular turnover of L-fucose on plasma membrane DPP IV in regenerating liver can be derived. The intramolecular N-acetylneuraminic acid turnover is affected to only a minor extent. D-Mannose turns over like the polypeptide in both normal and regenerating liver. The intramolecular L-fucose turnover may be involved in membrane glycoprotein recycling, which presumably is altered in regenerating liver. Additionally, L-fucose could regulate the rate of degradation of DPP IV, since core-fucosylated glycoproteins appear to be resistant to mammalian endo-N-acetylglucosaminidase.
Similar articles
-
Heterogeneous turnover of terminal and core sugars within the carbohydrate chain of dipeptidylaminopeptidase IV isolated from rat liver plasma membrane.FEBS Lett. 1983 Oct 31;163(1):150-2. doi: 10.1016/0014-5793(83)81183-1. FEBS Lett. 1983. PMID: 6354750
-
Remodeling of a rat hepatocyte plasma membrane glycoprotein. De- and reglycosylation of dipeptidyl peptidase IV.J Biol Chem. 1988 Aug 25;263(24):11736-42. J Biol Chem. 1988. PMID: 2900246
-
Rapid intramolecular turnover of N-linked glycans in plasma membrane glycoproteins. Extension of intramolecular turnover to the core sugars in plasma membrane glycoproteins of hepatoma.Eur J Biochem. 1989 Dec 8;186(1-2):55-62. doi: 10.1111/j.1432-1033.1989.tb15177.x. Eur J Biochem. 1989. PMID: 2598940
-
Decreased intramolecular turnover of L-fucose in membrane glycoproteins of rat liver during liver regeneration.Biol Chem Hoppe Seyler. 1989 Nov;370(11):1221-8. doi: 10.1515/bchm3.1989.370.2.1221. Biol Chem Hoppe Seyler. 1989. PMID: 2610938
-
[Dipeptidyl peptidase IV - a serine exopeptidase of the cellular membrane].Cesk Fysiol. 1982;31(1):27-53. Cesk Fysiol. 1982. PMID: 7037206 Review. Czech. No abstract available.
Cited by
-
Increased activity of dipeptidyl peptidase IV in serum of hepatoma-bearing rats coincides with the loss of the enzyme from the hepatoma plasma membrane.Experientia. 1986 Jul 15;42(7):826-8. doi: 10.1007/BF01941540. Experientia. 1986. PMID: 2874051
Publication types
MeSH terms
Substances
LinkOut - more resources
Full Text Sources