Skip to main page content
U.S. flag

An official website of the United States government

Dot gov

The .gov means it’s official.
Federal government websites often end in .gov or .mil. Before sharing sensitive information, make sure you’re on a federal government site.

Https

The site is secure.
The https:// ensures that you are connecting to the official website and that any information you provide is encrypted and transmitted securely.

Access keys NCBI Homepage MyNCBI Homepage Main Content Main Navigation
. 1994 Apr-Jun;11(2):127-34.
doi: 10.3109/09687689409162230.

Biosynthesis and intracellular transport of a membrane glycoprotein (plgp57) of the prelysosome compartment

L Heller  1 , J E Park, W J Brown
Affiliations
Free article

Biosynthesis and intracellular transport of a membrane glycoprotein (plgp57) of the prelysosome compartment

L Heller et al. Mol Membr Biol. 1994 Apr-Jun.
Free article

Abstract

We have characterized the biosynthesis and intracellular transport of a membrane glycoprotein, designated plgp57, which is found predominantly in the prelysosome compartment (PLC) of Madin-Darby bovine kidney cells. In pulse-chase experiments, plgp57 was found to be initially synthesized as a 35 kDa precursor which was modified to yield a diffuse approximately 57 kDa mature form. Digestion with endoglycosidase H (endo H) demonstrated that the 35 kDa precursor contained three endo H-sensitive, high mannose-type oligosaccharides which became modified to endo H-resistant, complex-type sugars on the approximately 57 kDa mature form. Labelling cells in the presence of tunicamycin and treatment of the 35 kDa precursor with endo H revealed that plgp57 has a core protein of 24 kDa to which three N-asparagine-liked oligosaccharides are attached. Other experiments indicated that plgp57 could be differentially glycosylated on a common 24 kDa core protein in different cell types. The half-lives of the glycosylated and non-glycosylated forms of plgp57 were approximately 18 and approximately 13 h, respectively. Glycosylated and non-glycosylated plgp57 exhibited similar steady-state intracellular distributions, indicating that targeting of plgp57 to the PLC does not require carbohydrate address markers. Pulse-labeling of cells followed by organelle fractionation at various chase times revealed a t1/2 = approximately 1 h for the transit of newly synthesized plgp57 to the PLC. Finally, amino terminal sequencing of plgp57 revealed the similarity of this protein to the CD63/ME491 family of membrane glycoproteins.

PubMed Disclaimer

Similar articles

See all similar articles

Cited by

Publication types

Substances

LinkOut - more resources