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J. Biol. Chem., Vol. 269, Issue 6, 4035-4041, Feb, 1994
A Schweizer, H Clausen, G van Meer and HP Hauri
The identification of an endoplasmic reticulum-Golgi intermediate
compartment (ERGIC), defined by the 53-kDa transmembrane marker protein
ERGIC-53, has added to the complexity of the exocytic pathway of higher
eukaryotic cells. Recently, a subcellular fractionation procedure was
established for the isolation of the ERGIC from Vero cells (Schweizer, A.,
Matter, K., Ketcham, C. M., and Hauri, H.-P. (1991) J. Cell Biol. 113,
45-54) which provides a means to study more precisely the
compartmentalization of the various enzymic functions along the early
secretory pathway. Here, we have investigated if O-glycan initiation and
sphingomyelin synthesis are associated with the ERGIC by analyzing both the
responsible enzyme activities and their corresponding products. Moreover,
the synthesis of glucosylceramide, the precursor of most
glycosphingolipids, was also analyzed. In the purified ERGIC fraction
UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase (GalNAc
transferase) was only minimally enriched, sphingomyelin synthase was not
enriched, and UDP-glucose:ceramide-glucosyl transferase specific activity
was lower than in the homogenate. On Percoll gradients all three enzymes
cofractionated with Golgi markers rather than ERGIC-53. Accordingly,
sphingomyelin concentrations were extremely low in the ERGIC fraction.
Double immunofluorescence localization of core N-acetylgalactosamine, the
product of GalNAc transferase, by monoclonal antibodies against
GalNAc-Ser/Thr (Tn antigen) revealed only little apparent overlap with
ERGIC-53. This was particularly evident in brefeldin A-treated cells which
showed entirely different patterns of Tn antigens and ERGIC-53. The results
suggest that in the secretory pathway of Vero cells O-glycan initiation and
sphingomyelin as well as glucosylceramide synthesis mainly occur beyond the
ERGIC in the Golgi apparatus.
Localization of O-glycan initiation, sphingomyelin synthesis, and glucosylceramide synthesis in Vero cells with respect to the endoplasmic reticulum-Golgi intermediate compartment
Department of Pharmacology, University of Basel, Switzerland.
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