Protein glycosylation

David Ashford da5 at unix.york.ac.uk
Tue Feb 21 08:53:28 EST 1995


On 19 Feb 1995 07:06:13 -0800 Kieran Breen wrote:

> From: Kieran Breen <K.C.BREEN at dundee.ac.uk>
> Date: 19 Feb 1995 07:06:13 -0800
> Subject: Protein glycosylation
> To: "bionet.glycosci mail newsgroup" <bionet-news at dl.ac.uk>
> 
> Does anybody know of examples whose subcellular distribution may be 
> etermined by their differential glycosylation state. This has been 
> suggested as a possible reason as to why a particular protein may exist 
> in both a membrane-bound and secreted form, both exhibiting different 
> glycosylation patterns.
> 
> Any suggestions would be gratefully received.
> 
> Kieran Breen
> Dept. of Pharmacology, University of Dundee
> k.c.breeb at dundee.ac.uk
>

I'm assuming you mean plasma membrane rather than an intracellular membrane 
localisation? The only instance I am aware of where glycosylation is responsible 
for _determining_ subcellular distribution is in the case of lysosomal targeting by 
Man-6-P.

What you may have is not cause but effect. The different glycosylation patterns 
may be due to one form of the protein being soluble and the other being membrane 
bound during their passage along the secretory pathway.  Check out papers by 
Fukuda in the mid/late 80s. One in particular may be of interest. Fukuda et al., 
(1988), A membrane-anchored from but not the secretory form of human chorionic 
gonadotrophin-alpha chain acquires polylactosaminoglycan. J.Biol.Chem. 263, 
5314-5318.

David Ashford
Plant Glycoprotein Research Facility
Dept of Biology, University of York
da5 at york.ac.uk









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