Polypeptide and glycoprotein abnormalities in dorsal root ganglia of streptozotocin-diabetic rats.
Observations were made on the polypeptide and glycoprotein composition of dorsal root ganglia from streptozotocin-induced diabetic rats by sodium dodecyl sulphate (SDS)-polyacrylamide gel electrophoresis (PAGE). Silver staining of one-dimensional gels failed to demonstrate any differences between diabetic and control animals. In two-dimensional studies, good resolution of polypeptides with a mass greater than 70 kDa was not obtained, but a number of important abnormalities in the polypeptide composition of diabetic ganglia were detected. Some polypeptides recognized in the gels from control ganglia were present in high concentrations in diabetic ganglia; other polypeptides, particularly a number of basic polypeptides of low molecular mass, were only identified in the diabetic rats. Three major polypeptides showed a small shift in their isoelectric point in the diabetic animals. The glycoprotein content of the ganglia was examined by lectin binding to both one- and two-dimensional gel separations. An increase in total glycoprotein content was evident in the diabetic ganglia. A number of polypeptides with a molecular mass between 70 and 110 kDa showed heavy glycosylation. Altered glycosylation of some specific polypeptides of lower molecular mass was also seen, 7 of these showing increased and 3 reduced glycosylation. The significance of these findings is discussed.
Schapira
A H
AH
University Department of Clinical Neurology, Queen Square, London, U.K.
Llewelyn
J G
JG
Patel
N J
NJ
Thomas
P K
PK
D000818:Animals; D003921:Diabetes Mellitus, Experimental / Q000139:chemically induced / Q000378:metabolism*; D005727:Ganglia, Spinal / Q000378:metabolism* / Q000473:pathology; D006023:Glycoproteins / Q000378:metabolism*; D008297:Male; D008970:Molecular Weight; D010455:Peptides / Q000378:metabolism*; D051381:Rats; D011919:Rats, Inbred Strains; D013311:Streptozocin
D006023:Glycoproteins; D010455:Peptides; D013311:Streptozocin