RT Book, Section
A1 Jaeken, Jaak
A2 Kline, Mark W.
SR Print(0)
ID 1182929762
T1 Congenital Disorders of Protein Glycosylation
T2 Rudolph's Pediatrics, 23e
YR 2018
FD 2018
PB McGraw-Hill Education
PP New York, NY
SN 9781259588594
LK accesspediatrics.mhmedical.com/content.aspx?aid=1182929762
RD 2024/04/20
AB Glycosylation  is  an  important  posttranslational  protein  modification  occurring  in  the  cytoplasm,  the  endoplasmic  reticulum,  and  the  Golgi  apparatus.  A  rapidly  growing  family  of  genetic  diseases  is  due  to  defects  in  protein  and  lipid  glycosylation  (congenital  disorders  of  glycosylation  [CDG]).  Most  CDGs  are  severe,  multisystem  diseases  with  prominent  neurologic  involvement.  Nearly  100  CDGs  have  been  identified.  This  chapter  is  limited  to  the  protein  glycosylation  defects  (some  80  disorders).  Twenty-five  CDGs  are  due  to  an  N-glycosylation  defect  (Table  158-1).  Twenty  disorders  have  been  identified  in  O-glycosylation,  including  some  long-known  diseases  such  as  hereditary  multiple  exostoses  (Table  158-2).  Thirty-four  disorders  have  a  combined  N-  and  O-glycosylation  defect,  including  dolichol  metabolism  defects  (Table  158-3).  Important  tools  in  the  diagnosis  are  serum  transferrin  (Tf)  isoelectric  focusing  (IEF),  serum  apolipoprotein  C-III  (apo  C-III)  isoelectrofocusing,  protein-linked  glycan  analysis,  and  genetic  analysis.  In  this  text,  we  use  the  nomenclature  introduced  in  2009,  namely  the  official  gene  symbol  (not  in  italics)  followed  by  “-CDG.”