TY  - CHAP
M1  - Book, Section
TI  - Congenital Disorders of Glycosylation
A1  - Thiel, Christian
A1  - Himmelreich, Nastassja
A1  - Hoffmann, Georg F.
A1  - Körner, Christian
A2  - Sarafoglou, Kyriakie
A2  - Hoffmann, Georg F.
A2  - Roth, Karl S.
Y1  - 2017
N1  - 
T2  - Pediatric Endocrinology and Inborn Errors of Metabolism, 2e
AB  - Congenital  disorders  of  glycosylation  (CDG)  comprise  a  continuously  growing  group  of  monogenetic  inherited  diseases  in  glycoprotein  biosynthesis1,2,3,4,5,6  (Figure  44-1)  which  affect  the  generation  of  structurally  highly  diverse  oligosaccharides  that  are  covalently  attached  to  proteins  mostly  by  N-glycosidic  linkage  to  amino  groups  of  asparagine  residues,  or  by  O-glycosidic  linkage  to  hydroxyl  groups  of  serine  or  threonine  residues.  The  oligosaccharide  moieties  determine  crucial  biological  processes  like  protein  quality  control,  directed  protein  transport,  enzymatic  activity,  and  protein  stability.  Deficiencies  in  this  complex  metabolic  pathway  lead  to  multi-organ  diseases  with  neurologic  symptoms  often  dominating  (see  At-A-Glance).  Based  on  the  glycosylation  pattern  of  serum  transferrin  in  the  isoelectric  focusing  and  thereby  corresponding  to  their  subcellular  localization,  CDG  have  traditionally  been  subdivided  in  “CDG-I”  and  “CDG-II.”  CDG-I  comprise  deficiencies  that  either  diminish  the  biosynthesis  of  dolichol-linked  oligosaccharides  or  reduce  their  transfer  onto  newly  synthesized  proteins  by  the  oligosaccharyltransferase  complex  in  the  endoplasmic  reticulum.  CDG-II  affect  the  subsequent  trimming  and  elongation  of  glycans  bound  to  proteins  in  the  endoplasmic  reticulum  and  Golgi  apparatus  (Figure  44-1).  The  identification  of  a  considerable  number  of  new  CDG  types  afforded  the  improvement  of  nomenclature  which  now  connect  the  abbreviation  of  defective  proteins  with  the  term  CDG  (eg,  deficiency  of  the  enzyme  phosphomannomutase  2  [PMM2]),  formerly  known  as  CDG-Ia,  changed  to  PMM2-CDG  (see  At-A-Glance).  CDG  of  unknown  molecular  nature  remain  CDG-Ix  or  CDG-IIx.  Here  we  focus  on  N-glycosylation  defects  including  those  which  are  combined  with  mucin-type  O-glycosylation  involvement,  as  deficiencies  in  O-mannosylation  leading  to  muscular  dystrophies  with  neurological  impairment  have  recently  been  reviewed  elsewhere.7,8  
SN  - 
PB  - McGraw-Hill Education
CY  - New York, NY
Y2  - 2024/04/18
UR  - accesspediatrics.mhmedical.com/content.aspx?aid=1140323180
ER  -