title: Neuronal ceroid lipofuscinosis: late infantile or Jansky Bielschowsky type--re-revisited.
abstract: Among the now eight genetic types of neuronal ceroid-lipofuscinoses (NCL), CLN1 to CLN8, CLN2 is considered classic late-infantile NCL. It was originally described by Jansky in a family of eight children with four of them affected [Jansky J (1908) Sborn Lék 13:165-196] and, subsequently, by Bielschowsky in a family of three children each of whom was affected, and, hence, termed Jansky-Bielschowsky type of NCL. Earlier, archival studies of Bielschowsky's original post-mortem tissue blocks had documented accumulation of autofluorescent lipopigments with a curvilinear ultrastructure. In a subsequent study, described here, immunohistochemical absence of the CLN2-related lysosomal enzyme tripeptidyl peptidase-I and two heterozygous mutations in the CLN2 gene could be demonstrated in these archival tissues, further corroborating the identity of Bielschowsky's familial disorder and CLN2 described by M. Bielschowsky at the beginning of the last century. Furthermore, these immunohistochemical and mutational investigations underscore the value of archival tissue studies.
authors.affiliation: Department of Paediatrics, Royal Free and University College Medical School, The Rayne Institute, London, UK. ruth.wheeler@ucl.ac.uk
authors.forename: R B
authors.initials: RB
authors.lastname: Wheeler
authors.forename: M
authors.initials: M
authors.lastname: Schlie
authors.forename: E
authors.initials: E
authors.lastname: Kominami
authors.forename: L
authors.initials: L
authors.lastname: Gerhard
authors.forename: H H
authors.initials: HH
authors.lastname: Goebel
mesh_terms: D000626:Aminopeptidases; D001109:Archives; D002490:Central Nervous System / Q000378:metabolism / Q000473:pathology; D004252:DNA Mutational Analysis; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; D010450:Endopeptidases; D006801:Humans; D007150:Immunohistochemistry; D009472:Neuronal Ceroid-Lipofuscinoses / Q000235:genetics* / Q000473:pathology*; D009474:Neurons / Q000378:metabolism / Q000473:pathology; D010447:Peptide Hydrolases / Q000032:analysis / Q000235:genetics*; D057057:Serine Proteases; D000091346:Tripeptidyl-Peptidase 1
chemical_list: D000091346:Tripeptidyl-Peptidase 1; D010450:Endopeptidases; D010447:Peptide Hydrolases; D057057:Serine Proteases; D000626:Aminopeptidases; D004152:Dipeptidyl-Peptidases and Tripeptidyl-Peptidases; C000717267:TPP1 protein, human