Palmitoyl-protein thioesterase and the molecular pathogenesis of infantile neuronal ceroid lipofuscinosis

Sandra L. Hofmann; Laura A. Lee; Jui Yun Lu; Linda A. Verkruyse

doi:10.1055/s-2007-973661

Palmitoyl-protein thioesterase and the molecular pathogenesis of infantile neuronal ceroid lipofuscinosis

Sandra L. Hofmann, Laura A. Lee, Jui Yun Lu, Linda A. Verkruyse

Research output: Contribution to journal › Article › peer-review

43 Scopus citations

Abstract

Palmitoyl-protein thioesterase (PPT) has recently been shown to be the defective enzyme underlying the infantile form of neuronal ceroid lipofuscinosis (INCL). In this paper, we review the enzymology of PPT, evidence for its localization in lysosomes, and recent advances in understanding the metabolic defect caused by PPT deficiency. Absence of PPT activity in lysosomes isolated from INCL lymphoblasts is demonstrated. A model for the formation of the storage bodies in INCL involving defective autophagocytic proteolysis is proposed.

Original language	English (US)
Pages (from-to)	27-30
Number of pages	4
Journal	Neuropediatrics
Volume	28
Issue number	1
DOIs	https://doi.org/10.1055/s-2007-973661
State	Published - Feb 1997

Keywords

Infantile neuronal ceroid lipofuscinosis
Lysosomal enzymes
Neurodegeneration
Protein acylation
Thioesterases

ASJC Scopus subject areas

Pediatrics, Perinatology, and Child Health
Clinical Neurology

Access to Document

10.1055/s-2007-973661

Cite this

@article{9100ebe8217449e0a19fa1c4b8ffccf8,

title = "Palmitoyl-protein thioesterase and the molecular pathogenesis of infantile neuronal ceroid lipofuscinosis",

abstract = "Palmitoyl-protein thioesterase (PPT) has recently been shown to be the defective enzyme underlying the infantile form of neuronal ceroid lipofuscinosis (INCL). In this paper, we review the enzymology of PPT, evidence for its localization in lysosomes, and recent advances in understanding the metabolic defect caused by PPT deficiency. Absence of PPT activity in lysosomes isolated from INCL lymphoblasts is demonstrated. A model for the formation of the storage bodies in INCL involving defective autophagocytic proteolysis is proposed.",

keywords = "Infantile neuronal ceroid lipofuscinosis, Lysosomal enzymes, Neurodegeneration, Protein acylation, Thioesterases",

author = "Hofmann, {Sandra L.} and Lee, {Laura A.} and Lu, {Jui Yun} and Verkruyse, {Linda A.}",

year = "1997",

month = feb,

doi = "10.1055/s-2007-973661",

language = "English (US)",

volume = "28",

pages = "27--30",

journal = "Neuropediatrics",

issn = "0174-304X",

publisher = "Hippokrates Verlag GmbH",

number = "1",

}

TY - JOUR

T1 - Palmitoyl-protein thioesterase and the molecular pathogenesis of infantile neuronal ceroid lipofuscinosis

AU - Hofmann, Sandra L.

AU - Lee, Laura A.

AU - Lu, Jui Yun

AU - Verkruyse, Linda A.

PY - 1997/2

Y1 - 1997/2

N2 - Palmitoyl-protein thioesterase (PPT) has recently been shown to be the defective enzyme underlying the infantile form of neuronal ceroid lipofuscinosis (INCL). In this paper, we review the enzymology of PPT, evidence for its localization in lysosomes, and recent advances in understanding the metabolic defect caused by PPT deficiency. Absence of PPT activity in lysosomes isolated from INCL lymphoblasts is demonstrated. A model for the formation of the storage bodies in INCL involving defective autophagocytic proteolysis is proposed.

AB - Palmitoyl-protein thioesterase (PPT) has recently been shown to be the defective enzyme underlying the infantile form of neuronal ceroid lipofuscinosis (INCL). In this paper, we review the enzymology of PPT, evidence for its localization in lysosomes, and recent advances in understanding the metabolic defect caused by PPT deficiency. Absence of PPT activity in lysosomes isolated from INCL lymphoblasts is demonstrated. A model for the formation of the storage bodies in INCL involving defective autophagocytic proteolysis is proposed.

KW - Infantile neuronal ceroid lipofuscinosis

KW - Lysosomal enzymes

KW - Neurodegeneration

KW - Protein acylation

KW - Thioesterases

UR - http://www.scopus.com/inward/record.url?scp=0030739514&partnerID=8YFLogxK

UR - http://www.scopus.com/inward/citedby.url?scp=0030739514&partnerID=8YFLogxK

U2 - 10.1055/s-2007-973661

DO - 10.1055/s-2007-973661

M3 - Article

C2 - 9151316

AN - SCOPUS:0030739514

SN - 0174-304X

VL - 28

SP - 27

EP - 30

JO - Neuropediatrics

JF - Neuropediatrics

IS - 1

ER -

Palmitoyl-protein thioesterase and the molecular pathogenesis of infantile neuronal ceroid lipofuscinosis

Abstract

Keywords

ASJC Scopus subject areas

Access to Document

Other files and links

Fingerprint

Cite this