Geometry.Net - Health_Conditions: Neuronal Ceroid Lipofuscinosis

REFERENCES [J. Biochem. Vol. 128, Pp. 509-516 (2000)]
5, 2126 Medline; Rider, JA, Dawson, G., and Siakotos, AN (1992) Perspective ofbiochemical research in the neuronal ceroid lipofuscinosis. Am. J. Med. Genet.
http://jb.bcasj.or.jp/128-3/3eyatprf.htm
JAX®Mice Database - Mouse/Human Gene Homologs: Infantile Neuronal Ceroid Lipofu
JAX®MICE Database Mouse/Human Gene HomologsInfantile neuronal ceroid lipofuscinosis List.
http://jaxmice.jax.org/jaxmicedb/html/model_1567.shtml
SUP: July 1998 Case Of The Month
Diagnosis neuronal ceroid lipofuscinosis, late infantile type. Discussion GoebelHH, Morphologic Diagnosis in neuronal ceroid lipofuscinosis.
http://sup.ultrakohl.com/Cases98/Jul98/jul98p2.htm

Extractions: Reader Feedback Diagnosis: Neuronal ceroid lipofuscinosis, late infantile type Discussion: The neuronal ceroid lipofuscinoses are a group of progressive encephalopathies which are inherited in an autosomal recessive manner. Four main types are recognized: infantile, late infantile, juvenile and adult. Morphologically they are characterized by widespread accumulation of autofluorescent lipopigments inside and outside the central nervous system. In the infantile type the lipopigments are granular. The late infantile type shows characteristic curvilinear profiles. Fingerprint profiles are seen in the classical juvenile type while the adult type can be somewhat variable showing granular material and/or fingerprint profiles. Many cell types contain the abnormal inclusions including endothelial cells and amniotic fluid cells. This has allowed for prenatal diagnosis in some subtypes by ultrastructural examination of uncultured amniotic cells (late infantile type) and endothelial cells of biopsied chorionic stromal vessels (infantile type) (1). Immunohistochemical studies have shown the accumulation of the subunit C of mitochondrial ATPase in the late infantile, juvenile and occassionally the adult type. Accumulation of sphingolipid activator proteins saposins A and D has been shown in the infantile type and to a lesser degree in the other subtypes (2).
Ntsad's What Every Family Should Know: The Allied Diseases Profiled
Back to top. 4) Other lysosomal storage disorders. Batten Disease (Juvenileneuronal ceroid lipofuscinosis), Unknown, 204200, Yes, ? 16, AR.
http://www.ntsad.org/pages/ntsad.htm

Extractions: The Allied Diseases Profiled TAY-SACHS AND THE ALLIED DISEASES ARE GENETIC CONDITIONS CLASSIFIED as storage diseases. They are caused by the abnormal accumulation, or storage, of certain waste products in the cells or tissues of affected individuals. As these products build up, cells become damaged and gradually lose their ability to function properly, causing disease symptoms. While the specific clinical courses of these related disorders differ, there are certain commonalities, and children and adults affected with Tay-Sachs or any of the allied diseases share many issues associated with chronic, progressive illness. T he chart below provides a quick reference for the major characteristics of the allied diseases. Underlined words are links to more information on this site or elsewhere on the Internet. The Omim # refers to the catalogue citation on the Online Mendelian Inheritance In Man , the hypertext version of Victor McCusick's landmark catalogue of human genetic disease. A dditionally, the following Allied Diseases are profiled in more depth in their own sections: T his information is provided in response to a growing demand for knowledge and in the hopes of increasing awareness and understanding of these rare, but often devastating, diseases.
Error Page
neuronal ceroid lipofuscinosis encompasses a family of neurodegenerative diseasescharacterized by the accumulation of autofluorescent lipopigments, mainly in
http://www.orpha.net/consor/cgi-bin/OC_Exp.php?Lng=GB&Expert=216
What's Your Diagnosis?
Diagnosis neuronal ceroid lipofuscinosis. A timely diagnosis of late infantileand juvenile neuronal ceroid lipofuscinosis is important for family.
http://www.kfshrc.edu.sa/annals/196/98-308A.html

Extractions: Editors: Husn Frayha, MD, and Mansour Al Nozha, FRCP WHAT'S YOUR DIAGNOSIS? Submitted by Oluwole Ogunmekan, MD, FRCP(Lond), DCh; Ali Said Dammas, MD, DCh, Fachartz FIGURE 1. Brain MRI of the patient. FIGURE 2. Electron photomicrograph of a peripheral blood lymphocyte of the patient. History Physical examination showed a severely mentally retarded child, with lack of awareness of his surroundings, drooling of saliva, and occasional myoclonic jerks. He had generalized hyperspasticity and multiple contractures, and could not stand or walk. His plantar responses were equivocal. He had bilaterally optic atrophy. All routine laboratory investigations were normal. Electroencephalogram showed excess slow waves, with interictal record of polyspikes, and spike slow waves bisynchronously. MRI of the brain (figure 1) and an electron microscopic photomicrograph of a peripheral blood lymphocyte of the patient are shown (Figure 2). What abnormalities are seen in Figure 1? What abnormalities are seen in Figure 2? What is the diagnosis? ANSWER TO WHAT'S YOUR DIAGNOSIS? (PREVIOUS PAGE)
Literature For Peptidase S53.003
2000; BerryKravis,E., Sleat,DE, Sohar,I., Meyer,P., Donnelly,R. Lobel,P. (2000)Prenatal testing for late infantile neuronal ceroid lipofuscinosis. Ann.
http://meropslinks.iapc.bbsrc.ac.uk/MeropsLinks/Lit/S53p003_Lit.htm
NPI Listing For Leena Peltonen, M.D., Ph.D.
Rapola J, Santavuori P, Hofmann SL and Peltonen L (1995) Mutations in the palmitoylprotein thioesterase gene causing infantile neuronal ceroid lipofuscinosis.
http://directory.neuropsychiatricinstitute.org/cgi-bin/showfaculty?4
16 Neuronal Ceroid Lipofuscinosis A Novel Gene (CLN8) Is
neuronal ceroid lipofuscinosis A novel gene (CLN8) is mutated in human progressiveepilepsy with mental retardation and the motor neuron degeneration mouse
http://www.faseb.org/genetics/ashg99/f16.htm
Untitled Document
Mutations in the palmitoylprotein thioesterase gene (PPT; CLN1) causing juvenileneuronal ceroid lipofuscinosis with granular osmiophilic deposits (abstract).
http://www.ucl.ac.uk/paediatrics/97-98_Publications.htm

Extractions: Departmental Publications Amess P. N., Penrice J., Howards S., Thoresen M., Edwards A.D., Cady E.B., Wyatt J.S., Sams V. (1998). Organ pathology following mild hypothermia used as neural rescue therapy in newborn piglets. Biology of the Neonate Annals of the New York Academy of Sciences Cribbs L. L., Lee J-H., Yang J., Satin J., Zhange D., Barcley J., Williamson M.P., Fox M., Rees M., Perez-Reyes E. (1998). Cloning and characterization of alpha1H from human heart, a member of the T-type Ca2+ channel gene family. Circulation Research Edwards A.D., Wyatt J.S., Thoresen M. (1998). Treatment of hypoxic-ischaemic brain damage by moderate hypothermia. Archives of Disease in Childhood Goebel H.H., Sharp J.D. (1998). The Neuronal Ceroid-Lipofuscinoses. Recent Advances. Brain Pathology Greene N.D.E., Bernard D.L., Mole S.E., Gardiner R.M., Nussbaum R.L., Mitchison H.M., Taschner P.E.M., de Vos N., Breuning M.H. (1998). Progress towards development of mouse models for JNCL. (abstract). European Journal of Paediatric Neurology Greene N.D.E., Gerelli D., Van Straaten H.W.M., Copp A.J. (1998). Abnormalities of floor plate, notochord and somite differentation in the loop-tail (Lp) mouse: a model of severe neural tube defects.
Center For Advanced Biotechnology And Medicine: Faculty & Research
Lysosomal storage disorders, neuronal ceroid lipofuscinosis, NiemannPick disease, proteomics, mannose 6phosphate receptors. Our
http://faculty.umdnj.edu/cabm/faculty_lobel.asp

Extractions: lobel@cabm.rutgers.edu Our laboratory has developed new methods for disease discovery and identified the molecular bases for three fatal neurodegenerative disorders. This work grew out of our basic research on lysosomal enzyme targeting. In addition to their roles in human inherited diseases, alterations in the lysosomal system have been implicated in a variety of disease processes such as tumor invasion and metastasis in cancer, tissue destruction in arthritis, and early changes associated with Alzheimer disease. Once we develop the tools to visualize and characterize the players, our ultimate goal will be to understand the role that lysosomal proteins play in these widespread pathological processes. Identification of a lysosomal protein deficient in a hereditary human neurodegenerative disease. Specimens from an unaffected control and a child diagnosed with late infantile neuronal ceroid lipofuscinosis were fractionated by two dimensional gel electrophoresis, transferred to a membrane, and probed with radiolabeled mannose 6-phosphate receptor. This revealed the absence of a specific protein in the disease specimen and lead to the identification of the molecular basis of the disease.
Search By Disease
58 neuronal ceroid lipofuscinosis, adult type (NCL). 59 Neuronalceroid lipofuscinosis, finnish variant, late infantile type (NCL).
http://www.eddnal.com/directory/disease.php?letter=N&page=4
Peter Lobel
In this manner, we found that a fatal childhood neurodegenerative disease calledLINCL (late infantile neuronal ceroid lipofuscinosis) is caused by mutations
http://www2.umdnj.edu/~pharm/pharmdep/faculty/plobel/plobel.htm

Extractions: Our laboratory has developed new methods for disease discovery and identified the molecular bases for three fatal neurodegenerative disorders. This work grew out of our basic research on lysosomal enzyme targeting. LINCL is literally a disease from hell, as parents see what has been a normally developing child degenerate before their eyes. Children typically develop normally until age 3 at which point they exhibit ataxia and seizures. They start losing vision a year later, and within a few years are blind, mute, and completely bedridden. The children usually die between ages eight and fifteen, although there are some mutations that result in a later-onset, prolonged disease. At the cellular level there is extensive lysosomal accumulation of autofluorescent storage material (ceroid lipofuscin) accompanied by massive death of neurons and marked brain atrophy. About fifty children are diagnosed with LINCL each year in the United States and the disease has devastating effects on the affected children and families. While our laboratory primarily conducts basic research, our interactions with many LINCL families have given us added impetus to extend our research to the clinic. After we identified the gene and determined the function of corresponding protein, we developed rapid biochemical and DNA-based assays for definitive pre-and postnatal diagnosis and carrier screening. This allows for genetic counseling to prevent further occurrence of the disease. However, in the absence of universal carrier testing, new cases will continue to arise so it is important to develop effective therapies that can halt and reverse disease progression. To this end, we have produced recombinant enzyme in a form that can be taken up by affected cells in culture to correct the primary defect. We are also working to develop a LINCL mouse model that should allow detailed studies of disease pathophysiology and evaluation of potential therapeutics strategies.
Patricia B. Munroe
Delayed classic and protracted phenotypes of compound heterozygous juvenileneuronal ceroid lipofuscinosis. Neurology 1999;52(2)3605.
http://www.mds.qmw.ac.uk/clinpharm/munroe.html
Peter Lobel
lysosomal storage disorders of unknown etiology and have used these to identify thedisease genes in late infantile neuronal ceroid lipofuscinosis (LINCL) and
http://lifesci.rutgers.edu/~molbiosci/Professors/lobel.html

Extractions: lobel@cabm.rutgers.edu Our laboratory studies lysosomes and associated human. Lysosomes are organelles found in all eukaryotic cells that contain many different proteases, glycosidases, lipases and other hydrolytic enzymes. The lysosome functions as the cell's recycling compartment, breaking down complex biological macromolecules into simple components. The importance of these organelles is underscored by the existence of over thirty human genetic disorders (e.g., Tay-Sachs disease) where loss of function of a single lysosomal enzyme can lead to severe health problems including neurodegeneration, progressive mental retardation, and early death. 1. Disease discovery. Our laboratory has pioneered novel protein-based approaches to identify the molecular basis for lysosomal storage disorders of unknown etiology and have used these to identify the disease genes in late infantile neuronal ceroid lipofuscinosis (LINCL) and Niemann-Pick Type C2 disease NPC2). We are currently using this and other approaches to determine the causes of other hereditary lysosomal diseases. 2. Medical applications. One tragic aspect of lysosomal neurodegenerative diseases is that they are often misdiagnosed and families can spend years trying to determine the cause of their child's progressive decline. Our laboratory has developed DNA and enzyme based assays for LINCL that allow carrier screening, diagnosis, and prenatal testing. In addition, we are developing knockout mice to produce small animal models for LINCL and NPC2 that will allow detailed studies of disease pathophysiology and evaluation of neuroprotective, enzyme replacement, and gene therapies.
Diseases Database Disease, Symptom, Sign, Etc Alphabetical Index : N Diseases Da
infantile see Ceroid lipofuscinosis, neuronal 1, infantile neuronal ceroid lipofuscinosisFinnish variant, late infantile see Ceroid lipofuscinosis, neuronal 5
http://www.diseasesdatabase.com/sieve/disease_index_n.asp
Diseases Database Disease, Symptom, Sign, Etc Alphabetical Index : J Diseases Da
colonic polyposis Juvenile nephronophthisis with Leber amaurosis see Loken Seniorsyndrome Juvenile neuronal ceroid lipofuscinosis see Ceroid lipofuscinosis
http://www.diseasesdatabase.com/sieve/disease_index_j.asp
MGH Neurogenetics DNA Diagnostic Laboratory
Hyperkalemic Periodic Paralysis (HYPP); Infantile neuronal ceroid lipofuscinosis(INCL, CLN1); Late Infantile neuronal ceroid lipofuscinosis
http://neuro-oas.mgh.harvard.edu/neurogenetics/

Extractions: We are a clinical service laboratory offering molecular DNA diagnostic testing for neurogenetic disorders. Some of our test protocols have been developed directly from the Massachusetts General Hospital (MGH) research laboratories actively working in these areas. We maintain a close working affiliation with these laboratories so that our technology and interpretation is the most up-to-date. We work with professionals to assist patients in obtaining accurate and useful DNA mutational analysis. Consultation by telephone or email is provided to referring physicians and genetic counselors as well as to patients and their families. Genetic counseling can be provided in our affiliated MGH Developmental Neurogenetics Clinic.
Biochem. J. (2001) 357, 49-55 - L. Lin And P. Lobel - Recombinant Human CLN2 Pro
Production and characterization of recombinant human CLN2 protein for enzymereplacementtherapy in late infantile neuronal ceroid lipofuscinosis.
http://www.biochemj.org/bj/357/bj3570049.htm

Extractions: Key words: endocytosis, lysosomal storage, overexpression, tripeptidyl peptidase I. Abbreviations used: LINCL, late infantile neuronal ceroid lipofuscinosis; TPP-I, tripeptidyl peptidase I; CLN2p, CLN2 ( c eroid l ipofuscinosis, n euronal 2) protein; LAMP, lysosome-associated membrane protein; 4-MU, 4-methylumbelliferyl; MTX, methotrexate; Man-6- P , mannose 6-phosphate; MPR, Man-6- P receptor; subunit c, mitochondrial ATP synthase subunit c; CHO, Chinese-hamster ovary; DME, Dulbecco's modified Eagle's; FBS, fetal-bovine serum. Late infantile neuronal ceroid lipofuscinosis (LINCL) is a fatal recessive childhood disease caused by mutations in the gene, which encodes the lysosomal enzyme tripeptidyl peptidase I. As a step towards understanding the protein and developing therapeutics for the disease, we have produced and characterized recombinant human CLN2 ( eroid ipofuscinosis
Biochem. J. (2003) 369, 55-62 - S. Partanen And Others - Intracellular Transport
1, D35033 Marburg, Germany. Key words fluorimetric substrate, lysosomalstorage, neuronal ceroid lipofuscinosis, overexpression.
http://www.biochemj.org/bj/369/bj3690055.htm

Extractions: Key words: fluorimetric substrate, lysosomal storage, neuronal ceroid lipofuscinosis, overexpression. Abbreviations used: AMCA-Hb, 6-[(7-amino-4-methylcoumarin-3-acetyl)amino]hexoid acid coupled to haemoglobin; CHO, Chinese hamster ovary; CONCL, congenital ovine NCL; CTSD, cathepsin D; DMEM, Dulbecco's modified Eagle's medium; hCTSD, human CTSD; mCTSD, mouse CTSD; M6P, mannose 6-phosphate; NCL, neuronal ceroid lipofuscinosis; PDI, protein disulphide isomerase. Received 5 August 2002/17 September 2002; accepted 26 September 2002 Published as BJ Immediate Publication 26 September 2002, DOI 10.1042/BJ20021226

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