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  • 1
    Electronic Resource
    Electronic Resource
    Autofluorescence emission spectra of neuronal lipopigment in animal and human ceroidoses (ceroid-lipofuscinoses) (1982)
    Springer
    Acta neuropathologica 58 (1982), S. 152-156 
    Details
    ISSN: 1432-0533
    Keywords: Aminal diseases ; Ceroid ; Lipofuscin
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary A method for the measurement of autofluorescence emission spectra of intraneuronal lipopigment in tissue sections has been applied to specimens from dogs and sheep with forms of neuronal ceroid-lipofuscinosis (NCL). The characteristics of an emission spectrum probably reflect the composition of the lipopigment, and the results are compared with those previously reported from human NCLs and lipofuscin in non-diseased elderly human brains. Lipopigment in the animal NCLs differed from lipofuscin in the non-diseased human brains, but no differences could be demonstrated between the spectra from animal and human NCLs. These findings support the use of the animal diseases as models for research into the pathogenesis and treatment of human NCLs. Both human and animal NCLs would be more accurately designated as the “ceroidoses”.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00691656
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  • 2
    Electronic Resource
    Electronic Resource
    Batten disease (ceroid-lipofuscinosis): The enigma of subunit c of mitochondrial ATP synthase accumulation (1995)
    Springer
    Neurochemical research 20 (1995), S. 1301-1304 
    Details
    ISSN: 1573-6903
    Keywords: Batten disease ; ceroid-lipofuscinosis ; neurodegeneration
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract Ceroid-lipofuscinosis is an inherited neurodegenerative disease of human beings and domestic animals characterized by the accumulation in neurons and other cells of a fluorescent lipopigment. In the ovine form of disease, subunit c of mitochondrial ATP synthase is the dominant accumulated metabolite (〉50%). It also accumulates significantly in the late infantile and juvenile forms of the human disease and several other animal forms. Evidence is accumulating that the underlying biochemical defect may be associated with mitochondria. The extreme hydrophobicity of subunit c and its propensity to aggregate with lipids into regular multilamellar arrays that cannot be catabolised may reflect an initial defect not necessarily associated with faulty proteolysis. This hypothesis extends an earlier one that subunit c accumulated due to a defect in its catabolic pathway.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00992504
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  • 3
    Electronic Resource
    Electronic Resource
    Ceroid, lipofuscin and the ceroid-lipofuscinoses (Batten Disease) (1993)
    Springer
    Journal of inherited metabolic disease 16 (1993), S. 280-283 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Conclusion The similar histochemical, fluorescent and ultrastructural appearance of some lipofuscins and the pigment of Batten disease imply some underlying common chemical feature. The similar chloroform—methanol solubility of the protein subunit c in Batten disease and the specific proteins accumulated in thyroid lipofuscin imply that disordered or delayed catabolism of hydrophobic protein may be that common feature.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00710265
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  • 4
    Electronic Resource
    Electronic Resource
    Round-table discussion of animal models of ceroid-lipofuscinosis (Batten Disease) (1993)
    Springer
    Journal of inherited metabolic disease 16 (1993), S. 278-279 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00710264
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  • 5
    Electronic Resource
    Electronic Resource
    Accumulation of sphingolipid activator proteins (SAPs) A and D in granular osmiophilic deposits in miniature Schnauzer dogs with ceroid-lipofuscinosis (1997)
    Springer
    Journal of inherited metabolic disease 20 (1997), S. 74-84 
    Details
    ISSN: 1573-2665
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The neuronal ceroid-lipofuscinoses (NCL, Batten disease) are fatal inherited neurodegenerative diseases of children characterized by retinal and brain atrophy and the accumulation of electron-dense storage bodies in cells. Mutations in different genes underlie different major forms. The infantile disease (CLN-1, McKusick 256730) is distinguished by the storage of the sphingolipid activator proteins (SAPs) A and D in distinctive granular osmiophilic deposits (GRODs). This contrasts with the other major forms, where subunit c of mitochondrial ATP synthase is stored in various multilamellar profiles. Ceroid-lipofuscinoses also occur in dogs, including a form in miniature Schnauzers with distinctive granular osmiophilic deposit-like storage bodies. Antisera to SAPs A and D reacted to these storage bodies in situ. The presence of SAP D was confirmed by Western blotting and of SAP A by protein sequencing. Neither subunit c of mitochondrial ATP synthase nor of vacuolar ATPase is stored. This suggests that there are two families of ceroid-lipofuscinoses, the subunit c-storing forms, and those in which SAPs A and D, and perhaps other proteins, accumulate. Further work is required to determine whether other forms with granular osmiophilic deposits belong to the latter class and the genetic relationships between them and the human infantile disease.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1023/A:1005365709340
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  • 6
    Electronic Resource
    Electronic Resource
    The subependymal plate and associated ependyma in the dog. An ultrastructural study (1972)
    Springer
    Journal of neurocytology 1 (1972), S. 69-84 
    Details
    ISSN: 1573-7381
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Summary The ultrastructural appearances of the ependyma and subependymal region in the anterior part of the caudate nucleus in the dog are described. The region in this species is more complex than that previously recorded in the rat. Ependymal cells have slender processes that contribute to the fibrillar layer. A small number of tanycytes were seen in all dogs examined. The subependymal cells, excluding microglia, can be divided into two groups, those with large pale nuclei and those with smaller darker nuclei. The latter group have undifferentiated cytoplasm, and is considered to be composed of subependymal plate cells. The group with large pale nuclei is composed of tanycytes, ectopic ependymal cells and astrocytes. It was often difficult to differentiate between cells within this group. Both types of subependymal cells were seen in mitosis. The fate of subependymal cells is discussed and it is concluded that a certain percentage diein situ while others may migrate either into the distant neuropil or form nests in the adjacent neuropil. The relationship between the subependymal plate cells and the pale nucleated cells is also discussed.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF01098647
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  • 7
    Electronic Resource
    Electronic Resource
    Bovine ceroid-lipofuscinosis (Batten's disease): The major component stored is the DCCD-reactive proteolipid, subunit c, of mitochondrial ATP synthase (1991)
    Springer
    Veterinary research communications 15 (1991), S. 85-94 
    Details
    ISSN: 1573-7446
    Keywords: ATP synthase ; cattle ; ceroid-lipofuscinosis ; lysosomes ; proteolipid ; subunit c
    Source: Springer Online Journal Archives 1860-2000
    Topics: Medicine
    Notes: Abstract The ceroid-lipofuscinoses (Batten's disease) are a group of recessively inherited lysosomal storage diseases of children and animals in which there is intracellular accumulation of a fluorescent lipopigment in a wide variety of cells. Lipopigment bodies isolated from pancreas, liver, kidney and brain tissue from a heifer affected with ceroid-lipofuscinosis contained between 55 and 62% protein. A dominant component comigrated on LDS-PAGE with the major low molecular weight protein stored in ovine ceroid-lipofuscinosis. It was identified by amino acid sequence and mass spectroscopy as the full subunit c of mitochondrial ATP synthase, normally found only in the inner mitochondrial membrane, where it is estimated to account for 2–4% of the membrane protein. In pancreatic lipopigment it accounted for at least 40% of the total lipopigment mass and this storage was considered specific to the disease. No other mitochondrial proteins were found in storage bodies. These results are similar to those found in studies on the ovine and the late infantile and juvenile human forms of the disease. It is concluded that bovine ceroid-lipofuscinosis is also a proteolipid proteinosis in which subunit c of mitochondrial ATP synthase is specifically stored in lysosome derived organelles.
    Type of Medium: Electronic Resource
    URL: http://dx.doi.org/10.1007/BF00405140
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