Literature DB >> 2013821

Role of the Golgi apparatus in cellular pathology.

D M Morré1.   

Abstract

The Golgi apparatus response to pathological disorders is predominantly as an intermediary component of membrane biogenesis where it is involved in processing, sorting and secretion of materials via secretory granules, and in the formation of lysosomes. A common initial response of the Golgi apparatus to any stress is an alteration or cessation of secretory activity. In the transformed cell, the Golgi apparatus is altered both morphologically and biochemically, suggesting a shift from a secretory to a membrane-generating mode of functioning. However, since fewer or less well-developed Golgi apparatus are frequently found in transformed cells, analytical methods of membrane isolation developed for normal tissues may not always yield equivalent results when applied to tumors. Cell surface alterations characteristic of malignant cells may result from modifications occurring at the level of the Golgi apparatus. Some lysosomal dysfunctions may result from underglycosylation of acid hydrolases by the Golgi apparatus. The use of cell-free systems between endoplasmic reticulum and Golgi apparatus or within Golgi apparatus cisterane is providing a new approach to the elucidation of the role of the Golgi apparatus in normal as well as pathological states.

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Year:  1991        PMID: 2013821      PMCID: PMC7166452          DOI: 10.1002/jemt.1060170207

Source DB:  PubMed          Journal:  J Electron Microsc Tech        ISSN: 0741-0581


  133 in total

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3.  Recognition and receptor-mediated uptake of a lysosomal enzyme, alpha-l-iduronidase, by cultured human fibroblasts.

Authors:  G N Sando; E F Neufeld
Journal:  Cell       Date:  1977-11       Impact factor: 41.582

4.  Effect of reduced temperature on glycoprotein (Ig, HLA) processing and transport in lymphoid cells.

Authors:  M Brand; E Jansen; H L Ploegh
Journal:  Mol Immunol       Date:  1985-07       Impact factor: 4.407

5.  Uukuniemi virus maturation: immunofluorescence microscopy with monoclonal glycoprotein-specific antibodies.

Authors:  E Kuismanen; B Bång; M Hurme; R F Pettersson
Journal:  J Virol       Date:  1984-07       Impact factor: 5.103

6.  Evidence for extensive subcellular organization of asparagine-linked oligosaccharide processing and lysosomal enzyme phosphorylation.

Authors:  D E Goldberg; S Kornfeld
Journal:  J Biol Chem       Date:  1983-03-10       Impact factor: 5.157

7.  Effects of the ionophore monensin on type II collagen and proteoglycan synthesis and secretion by cultured chondrocytes.

Authors:  S K Nishimoto; T Kajiwara; P W Ledger; M L Tanzer
Journal:  J Biol Chem       Date:  1982-10-10       Impact factor: 5.157

8.  Unique glycoprotein-proteoglycan complex defined by monoclonal antibody on human melanoma cells.

Authors:  T F Bumol; R A Reisfeld
Journal:  Proc Natl Acad Sci U S A       Date:  1982-02       Impact factor: 11.205

9.  Processing of the phosphorylated recognition marker in lysosomal enzymes. Characterization and partial purification of a microsomal alpha-N-acetylglucosaminyl phosphodiesterase.

Authors:  A Waheed; A Hasilik; K von Figura
Journal:  J Biol Chem       Date:  1981-06-10       Impact factor: 5.157

10.  Fibroblast receptor for lysosomal enzymes mediates pinocytosis of multivalent phosphomannan fragment.

Authors:  H D Fischer; M Natowicz; W S Sly; R K Bretthauer
Journal:  J Cell Biol       Date:  1980-01       Impact factor: 10.539

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  1 in total

1.  Fragmentation of the Golgi apparatus of motor neurons in amyotrophic lateral sclerosis.

Authors:  N K Gonatas; A Stieber; Z Mourelatos; Y Chen; J O Gonatas; S H Appel; A P Hays; W F Hickey; J J Hauw
Journal:  Am J Pathol       Date:  1992-03       Impact factor: 4.307

  1 in total

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