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Xylosylated-proteoglycan-induced Golgi alterations.
Summary
p-nitrophenyl beta-D-xylopyranoside disrupts proteoglycan (PG) synthesis in kidney cells. This leads to Golgi apparatus changes and an imbalance of PGs between cellular and extracellular compartments.
Area of Science:
- Renal physiology
- Cell biology
- Biochemistry
Background:
- Proteoglycans (PGs) are crucial components of the glomerular extracellular matrix.
- The Golgi apparatus is central to PG synthesis and modification.
- Disruptions in PG synthesis can impact kidney function.
Purpose of the Study:
- To investigate the effects of p-nitrophenyl beta-D-xylopyranoside (beta-xyloside) on Golgi apparatus and proteoglycans in the renal glomerulus.
- To understand the cellular and extracellular distribution of newly synthesized PGs under beta-xyloside treatment.
Main Methods:
- Isolated kidney organ perfusion system.
- [35S]sulfate labeling to trace PG synthesis.
- Electron microscopy and autoradiography to visualize cellular and extracellular changes.
- Biochemical analysis of PG molecular weight and distribution.
Main Results:
- Beta-xyloside induced intracytoplasmic vesiculization of the Golgi apparatus in glomerular visceral epithelial cells.
- [35S]sulfate incorporation increased intracellularly (2.3-fold) and decreased extracellularly (1.7-fold).
- Lower molecular weight PGs and free glycosaminoglycans accumulated intracellularly and in the media.
- A significant increase (3.8-fold) in radioactivity was observed in the media fraction, associated with small PGs and glycosaminoglycans.
Conclusions:
- Beta-xyloside causes a significant imbalance in de novo PG synthesis between cellular and extracellular compartments.
- Accumulation of xylosylated PGs within cells selectively alters the Golgi apparatus of glomerular epithelial cells.
- These findings highlight the critical role of glomerular epithelial cells in PG synthesis and the impact of altered synthesis on cellular structures.