ISSN:
1432-0878
Schlagwort(e):
Retinal pigment epithelium
;
Myeloid bodies
;
Diurnal variation
;
Morphometrics
;
Ultrastructure
;
Lipid metabolism
;
Endoplasmic reticulum
Quelle:
Springer Online Journal Archives 1860-2000
Thema:
Biologie
,
Medizin
Notizen:
Summary Myeloid bodies (MBs) occur in the newt (Notophthalmus viridescens) retinal pigment epithelium (RPE) and are similar to areas of specialized endoplasmic reticulum found in a variety of other cell types. The function of these structures is unknown, although a role in lipid metabolism has been strongly suggested. Random samples from conventionally-fixed and sectioned newt RPE, obtained over a 24-hr cycle (LD 12∶12), were examined by electron microscopy. Myeloid bodies appear as stacks of flattened endoplasmic reticulum-associated saccules which increase in length and number as the RPE accumulates shed outer segment material, prior to increase in the amount of stored lipid. Associations of MBs with the nuclear envelope can be related to this increased length. Myeloid bodies decrease numerically in the cell as phagosomes are removed from the cytoplasm, but a decrease in mean sectional MB area, seen in the light phase, is counteracted in darkness where individual MBs are larger than those found in the light. The total sectional area of MBs within a cell and their mean length varied depending on the lighting condition; differences were also found between eyes after extended periods of continuous light and dark. Ribosomes were found in association with the surfaces of both flattened and circular MBs, but they were consistently more densely associated with the shorter concave surfaces of curved regions. A new hypothesis for MB function is presented, which is concerned with their role in isolating toxic lipids such as retinoids, which are accumulated during phagocytosis of shed outer segment tips, and which are capable of disrupting membrane-bound systems necessary for their eventual metabolism and safe storage.
Materialart:
Digitale Medien
URL:
http://dx.doi.org/10.1007/BF00213738
Permalink
