TY - JOUR
T1 - Evidence of microfilament-associated mitochondrial movement
AU - Bradley, T. J.
AU - Satir, P.
PY - 1979
Y1 - 1979
N2 - The mitochondria in the lower Malpighian tubule of the insect Rhodnius prolixus can be stimulated by feeding in vivo and by 5-hydroxytryptamine in vitro, to move from a position below the cell cortex to one inside the apical microvilli. During and following their movement into the microvilli, the mitochondria are intimately associated with the microfilaments of the cell cortex and microvillar core bundle. Bridges approximately 14 nm in length and 4 nm in diameter are observed connecting the microvillar microfilaments to the outer mitochondrial membrane and microvillar plasma membrane. Depolymerization of all visible microtubules with colchicine does not inhibit 5-HT-stimulated mitochondrial movement. On the other hand, treatment with cytochalasin B does block mitochondrial movement, suggesting that microfilaments play a role in the mitochondrial motility. We have labeled the microvillar microfilaments, which are 6 nm in diameter, with heavy meromyosin, which supports the contention that they contain actin. A model of the mechanism of mitochondrial movement is presented in which mitochondria slide into position in the microvilli along actin-containing microfilaments in a manner analogous to the sliding actin-myosin model of skeletal muscle.
AB - The mitochondria in the lower Malpighian tubule of the insect Rhodnius prolixus can be stimulated by feeding in vivo and by 5-hydroxytryptamine in vitro, to move from a position below the cell cortex to one inside the apical microvilli. During and following their movement into the microvilli, the mitochondria are intimately associated with the microfilaments of the cell cortex and microvillar core bundle. Bridges approximately 14 nm in length and 4 nm in diameter are observed connecting the microvillar microfilaments to the outer mitochondrial membrane and microvillar plasma membrane. Depolymerization of all visible microtubules with colchicine does not inhibit 5-HT-stimulated mitochondrial movement. On the other hand, treatment with cytochalasin B does block mitochondrial movement, suggesting that microfilaments play a role in the mitochondrial motility. We have labeled the microvillar microfilaments, which are 6 nm in diameter, with heavy meromyosin, which supports the contention that they contain actin. A model of the mechanism of mitochondrial movement is presented in which mitochondria slide into position in the microvilli along actin-containing microfilaments in a manner analogous to the sliding actin-myosin model of skeletal muscle.
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U2 - 10.1002/jss.400120203
DO - 10.1002/jss.400120203
M3 - Article
C2 - 397369
AN - SCOPUS:0018572327
SN - 0730-2312
VL - 12
SP - 165
EP - 175
JO - Journal of supramolecular structure and cellular biochemistry
JF - Journal of supramolecular structure and cellular biochemistry
IS - 2
ER -