Mitochondrial Differentiation During Animal Development

Boell, E. J.; Greenfield, Phyllis

doi:10.1016/b978-0-12-740603-9.50015-2

Cited by 3 publications

(4 citation statements)

References 209 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…For SDH , the rapid postnatal increase in activity has been observed in mitochondrial fraction studies (27) and in homogenates ( 28), but we demonstrated in addition that its increase was synchronous in both zones so that the ratio of periportal to perivenular activities was similar from day I onward. On histochemical reaction, the SDH gradient of distribution was observed from the 2nd week of life in neonate rats (28).…”

Section: Microsomal Enzymessupporting

confidence: 63%

Developmental Changes in the Intra‐acinar Distribution of Succinate Dehydrogenase, Glutamate Dehydrogenase, Glucose‐6‐Phosphatase, and NADPH Dehydrogenase in the Rat Liver

Sokal,

Trivedi,

Portmann

et al. 1989

J. pediatr. gastroenterol. nutr.

View full text Add to dashboard Cite

SummaryHepatocytes differ in their metabolism depending on their position in the liver acinus. To assess how such specialization changes during development, we used quantitative cytochemistry to measure succinate dehydrogenase (SDH), glutamate dehydrogenase (GDH), glucose‐6‐phosphatase (G6P), and NADPH dehydrogenase (ND) activities specifically in periportal and perivenular hepatocytes in developing rats, aged between 1–114 days. Important and distinct changes were observed in each zone for each enzyme during development. An intraacinar gradient of distribution was present from day 1 for SDH and G6P and from day 5 for GDH and ND. It was being similar to the adult value for SDH but less pronounced for the remaining enzymes. The SDH and G6P activity was greater in periportal cells, and the GDH and ND activity was greater in perivenular cells. The more pronounced distribution with age was due, for G6P, to an initial specific periportal increase combined with a mild perivenular decrease and for GDH to a greater perivenular than periportal increase. The ND first increased simultaneously in both zones, but from day 20 the perivenular increase became prevalent. The SDH changes were parallel in both zones. All zonal enzyme activities changed distinctly after weaning. To what extent the changes in activities and metabolic zonation observed in our study reflect a response to specific metabolic demands of the liver or can be modified by environmental factors remains to be investigated.

show abstract

Section: Microsomal Enzymessupporting

confidence: 63%

Developmental Changes in the Intra‐acinar Distribution of Succinate Dehydrogenase, Glutamate Dehydrogenase, Glucose‐6‐Phosphatase, and NADPH Dehydrogenase in the Rat Liver

Sokal,

Trivedi,

Portmann

et al. 1989

J. pediatr. gastroenterol. nutr.

View full text Add to dashboard Cite

show abstract

“…Mitochondria in rat hepatocytes exhibit heterogeneity in both size and morphology, conditions which are considered to reflect differences in respiratory state and biosynthetic activity (for recent reviews, see references 4,21). It is possible that such differences may correspond to different topographical positions of mitochondria within the cell, particularly as this pertains to associations of mitochondria with different organelles.…”

mentioning

confidence: 99%

Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria.

Shore¹,

Tata²

1977

The Journal of Cell Biology

166

View full text Add to dashboard Cite

Low-speed centrifugation (640 g) of rat liver homogenates, prepared with a standard ionic medium, yielded a pellet from which a rapidly sedimenting fraction of rough endoplasmic reticulum (RSER) was recovered free of nuclei. This fraction contained 20-25% of cellular RNA and approximately 30% of total glucose-6-phosphatase (ER marker) activity. A major portion of total cytochrome c oxidase (mitochondrial marker) activity was also recovered in this fraction, with the remainder sedimenting between 640 and 6,000 g. Evidence is provided which indicates that RSER may be intimately associated with mitochondria. Complete dissociation of ER from mitochondria in the RSER fraction required very harsh conditions. Sucrose density gradient centrifugation analysis revealed that 95% dissociation could be achieved when the RSER fraction was first resuspended in buffer containing 500 mM KC1 and 20 mM EDTA, and subjected to shearing. Excluding KCI, EDTA, or shearing from the procedure resulted in incomplete separation.Both electron microscopy and marker enzyme analysis of mitochondria purified by this procedure indicated that some structural damage and leakage of proteins from matrix and intermembrane compartments had occurred. Nevertheless, when mitochondria from RSER and postnuclear 6,000-g pellet fractions were purified in this way from animals injected with [asS]methionine _ cycloheximide, mitochondria from the postnuclear 6,000-g pellet were found to incorporate approximately two times more cytoplasmically synthesized radioactive protein per milligram mitochondrial protein (or per unit cytochrome c oxidase activity) than did mitochondria from the RSER fraction. Mitochondria-RSER associations, therefore, do not appear to facilitate enhanced incorporation of mitochondrial proteins which are newly synthesized in the cytoplasm.

show abstract

“…By comparing the activity of enzymes from different compartments in mitochondria isolated from segmenting eggs and larvae (stage [30][31][32][33][34][35] it is apparent that the activities have changed unevenly, giving the mitochondria in the two stages different properties. The most dramatic changes occur over a relatively short period of time, during gastrulation and neurulation.…”

Section: Discussionmentioning

confidence: 99%

“…The enzyme content is, according to BOELL and GREENFIELD (32), the single most informative index of mitochondrial differentiation. "Mitochondria differentiate when the relative amounts of enzymes change within them"…”

Section: Discussionmentioning

confidence: 99%

Changes in Activity of Mitochondrial Enzymes during the Development of Xenopus laevis

Nelson

Løvtrup-Rein

1983

Dev Growth Differ

View full text Add to dashboard Cite

Changes in activity of mitochondrial enzymes were studied during the embryonic development of Xenopus laevis.The following enzymes were determined: malate dehydrogenase (MDH), isocitrate dehydrogenase (NAD+-dependent) (IDH), aspartate aminotransferase (GOT), cytochrome oxidase (COX), succinate dehydrogenase (SDH), rotenone-insensitive NADH cytochrome c reductase (NADH-red) and monoamine oxidase (MAO). IDH is constant throughout the period studied. COX and SDH, two enzymes of the inner membrane, are constant in pregastrula stages, and subsequently decrease significantly. MDH and NADH-red are highly active in the pregastrula stages and decline thereafter, while M A 0 is undetectable during early development and increases significantly only in the larvae. GOT increases during the cleavage stages, being most active in the gastrula stages, and decreases subsequently.The results are discussed in the sense of mitochondrial differentiation during the early development of the amphibian embryo.

show abstract

Mitochondrial Differentiation During Animal Development

Cited by 3 publications

References 209 publications

Developmental Changes in the Intra‐acinar Distribution of Succinate Dehydrogenase, Glutamate Dehydrogenase, Glucose‐6‐Phosphatase, and NADPH Dehydrogenase in the Rat Liver

Developmental Changes in the Intra‐acinar Distribution of Succinate Dehydrogenase, Glutamate Dehydrogenase, Glucose‐6‐Phosphatase, and NADPH Dehydrogenase in the Rat Liver

Two fractions of rough endoplasmic reticulum from rat liver. I. Recovery of rapidly sedimenting endoplasmic reticulum in association with mitochondria.

Changes in Activity of Mitochondrial Enzymes during the Development of Xenopus laevis

Contact Info

Product

Resources

About