Tissue-specific mitochondrial proteins

Vayssière, Jean-Luc; Cordeau, Laurence; Larcher, Jean Christophe; Gros, François; Croizat, Bernard

doi:10.1016/0300-9084(89)90041-2

Cited by 6 publications

(3 citation statements)

References 17 publications

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“…Some polypeptides were found specific to each tissue analyzed (see Table I). Similar observations were made in a comparative study of two-dimensional mitochondrial patterns of different rat organs (25), in which the authors point out the existence of a pool of mitochondrial proteins common to all organs studied, and of some polypeptides specific to each tissue analyzed, suggesting the existence of tissue-specific functions as well as the common mitochondrial function of ATP production. Figure 2 shows the partitioning of soluble and membrane polypeptides from tuber mitochondria: 77% of the spots revealed after silver staining belong to the soluble fraction and 23% to the membrane fraction.…”

Section: Variations Revealed By a High Resolution Two-dimensional Tecsupporting

confidence: 73%

Variation of the Polypeptide Composition of Mitochondria Isolated from Different Potato Tissues

Francs‐Small¹,

Ambard‐Bretteville²,

Darpas³

et al. 1992

Plant Physiol.

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The protein contents of mitochondria from different potato (Solanum tuberosum L.) tissues (tubers, dark-grown shoots, and green leaves) grown in a greenhouse or in vitro were compared by two-dimensional polyacrylamide gel electrophoresis. Two different methods were used: using the method that gave the highest resolution, an average number of 360 polypeptides was revealed on the mitochondrial pattems after silver staining. The mitochondrial protein patterns of etiolated tissues (tubers, darkgrown shoots) are roughly similar but distinct from those of green leaves. The four subunits of the glycine decarboxylase complex (involved in photorespiration) and a few other polypeptides are very abundant in green tissues, compared with nonphotosynthetic tissues. Conversely, some other polypeptides that are abundant in tubers and dark-grown shoots are hardly detectable in green leaf mitochondria. A rabbit antiserum was raised against a 40 kilodalton polypeptide that is among the most characteristic of these nonphotosynthetic tissue-specific polypeptides, and the Nterminal sequence of this polypeptide was determined. No effect of in vitro culture was observed on the protein composition of mitochondria isolated from differentiated tissues. However, the protein pattems of callus and cell suspension mitochondria are distinct from those of any differentiated tissues, although their basic pattem is clearly mitochondrial.

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Section: Variations Revealed By a High Resolution Two-dimensional Tecsupporting

confidence: 73%

Variation of the Polypeptide Composition of Mitochondria Isolated from Different Potato Tissues

Francs‐Small¹,

Ambard‐Bretteville²,

Darpas³

et al. 1992

Plant Physiol.

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“…It is thus not surprising that mitochondria found in various animal tissues show considerable differences in physiological activity, depending on the specific metabolic requirements [18]. In agreement with this statement, work from our laboratory has previously shown that mitochondriai proteins purified from various tissues and analyzed by 2-dimensional NEPHGE display a certain degree of tissue specificity [24]. Mitochondriai morphology also varies; the organelles are capable of changing their shape and size [18].…”

Section: Introductionmentioning

confidence: 70%

“…In a previous work, we described a neurospecific phenotype for mt-proteins from rat brain cortex, according to their electrophoretical behaviors [24].…”

Section: Introductionmentioning

confidence: 99%

Mitochondrial maturation during neuronal differentiation in vivo and in vitro

Cordeau-Lossouarn

Vayssière

Larcher

et al. 1991

Biology of the Cell

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The evolution of the mitochondrion has been followed within differentiating neuronal cells, both in primary cultures of neurons from fetal rat cortex and during rat brain cortex maturation. Changes in total mitochondrial proteins (mt-proteins) were evaluated, and qualitative changes in the mt-proteins pattern were analyzed using the Western blot technique. The evolution of mt-protein contents in cultured neurons resembles what is observed during rat brain maturation. The mitochondrion exhibits pronounced changes in the course of neurogenesis, in particular, bursts of mitochondrial masses accompanying the successive steps of neurogenesis are observed. There are indications that protein equipment of mitochondria during neuronal development undergoes variations. Although more work is required to establish the significance of these correlations, the present data might suggest an important role of the mitochondrion in neurogenesis.

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Tissue‐specific variation of pea mitochondrial polypeptides detected by computerized image analysis of two‐dimensional electrophoresis gels

et al. 1992

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A tissue-specific variation of a total of 152 mitochondria-associated polypeptides is detailed for etiolated leaves, epicotyls and roots from the pea, Pisum satisum L., using computerized image analysis. These organ systems possess, respectively, 128, 100, and 96 mitochondria-associated polypeptides with 38, 8, and 10, respectively, being unique to each. Seventy-one polypeptides were observed to be present in all gels, but some of these also underwent a variety of quantifiable changes. Two polypeptides were identified that varied similarly to a polypeptide of interest (W), known to be abundant in pea epicotyls and potato tubers. It is postulated that these latter three polypeptides are therefore probably related functionally.

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Tissue-specific mitochondrial proteins

Cited by 6 publications

References 17 publications

Variation of the Polypeptide Composition of Mitochondria Isolated from Different Potato Tissues

Variation of the Polypeptide Composition of Mitochondria Isolated from Different Potato Tissues

Mitochondrial maturation during neuronal differentiation in vivo and in vitro

Tissue‐specific variation of pea mitochondrial polypeptides detected by computerized image analysis of two‐dimensional electrophoresis gels

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