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D Goldschmidt

Publications and source records attributed to D Goldschmidt.

At least 55 records · Page 3Linked to original sources
PubMed1994

Anomalous blood supply to the serratus anterior muscle flap.

The serratus anterior free muscle flap is useful in lower limb reconstruction, as it combines a moderate quantity of muscle with a long vascular pedicle. There are known vascular anatomical variations, for example the blood supply may come from the thoracodorsal pedicle, directly from the subscapular pedicle or from the axillary artery and vein. We present a case with a totally independent arterial supply to the flap from the first intercostal artery, while venous return from the flap went back as usual to the subscapular pedicle.

Foot↗
PubMed1994

[Plexiform fibrohistiocytic tumor of the hand. Late form].

Plexiform fibrohistiocytic tumours are very rare, apparently benign neoplasms of the superficial soft tissue: only two series and one case report have been described in the literature. Macroscopically located within the dermis or superficial subcutis, they seem to predominate in the upper limbs of children and young adults. Moreover their recurrence rate is relatively high. We report the case of a 56 year old male patient presenting such a plexiform fibrohistiocytic tumour of the hand, which was surgically excised after a progressive clinical evolution of approximately 5 years and in which no recurrence has been observed with a follow-up of more than 24 months.

Follow-Up Studies↗
PubMed1993

Binding of collagen XIV with the dermatan sulfate side chain of decorin.

As an approach to elucidate the role of collagen XIV, which is still unclear, molecules exhibiting affinity for this collagen have been sought in connective tissue. Extracts from fetal bovine tendon were resolved by gel electrophoresis and electrophoretically transferred to nitrocellulose. The blot was overlaid with native collagen XIV and the collagen XIV-binding molecules revealed by immunodecoration with a monoclonal antitype XIV collagen antibody. This experimental approach allowed us to reveal in tendon extracts a diffuse band, with an apparent molecular mass of approximately 100 kDa, that binds collagen XIV. This molecule was also found associated with the fractions containing partially purified type XIV collagen. This 100-kDa molecule was sensitive to chondroitinase ABC and, after chondroitinase digestion, yielded a core protein of about 48 kDa. N-terminal sequence analysis of the proteoglycan after blotting allowed us to identify it as decorin. By solid phase assays we have studied this newly described association between decorin and type XIV collagen and shown that it is a saturable process. In addition, preliminary determination of the domains of the two molecules involved in the association has been performed. The possible role of these interactions is discussed.

Animals↗
PubMed1993

[Lipoma of the fingers].

Benign tumours of the hand are a common disease, usually corresponding to nodes. Other etiologies are less common. Lipomas of the hand are a rare feature, especially in the fingers. We present four cases of digital lipomas and a review of surgery of lipomas over the past ten years, and of the literature.

Adult↗
PubMed1992

Purification and characterization of native type XIV collagen.

A new molecule, type XIV collagen, with domains homologous to type IX and XII collagens has been recently discovered in pepsin extracts of fetal bovine tissues (Dublet, B., and van der Rest, M. (1991) J. Biol. Chem. 266, 6853-6858). In the present study, we describe the purification and the characterization of the intact native form of this newly discovered collagen. By using only two chromatographic steps we were able to obtain pure type XIV collagen. Furthermore, minor modifications of the protocol allowed us to perform the simultaneous large scale purification of type XII and type XIV collagens from the same tissue. Intact type XIV collagen migrates on sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) as two bands of 220 and 290 kDa (reducing conditions). After collagenase treatment, a single band of 190 kDa is observed, which represents the large non-collagenous domain of the molecule (NC3). Rotary shadowing electron micrographs of intact type XIV collagen show a cross-shaped structure formed by a thin tail attached through a central globule to three identical "fingers." These properties are similar to those previously described for intact chicken type XII collagen (Dublet, B., Oh, S., Sugrue, S. P., Gordon, M. K., Gerecke, D. R., Olsen, B. R., and van der Rest, M. (1989) J. Biol. Chem. 264, 13150-13156), but the two molecules are different gene products and have charge and glycosylation differences. Finally, we show that the three chains of purified type XIV collagen have an apparent molecular mass of approximately 220 kDa and are not cross-linked to each other by bonds other than disulfide bridges. The same observation was made for type XII collagen. In both cases, the 290-kDa migrating band in SDS-PAGE is due to incomplete denaturation in electrophoresis sample buffer in the absence of urea.

Animals↗
PubMed1991

A peptide-sensitive channel of large conductance is localized on mitochondrial outer membrane.

Applying the technique of 'tip-dip' to mitochondria, we have shown the existence in this organelle of a cationic channel of large conductance, which is blocked by a 13-residue peptide possessing the sequence of the N-terminal extremity of the cytochrome c oxidase subunit IV precursor. To study the submitochondrial localization of the channel, the effect of trypsin on isolated channels and on entire mitochondria were compared. One side of isolated channels is sensitive to trypsin, which eliminates the voltage dependence. Channels isolated from trypsinized mitochondria were devoid of voltage dependence and were blocked by the peptide. This suggests a localization of the channel on the outer membrane. Consistent with this hypothesis, the channel was observed with the highest frequency in outer membrane fractions purified by different procedures, either from bovine adrenal cortex or from rat liver mitochondria. Such a localization is also consistent with digitonin solubilization experiments. The channel was solubilized before the inner membrane marker, cytochrome c oxidase. The orientation of the channel was inferred from its trypsin sensitivity and its potential dependence: a transmembrane potential (inside negative) will close the channel.

Animals↗
PubMed1991

A 28 kDa mitochondrial protein is radiolabelled by crosslinking with a 125I-labelled presequence.

A 13-residue peptide containing the first 12 amino acids of the N-terminal part of the signal sequence of yeast cytochrome c oxidase subunit IV is shown by chemical crosslinking to interact with a mitochondrial protein. This result is obtained with mitochondria from four different origins. Submitochondrial localization experiments suggest that the 28 kDa labelled component is present on the outer face of the inner membrane. Since such addressing peptides are imported into mitochondria through the same machinery as protein precursors, the 28 kDa protein might be a component of the translocation apparatus.

Amino Acid Sequence↗
PubMed1989

Blockade of a mitochondrial cationic channel by an addressing peptide: an electrophysiological study.

A voltage-dependent cationic channel of large conductance is observed in phospholipid bilayers formed at the tip of microelectrodes from proteoliposomes derived from mitochondrial membranes. This channel was blocked by a 13-residue peptide with the sequence of the amino terminal extremity of the nuclear-coded subunit IV of cytochrome c oxidase. The blockade was reversible, voltage- and dose-dependent. The peptide did not affect the activity of a Torpedo chloride channel observed under the same conditions. From experiments with phospholipid monolayers, it is unlikely that the peptide inserts into bilayers under the experimental conditions used. The blockade was observed from both sides of the membrane, being characterized by more frequent transitions to the lower conductance states, and a maximum effect was observed around 0 mV. Channels, the gating mechanism of which had been eliminated by exposure to trypsin, were also blocked by the peptide. For trypsinized channels, the duration of the closure decreased and the blockade saturated at potentials below -30 mV. These observations are consistent with a translocation of the peptide through the channel. Dynorphin B, which has the same length and charge as the peptide, had some blocking activity. Introduction of negative charges in the peptide by succinylation suppressed the activity.

Amino Acid Sequence↗