PubMed HealthSearch

PubMed · 3533736

[Breast reconstructions using a dermal fat flap].

Abstract

The popular breast reconstruction using a prosthetic implant has many disadvantages. Severe capsular contracture, for example, leads to breast deformities associated with pain. The development of many new types of prosthesis has not solved the fundamental problem. We therefore think it is better to reconstruct a female breast with a dermo-fat flap than a prosthesis. In this article we describe the indication and surgical techniques of our procedure to reconstruct a female breast.

Explore related subjects

Keep this discovery

Explore connections, maps & timelines

BibTeXRIS

J Schrudde. 1986. [Breast reconstructions using a dermal fat flap].. https://pubmed.ncbi.nlm.nih.gov/3533736/

Cite the original work for its findings. Save a collection to share your selection of sources.

KEEP EXPLORING

Related citations

The detection of breast microcalcifications with medical ultrasound.

Microcalcifications are small crystals of calcium apatites which form in human tissue through a number of mechanisms. The size, morphology, and distribution of microcalcifications are important indicators in the mammographic screening for and diagnosis of various carcinomas in the breast. Although x-ray mammography is currently the only accepted method for detecting microcalcifications, its efficacy in this regard can be reduced in the presence of dense parenchyma. Current ultrasound scanners do not reliably detect microcalcifications in the size range of clinical interest. The results of theoretical, simulation, and experimental studies focused on the improvement of the ultrasonic visualization of microcalcifications are presented. Methods for estimating the changes in microcalcification detection performance which result from changes in aperture geometry or the presence of an aberrator are presented. An analysis of the relative efficacy of spatial compounding and synthetic receive aperture geometries in the detection of microcalcifications is described. The impact of log compression of the detected image on visualization is discussed. Registered high resolution ultrasound and digital spot mammography images of microcalcifications in excised breast carcinoma tissue and results from the imaging of suspected microcalcifications in vivo are presented.

Breast

Comparison of O-linked carbohydrate chains in MUC-1 mucin from normal breast epithelial cell lines and breast carcinoma cell lines. Demonstration of simpler and fewer glycan chains in tumor cells.

MUC-1 mucin is considered to be aberrantly glycosylated in breast, ovary, and other carcinomas in comparison with mucin from corresponding normal tissues. In order to clarify these differences in glycosylation, we have compared the O-linked carbohydrate chains from MUC-1 immunoprecipitated from [3H]GlcN-labeled breast epithelial cell lines (MMSV1-1, MTSV1-7, and HB-2) derived from cells cultured from human milk, with three breast cancer cell lines (MCF-7, BT-20, and T47D). Analysis by high pH anion chromatography showed that the normal cell lines had a higher ratio of GlcN/GalN and more complex oligosaccharide profiles than the cancer cell lines. Structural analyses were carried out on the oligosaccharides from MTSV1-7 and T47D MUC-1, and the following structures were proposed. MUC-1 from T47D had rather a simple glycosylation pattern, with NeuAcalpha2-3Galbeta1-3GalNAc-ol, Galbeta1-3GalNAc-ol, and GalNAc-ol predominating; in contrast, MUC-1 from MTSV1-7 had more complex structures, including a number of disialo, core 2 species, i.e. NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-3]GalNAc- ol and NeuAcalpha2-3Galbeta1-4GlcNAcbeta1-6[NeuAcalpha2 -3Galbeta1-4GlcNAcbet a1-3Galbeta1-3]GalNAc-ol. Double-labeling experiments with [3H]GlcN and 14C-aminoacids and analysis of GalNAc or GalNAc-ol:protein ratios in MUC-1 showed that there was also a significant difference in the degree of glycosylation of the mucin between the two cell types. We conclude that MUC-1 from breast cancer cell lines has simpler, and fewer, carbohydrate chains than MUC-1 from normal breast epithelial cells, and that these differences, combined or separately, explain the differential tumor specificity of some MUC-1 antibodies and T cells.

Breast