Developmental expression of the alpha-skeletal actin gene

BACKGROUND: Actin is a cytoskeletal protein which exerts a broad range of functions in almost all eukaryotic cells. In higher vertebrates, six primary actin isoforms can be distinguished: alpha-skeletal, alpha-cardiac, alpha-smooth muscle, gamma-smooth muscle, beta-cytoplasmic and gamma-cytoplasmic isoactin. Expression of these actin isoforms during vertebrate development is highly regulated in a temporal and tissue-specific manner, but the mechanisms and the specific differences are currently not well understood. All members of the actin multigene family are highly conserved, suggesting that there is a high selective pressure on these proteins. RESULTS: We present here a model for the evolution of the genomic organization of alpha-skeletal actin and by molecular modeling, illustrate the structural differences of actin proteins of different phyla. We further describe and compare alpha-skeletal actin expression in two developmental stages of five vertebrate species (mouse, chicken, snake, salamander and fish). Our findings confirm that alpha-skeletal actin is expressed in skeletal muscle and in the heart of all five species. In addition, we identify many novel non-muscular expression domains including several in the central nervous system. CONCLUSION: Our results show that the high sequence homology of alpha-skeletal actins is reflected by similarities of their 3 dimensional protein structures, as well as by conserved gene expression patterns during vertebrate development. Nonetheless, we find here important differences in 3D structures, in gene architectures and identify novel expression domains for this structural and functional important gene

Oncoplastic breast surgery: A guide to good practice

Oncoplastic Breast Surgery has become standard of care in the management of Breast. Cancer Patents. These guidelines written by an Expert Advisory Group; convened by the Association of Breast Surgery (ABS) and the British Association of Plastic, Reconstructive and Aesthetic Surgeons (BAPRAS), are designed to provide all members of the breast cancer multidisciplinary team (MDT) with guidance on the best breast surgical oncoplastic and reconstructive practice at each stage of a patient's journey, based on current evidence. It is hoped they will also be of benefit to the wide range of professionals and service commissioners who are involved in this area of clinical practice

Developmental expression of the alpha-skeletal actin gene

Abstract Background Actin is a cytoskeletal protein which exerts a broad range of functions in almost all eukaryotic cells. In higher vertebrates, six primary actin isoforms can be distinguished: alpha-skeletal, alpha-cardiac, alpha-smooth muscle, gamma-smooth muscle, beta-cytoplasmic and gamma-cytoplasmic isoactin. Expression of these actin isoforms during vertebrate development is highly regulated in a temporal and tissue-specific manner, but the mechanisms and the specific differences are currently not well understood. All members of the actin multigene family are highly conserved, suggesting that there is a high selective pressure on these proteins. Results We present here a model for the evolution of the genomic organization of alpha-skeletal actin and by molecular modeling, illustrate the structural differences of actin proteins of different phyla. We further describe and compare alpha-skeletal actin expression in two developmental stages of five vertebrate species (mouse, chicken, snake, salamander and fish). Our findings confirm that alpha-skeletal actin is expressed in skeletal muscle and in the heart of all five species. In addition, we identify many novel non-muscular expression domains including several in the central nervous system. Conclusion Our results show that the high sequence homology of alpha-skeletal actins is reflected by similarities of their 3 dimensional protein structures, as well as by conserved gene expression patterns during vertebrate development. Nonetheless, we find here important differences in 3D structures, in gene architectures and identify novel expression domains for this structural and functional important gene.</p

Residual breast tissue after mastectomy: how often and where is it located?

Background Residual breast tissue after a mastectomy can lead to a (second) primary breast cancer. The development of breast cancer after prophylactic mastectomy and the finding of normal breast tissue around a local recurrence support this assumption. The aim of the present study was to investigate the prevalence and localization of residual breast tissue after a mastectomy. Methods A series of 206 women who underwent a mastectomy between January 2008 and August 2009 in 11 hospitals were enrolled onto this study after written informed consent was obtained. From each mastectomy specimen, a total of 36 samples were obtained from the superficial dissection plane at predetermined locations. The biopsy samples were analyzed for the presence of benign breast tissue in the inked superficial area. Differences in percentage of positive samples were analyzed by generalized estimating equations to account for their interdependence. Results A total of 7,374 biopsy samples from 206 breast specimens of 206 patients were included in the analysis. In 76.2 % of the specimens (n = 157), one or more positive biopsy samples were found. The positive findings were found diffusely across the superficial dissection surface of the specimen with a significant predilection for the lower outer quadrant and the middle circle of the superficial dissection plane. Conclusions After a mastectomy, there is a high probability of residual breast tissue. This tissue is predominantly located in the middle circle of the superficial dissection plane and in the lower outer quadrant. Surgeons should be aware of these locations so they may remove as much of the benign breast tissue as possibl