@article{26d455842e8c4dfca31a48a63211478b,
title = "Aid to accurate clinical staging. Histopathologic grading in prostatic cancer",
abstract = "Recently, pathologic staging systems have been used to aid in accurate clinical assignment of prostatic disease. With this in mind, we reviewed retrospectively 130 patients who were diagnosed as having prostatic cancer either by needle biopsy or by study of transurethral resection chips. These specimens were graded by the Gleason and Roswell Park histopathologic grading systems. Grading was done by 2 pathologists independently and without knowledge of the results of final surgical staging. All patients were without evidence of metastases by standard diagnostic studies, and all underwent pelvic lymphadenectomy and radical prostatectomy if nodes were grossly negative. The surgical specimens were examined and the final clinical stage was correlated with the histopathologic grading. Independently, the Gleason rather than the Roswell Park system was slightly more accurate and was a more reliable predictor of the surgical stage of the disease. Of the patients with a Gleason sum of 7 or above 86% had at least stage C disease, whereas the disease had been staged preoperatively as A or B. All patients with a Gleason sum of 2 to 5 had stage A or B disease.",
author = "R. Thomas and Lewis, {R. W.} and Sarma, {D. P.} and Coker, {G. B.} and Rao, {M. K.} and Roberts, {J. A.}",
note = "Funding Information: hrombospondin (TSP), also known as glycoprotein G and as thrombin-sensitive protein, is a 500,000 dal-ton glycoprotein [1] originally isolated from platelets [2]. It is a trimer of identical 180 kD subunits. Initial T interest in this molecule stemmed from its role in thrombosis [3J, which is evidenced by the ability of polyclonal Manuscript reccived March 24, 1986; accepted for publication August 11 , 1986. During this investigation Dr. Wikner was a Fellow in Immunodermatology in the Departmcnt of Dermatology. University of Colorado School of Medici ne, Denver, Colorado and was supportcd by NIADDK grant AM 07411 . T his work was also supported by NIH grant AM 31514 to RAFC and a grant from the Monsanto Company to WAF. *This work was presented at the Annual Meeting of Thc Society for Investigative Dermatology, May 1986. Repri nt requests to: Richard A. F. Clark, M.D. , Department of Medicine, NationalJewish Center for Immunology and Respiratory Medicine, 1400 Jackson Street, Denver, Colorado 80206. Abbreviations: BPE: bovine pituitary extract CBB: Coomassie Brilliant Blue DOC: sodium deoxycholate ECM: extracellular matrix HK: human keratinocyte(s) IF: immunoAuorescence(-cent) NP-40: Nonidet P-40 PAS: protein A-Sepharosc PBS: phosphate-buffcred salinc SDS-PAGE: sodium dodecyl sulfate-polyacrylamidc gel electrophoresis TCA: trichloroacetic acid TSP: thrombospondin or monoclonal antibodies to TSP to block platelet aggregation [4]. Recently, however, evidence has accumulated leading to the perception that TSP has a much more diverse physiologic role. Thrombospondin has been detected in a variety of tissues by immunofluorescence microscopy [5]. In the kidney it is located in pcritubular conncctive tissue and in blood vessels. It is present in the luminal surface of the aorta, in the basement membranes of glandular areas of embryonic lung, and in the interstitium of skeletal muscle. In skin it is located at the epidermal-dermal junction and in the basement membrane zone of sweat glands, as well as around dermal blood vessels. Wight et al [5) suggest a nonhe'matogenous source for the TSP at these sites because many areas of positive staining are separated from blood vessels. More evidence for a tissue source of TSP is provided by in vitro data. Numerous cell types have been shown to synthesize and secrete TSP into their culture m edia. T hese include fi broblasts [6,7), endothelial cells (aortic [7,8], umbilical [9,10], and dermal microvascular cells (11)), type 1\ pneumocytes [12], smooth muscle cells (7), monocytes, and peritonealmacrophages [13). Moreover, several of these cells, including fibroblasts [6] and endothelial cells [9,11 J, deposit TSP into their extracellular matrix (ECM). During our study of the ECM of keratinocytes, we had of tell observed a major 180 kD protein which we had not identified [14]. This protein was present and labeled in both the medium and ECM of [35S]labeled human keratinocyte cultures and had the same molecular weight as the TSP subunit. Because of this and because of the published observation ofTSP in the epidermal basement membrane zone [5], we wished to establish whether keratinocytes in culture synthesize TSP.",
year = "1982",
doi = "10.1016/S0022-5347(17)53156-0",
language = "English (US)",
volume = "128",
pages = "726--728",
journal = "Unknown Journal",
issn = "0003-1348",
publisher = "JAI Press",
number = "4",
}
