Synovial sarcoma--a misnomer.
PDF (2.3M)
Journal: 1984/November - American Journal of Pathology
ISSN: 0002-9440
PUBMED: 6207733
Abstract:
For an evaluation of the putative histogenetic relationship of synovia and synovial sarcomas, normal synovia, villonodular synovitis, and synovial sarcomas were compared for their patterns of expression of intermediate filaments of keratin and vimentin type and epithelial membrane antigen and for lectin binding sites. The lining cells in both normal synovia and villonodular synovitis reacted with anti-vimentin antibodies, but not with antibodies to different types of keratins or epithelial membrane antigen. The cleft-lining cells in synovial sarcoma, on the other hand, showed only keratin positivity, and epithelial membrane antigen could also be detected in these cells. Nonneoplastic synovial lining cells bound peanut agglutinin (PNA), Ricinus communis agglutinin (RCA), soybean agglutinin (SBA), concanavalin A (Con A), and wheat germ agglutinin (WGA) conjugates, but not Ulex europaeus I lectin (UEA I). In contrast, the epithelial-like cleft lining cells in synovial sarcomas showed an apical cytoplasmic binding of PNA, UEA I, RCA, and SBA, and binding of WGA to the whole cytoplasm but did not bind Con A. The distinct differences between synovial lining cells and synovial sarcoma cells speak against synovial cell features in synovial sarcoma. These results indicate that synovial sarcoma is a carcinosarcomalike tumor with true epithelial differentiation, and the term "synovial sarcoma" apparently is a misnomer that should be abandoned.
Open in
PUBMED | PMC | Google Scholar | Wikipedia
Relations:
Content
Citations
(23)
References
(59)
Diseases
(3)
Chemicals
(7)
Organisms
(1)
Processes
(1)
Anatomy
(2)
Similar articles
Articles by the same authors
Discussion board
Am J Pathol 117(1): 18-25
PMID: 6207733

Synovial sarcoma--a misnomer.

Abstract

For an evaluation of the putative histogenetic relationship of synovia and synovial sarcomas, normal synovia, villonodular synovitis, and synovial sarcomas were compared for their patterns of expression of intermediate filaments of keratin and vimentin type and epithelial membrane antigen and for lectin binding sites. The lining cells in both normal synovia and villonodular synovitis reacted with anti-vimentin antibodies, but not with antibodies to different types of keratins or epithelial membrane antigen. The cleft-lining cells in synovial sarcoma, on the other hand, showed only keratin positivity, and epithelial membrane antigen could also be detected in these cells. Nonneoplastic synovial lining cells bound peanut agglutinin (PNA), Ricinus communis agglutinin (RCA), soybean agglutinin (SBA), concanavalin A (Con A), and wheat germ agglutinin (WGA) conjugates, but not Ulex europaeus I lectin (UEA I). In contrast, the epithelial-like cleft lining cells in synovial sarcomas showed an apical cytoplasmic binding of PNA, UEA I, RCA, and SBA, and binding of WGA to the whole cytoplasm but did not bind Con A. The distinct differences between synovial lining cells and synovial sarcoma cells speak against synovial cell features in synovial sarcoma. These results indicate that synovial sarcoma is a carcinosarcomalike tumor with true epithelial differentiation, and the term "synovial sarcoma" apparently is a misnomer that should be abandoned.

Full text

Full text is available as a scanned copy of the original print version. Get a printable copy (PDF file) of the complete article (2.3M), or click on a page image below to browse page by page. Links to PubMed are also available for Selected References.
icon of scanned page 18
18
icon of scanned page 19
19
icon of scanned page 20
20
icon of scanned page 21
21
icon of scanned page 22
22
icon of scanned page 23
23
icon of scanned page 24
24
icon of scanned page 25
25

Images in this article

Figure 1
Figure 1
on p.20
Figure 2
Figure 2
on p.20
Figure 3
Figure 3
on p.21
Figure 4
Figure 4
on p.21
Figure 5
Figure 5
on p.22
Click on the image to see a larger version.

Selected References

These references are in PubMed. This may not be the complete list of references from this article.
  • Mackenzie DH. Synovial sarcoma. A review of 58 cases. Cancer. 1966 Feb;19(2):169–180. [PubMed] [Google Scholar]
  • Schmidt D, Mackay B. Ultrastructure of human tendon sheath and synovium: implications for tumor histogenesis. Ultrastruct Pathol. 1982 Jul-Sep;3(3):269–283. [PubMed] [Google Scholar]
  • Mickelson MR, Brown GA, Maynard JA, Cooper RR, Bonfiglio M. Synovial sarcoma: an electron microscopic study of monophasic and biphasic forms. Cancer. 1980 Apr 15;45(8):2109–2118. [PubMed] [Google Scholar]
  • Miettinen M, Lehto VP, Virtanen I. Keratin in the epithelial-like cells of classical biphasic synovial sarcoma. Virchows Arch B Cell Pathol Incl Mol Pathol. 1982 Aug;40(2):157–161. [PubMed] [Google Scholar]
  • Corson JM, Weiss LM, Banks-Schlegel SP, Pinkus GS. Keratin proteins in synovial sarcoma. Am J Surg Pathol. 1983 Jan;7(1):107–109. [PubMed] [Google Scholar]
  • Miettinen M, Lehto VP, Virtanen I. Monophasic synovial sarcoma of spindle-cell type. Epithelial differentiation as revealed by ultrastructural features, content of prekeratin and binding of peanut agglutinin. Virchows Arch B Cell Pathol Incl Mol Pathol. 1983;44(2):187–199. [PubMed] [Google Scholar]
  • Virtanen I, Lehto VP, Lehtonen E, Vartio T, Stenman S, Kurki P, Wager O, Small JV, Dahl D, Badley RA. Expression of intermediate filaments in cultured cells. J Cell Sci. 1981 Aug;50:45–63. [PubMed] [Google Scholar]
  • Virtanen I, von Koskull H, Lehto VP, Vartio T, Aula P. Cultured human amniotic fluid cells characterized with antibodies against intermediate filaments in indirect immunofluorescence microscopy. J Clin Invest. 1981 Nov;68(5):1348–1355.[PMC free article] [PubMed] [Google Scholar]
  • Holthöfer H, Miettinen A, Paasivuo R, Lehto VP, Linder E, Alfthan O, Virtanen I. Cellular origin and differentiation of renal carcinomas. A fluorescence microscopic study with kidney-specific antibodies, antiintermediate filament antibodies, and lectins. Lab Invest. 1983 Sep;49(3):317–326. [PubMed] [Google Scholar]
  • Heyderman E, Steele K, Ormerod MG. A new antigen on the epithelial membrane: its immunoperoxidase localisation in normal and neoplastic tissue. J Clin Pathol. 1979 Jan;32(1):35–39.[PMC free article] [PubMed] [Google Scholar]
  • Brozman M. Immunohistochemical analysis of formaldehyde- and trypsin- or pepsin-treated material. Acta Histochem. 1978;63(2):251–260. [PubMed] [Google Scholar]
  • Miettinen M, Lehto VP, Badley RA, Virtanen I. Alveolar rhabdomyosarcoma. Demonstration of the muscle type of intermediate filament protein, desmin, as a diagnostic aid. Am J Pathol. 1982 Aug;108(2):246–251.[PMC free article] [PubMed] [Google Scholar]
  • Howard DR, Batsakis JG. Peanut agglutinin: a new marker for tissue histiocytes. Am J Clin Pathol. 1982 Apr;77(4):401–408. [PubMed] [Google Scholar]
  • Franke WW, Schmid E, Schiller DL, Winter S, Jarasch ED, Moll R, Denk H, Jackson BW, Illmensee K. Differentiation-related patterns of expression of proteins of intermediate-size filaments in tissues and cultured cells. Cold Spring Harb Symp Quant Biol. 1982;46(Pt 1):431–453. [PubMed] [Google Scholar]
  • Osborn M, Weber K. Tumor diagnosis by intermediate filament typing: a novel tool for surgical pathology. Lab Invest. 1983 Apr;48(4):372–394. [PubMed] [Google Scholar]
  • Altmannsberger M, Weber K, Hölscher A, Schauer A, Osborn M. Antibodies to intermediate filaments as diagnostic tools: human gastrointestinal carcinomas express prekeratin. Lab Invest. 1982 May;46(5):520–526. [PubMed] [Google Scholar]
  • Madri JA, Barwick KW. An immunohistochemical study of nasopharyngeal neoplasms using keratin antibodies: epithelial versus nonepithelial neoplasms. Am J Surg Pathol. 1982 Mar;6(2):143–149. [PubMed] [Google Scholar]
  • Altmannsberger M, Osborn M, Hölscher A, Schauer A, Weber K. The distribution of keratin type intermediate filaments in human breast cancer. An immunohistological study. Virchows Arch B Cell Pathol Incl Mol Pathol. 1981;37(3):277–284. [PubMed] [Google Scholar]
  • Krepler R, Denk H, Weirich E, Schmid E, Franke WW. Keratin-like proteins in normal and neoplastic cells of human and rat mammary gland as revealed by immunofluorescence microscopy. Differentiation. 1981;20(3):242–252. [PubMed] [Google Scholar]
  • Lehto VP, Stenman S, Miettinen M, Dahl D, Virtanen I. Expression of a neural type of intermediate filament as a distinguishing feature between oat cell carcinoma and other lung cancers. Am J Pathol. 1983 Feb;110(2):113–118.[PMC free article] [PubMed] [Google Scholar]
  • Bonazzi del Poggetto C, Virtanen I, Lehto VP, Wahlström T, Saksela E. Expression of intermediate filaments in ovarian and uterine tumors. Int J Gynecol Pathol. 1983;1(4):359–366. [PubMed] [Google Scholar]
  • Miettinen M, Lehto VP, Virtanen I. Expression of intermediate filaments in normal ovaries and ovarian epithelial, sex cord-stromal, and germinal tumors. Int J Gynecol Pathol. 1983;2(1):64–71. [PubMed] [Google Scholar]
  • Nagle RB, McDaniel KM, Clark VA, Payne CM. The use of antikeratin antibodies in the diagnosis of human neoplasms. Am J Clin Pathol. 1983 Apr;79(4):458–466. [PubMed] [Google Scholar]
  • Espinoza CG, Azar HA. Immunohistochemical localization of keratin-type proteins in epithelial neoplasms. Correlation with electron microscopic findings. Am J Clin Pathol. 1982 Oct;78(4):500–507. [PubMed] [Google Scholar]
  • Ramaekers F, Puts J, Moesker O, Kant A, Jap P, Vooijs P. Demonstration of keratin in human adenocarcinomas. Am J Pathol. 1983 May;111(2):213–223.[PMC free article] [PubMed] [Google Scholar]
  • Ramaekers F, Huysmans A, Moesker O, Kant A, Jap P, Herman C, Vooijs P. Monoclonal antibody to keratin filaments, specific for glandular epithelia and their tumors. Use in surgical pathology. Lab Invest. 1983 Sep;49(3):353–361. [PubMed] [Google Scholar]
  • Miettinen M, Lehto VP, Virtanen I. Nasopharyngeal lymphoepithelioma. Histological diagnosis as aided by immunohistochemical demonstration of keratin. Virchows Arch B Cell Pathol Incl Mol Pathol. 1982 Aug;40(2):163–169. [PubMed] [Google Scholar]
  • Said JW. Immunohistochemical localization of keratin proteins in tumor diagnosis. Hum Pathol. 1983 Dec;14(12):1017–1019. [PubMed] [Google Scholar]
  • Miettinen M, Lehto VP, Badley RA, Virtanen I. Expression of intermediate filaments in soft-tissue sarcomas. Int J Cancer. 1982 Nov 15;30(5):541–546. [PubMed] [Google Scholar]
  • Denk H, Krepler R, Artlieb U, Gabbiani G, Rungger-Brändle E, Leoncini P, Franke WW. Proteins of intermediate filaments. An immunohistochemical and biochemical approach to the classification of soft tissue tumors. Am J Pathol. 1983 Feb;110(2):193–208.[PMC free article] [PubMed] [Google Scholar]
  • Osung OA, Chandra M, Holborow EJ. Intermediate filaments in synovial lining cells in rheumatoid arthritis and other arthritides are of vimentin type. Ann Rheum Dis. 1982 Feb;41(1):74–77.[PMC free article] [PubMed] [Google Scholar]
  • Miettinen M, Lehto VP, Vartio T, Virtanen I. Epithelioid sarcoma. Ultrastructural and immunohistologic features suggesting a synovial origin. Arch Pathol Lab Med. 1982 Nov;106(12):620–623. [PubMed] [Google Scholar]
  • Whillis J. The development of synovial joints. J Anat. 1940 Jan;74(Pt 2):277–283.[PMC free article] [PubMed] [Google Scholar]
  • GRAY DJ, GARDNER E. Prenatal development of the human knee and superior tibiofibular joints. Am J Anat. 1950 Mar;86(2):235–287. [PubMed] [Google Scholar]
  • To A, Dearnaley DP, Ormerod MG, Canti G, Coleman DV. Epithelial Membrane Antigen. Its use in the cytodiagnosis of malignancy in serous effusions. Am J Clin Pathol. 1982 Aug;78(2):214–219. [PubMed] [Google Scholar]
  • Sloane JP, Ormerod MG. Distribution of epithelial membrane antigen in normal and neoplastic tissues and it value in diagnostic tumor pathology. Cancer. 1981 Apr 1;47(7):1786–1795. [PubMed] [Google Scholar]
  • Corson JM, Pinkus GS. Mesothelioma: profile of keratin proteins and carcinoembryonic antigen: an immunoperoxidase study of 20 cases and comparison with pulmonary adenocarcinomas. Am J Pathol. 1982 Jul;108(1):80–88.[PMC free article] [PubMed] [Google Scholar]
  • Pisa R, Bonetti F, Chilosi M, Iannucci A, Menestrina F. Synovial sarcoma enzyme histochemistry of a typical case. Virchows Arch A Pathol Anat Histopathol. 1982;398(1):67–73. [PubMed] [Google Scholar]
  • CADMAN NL, SOULE EH, KELLY PJ. SYNOVIAL SARCOMA; AN ANALYSIS OF 34 TUMORS. Cancer. 1965 May;18:613–627. [PubMed] [Google Scholar]
  • Roth JA, Enzinger FM, Tannenbaum M. Synovial sarcoma of the neck: a followup study of 24 cases. Cancer. 1975 Apr;35(4):1243–1253. [PubMed] [Google Scholar]
  • Katenkamp D, Stiller D. Synovial sarcoma of the abdominal wall. Light microscopic, histochemical and electron microscopic investigations. Virchows Arch A Pathol Anat Histol. 1980;388(3):349–360. [PubMed] [Google Scholar]
  • Ghadially FN, Roy S. Experimentally produced synovial sarcomas. Cancer. 1966 Dec;19(12):1901–1908. [PubMed] [Google Scholar]
  • Barsky SH, Siegal GP, Jannotta F, Liotta LA. Loss of basement membrane components by invasive tumors but not by their benign counterparts. Lab Invest. 1983 Aug;49(2):140–147. [PubMed] [Google Scholar]
  • Birembaut P, Caron Y, van Cauwenberge D, Foidart JM. Distribution of laminin, a basement membrane glycoprotein in epithelial proliferations. A preliminary study in the breast, the lungs and uterine cervix. Coll Relat Res. 1983;3(1):25–31. [PubMed] [Google Scholar]
  • Gabbiani G, Kaye GI, Lattes R, Majno G. Synovial sarcoma. Electron microscopic study of a typical case. Cancer. 1971 Oct;28(4):1031–1039. [PubMed] [Google Scholar]
  • Dische FE, Darby AJ, Howard ER. Malignant synovioma: electron microscopical findings in three patients and review of the literature. J Pathol. 1978 Mar;124(3):149–155. [PubMed] [Google Scholar]
  • Miettinen M, Foidart JM, Ekblom P. Immunohistochemical demonstration of laminin, the major glycoprotein of basement membranes, as an aid in the diagnosis of soft tissue tumors. Am J Clin Pathol. 1983 Mar;79(3):306–311. [PubMed] [Google Scholar]
  • Krall RA, Kostianovsky M, Patchefsky AS. Synovial sarcoma: a clinical, pathological, and ultrastructural study of 26 cases supporting the recognition of a monophasic variant. Am J Surg Pathol. 1981 Mar;5(2):137–151. [PubMed] [Google Scholar]
  • Evans HL. Synovial sarcoma. A study of 23 biphasic and 17 probable monophasic examples. Pathol Annu. 1980;15(Pt 2):309–331. [PubMed] [Google Scholar]
  • Farris KB, Reed RJ. Monophasic, glandular, synovial sarcomas and carcinomas of the soft tissues. Arch Pathol Lab Med. 1982 Mar;106(3):129–132. [PubMed] [Google Scholar]
  • Kahn HJ, Yeger H, Baumal R, Thom H, Phillips JM. Categorization of pediatric neoplasms by immunostaining with antiprekeratin and antivimentin antisera. Cancer. 1983 Feb 15;51(4):645–653. [PubMed] [Google Scholar]
  • Balsaver AM, Gibley CW, Jr, Tessmer CF. Ultrastructural studies in Wilms's tumor. Cancer. 1968 Aug;22(2):417–427. [PubMed] [Google Scholar]
  • Saxén L, Koskimies O, Lahti A, Miettinen H, Rapola J, Wartiovaara J. Differentiation of kidney mesenchyme in an experimental model system. Adv Morphog. 1968;7:251–293. [PubMed] [Google Scholar]
  • Goldstein IJ, Hayes CE. The lectins: carbohydrate-binding proteins of plants and animals. Adv Carbohydr Chem Biochem. 1978;35:127–340. [PubMed] [Google Scholar]
  • Lotan R, Nicolson GL. Purification of cell membrane glycoproteins by lectin affinity chromatography. Biochim Biophys Acta. 1979 Dec 20;559(4):329–376. [PubMed] [Google Scholar]
  • Holthöfer H, Virtanen I, Pettersson E, Törnroth T, Alfthan O, Linder E, Miettinen A. Lectins as fluorescence microscopic markers for saccharides in the human kidney. Lab Invest. 1981 Nov;45(5):391–399. [PubMed] [Google Scholar]
  • Franklin WA. Tissue binding of lectins in disorders of the breast. Cancer. 1983 Jan 15;51(2):295–300. [PubMed] [Google Scholar]
  • Jamieson JD, Ingber DE, Muresan V, Hull BE, Sarras MP, Jr, Maylié-Pfenninger MF, Iwanij V. Cell surface properties of normal, differentiating, and neoplastic pancreatic acinar cells. Cancer. 1981 Mar 15;47(6 Suppl):1516–1527. [PubMed] [Google Scholar]
  • Yonezawa S, Nakamura T, Tanaka S, Sato E. Glycoconjugate with Ulex europaeus agglutinin-I-binding sites in normal mucosa, adenoma, and carcinoma of the human large bowel. J Natl Cancer Inst. 1982 Oct;69(4):777–785. [PubMed] [Google Scholar]
Copyright notice
Abstract
For an evaluation of the putative histogenetic relationship of synovia and synovial sarcomas, normal synovia, villonodular synovitis, and synovial sarcomas were compared for their patterns of expression of intermediate filaments of keratin and vimentin type and epithelial membrane antigen and for lectin binding sites. The lining cells in both normal synovia and villonodular synovitis reacted with anti-vimentin antibodies, but not with antibodies to different types of keratins or epithelial membrane antigen. The cleft-lining cells in synovial sarcoma, on the other hand, showed only keratin positivity, and epithelial membrane antigen could also be detected in these cells. Nonneoplastic synovial lining cells bound peanut agglutinin (PNA), Ricinus communis agglutinin (RCA), soybean agglutinin (SBA), concanavalin A (Con A), and wheat germ agglutinin (WGA) conjugates, but not Ulex europaeus I lectin (UEA I). In contrast, the epithelial-like cleft lining cells in synovial sarcomas showed an apical cytoplasmic binding of PNA, UEA I, RCA, and SBA, and binding of WGA to the whole cytoplasm but did not bind Con A. The distinct differences between synovial lining cells and synovial sarcoma cells speak against synovial cell features in synovial sarcoma. These results indicate that synovial sarcoma is a carcinosarcomalike tumor with true epithelial differentiation, and the term "synovial sarcoma" apparently is a misnomer that should be abandoned.
Collaboration tool especially designed for Life Science professionals.Drag-and-drop any entity to your messages.