BRONCHIOLOALVEOLAR PROGRESSIVE SYSTEMIC
CARCINOMA SCLEROSIS
D. BENHARROCH, MD, S. SUKENIK, MD,
AND
AND GENERALIZED
AMY LOIDOSIS
COMPLICATING
M. SACKS, MB, CHB, FRCPATH
We report a patient with progressive systemic sclerosis in whom an autopsy, performed 13 years after diagnosis, revealed the presence of ~o~hio~oa~~eo~ar carcinoma and of generalized amyloidosis. Characterization of the amyloid jib& protein suggested an immunoglobulin light chain (AL) origin. HUM PATHOL 23:839841. Copyright 0 I992 by W.B. Saunders Company Amyloidosis is a well-recognized complication in the autoimmune connective tissue group of diseases, particularly rheumatoid arthritis,’ but only occasionally has it been described in progressive systemic sclerosis (PSS). In an extensive review of the literature, Brandwein et al found only six reports of amyloidosis in PSS.” More recently, a case of PSS and amyloidosis associated with lung cancer has been reported.3 In this report we describe a patient with PSS in whom autopsy revealed systemic amyloidosis. An unexpected finding was a bronchioloalveolar carcinoma. The relationship among PSS, bronchioloalveolar carcinoma, and amyloidosis is discussed. An attempt was made to define the nature of the amyloid fibril protein by the use of congo red staining after oxidation with potassium permanganate, acrylamide sodium dodecyl sulfate electrophoresis on paraffin blocks, and immunohistochemical staining for kappa and lambda immunoglobulin light chains and for amyloid A protein.4-6
CASE REPORT A 51-year-old white woman who suffered from longstanding PSS was diagnosed 13 years before her death. When she was first examined at our hospital the positive findings included diffuse typical skin changes affecting the hands, arms, feet, upper chest, back, and face associated with areas of hypopigmentation, hyperpigmentation, and multiple telangiectases. In addition to sclerodactyly, there were multiple scars and occasional ulcers on the fingertips. There was a deforming arthritis of the wrists and metacarpophalangeal joints. Three years after diagnosis of PSS the patient gradually developed exertional dyspnea and a nonproductive cough. Pulmonary function tests revealed restrictive ventilatory defects with reduction of vital capacity and decreased lung compliance. The patient later developed severe pulmonary arterial hypertension leading to car pulmonale. Pericarditis was successfully treated with systemic steroids. Thirteen years‘after the diagnosis of PSS renal failure appeared abruptly and was associated with malignant hypertension and acute renal failure, which led to the patient’s death within 2 weeks. At autopsy, the diagnosis of PSS was confirmed by the drawn mask appearance of the face. The hands showed sclerodactyly. The visceral involvement included dilatation of the distal third of the esophagus and focal fibrosis of the small intestine. The kidneys showed vascular scars. Foci of fibrosis
were scattered in the myocardium in the complete absence of coronary artery disease. The lungs were involved by PSS and showed interstitial fibrosis mostly involving the lower lobes and honeycomb changes that were most marked in the right upper lobe. Cubical metaplasia of the alveolar lining was marked. Multiple whitish nodules were scattered throughout the left lung; in these foci the airspaces were lined by tall columnar cells with atypical hyperchromatic nuclei typical of bronchioloalveolar carcinoma (Fig 1). In addition to the multiple foci of fibrosis, the myocardium showed a homogenous hyaline material surrounding and partially replacing the myocardial fibers, which stained strongly positive for congo red and showed the typical emerald green birefringence of amyloid on polarized microscopy (Fig 2). Similar deposits were present in the endocardium and in multiple small vessels in many organs. A congo red stain of the myocardium, performed after potassium permanganate treatment, showed persistence of the green birefringence, a finding that favors the presence of immunoglobulin light chain (AL) amyloid.5 An acrylamide sodium dodecyl sulfate electrophoresis performed on myocardial tissue from the paraffin blocks was negative for amyloid A (AA) protein.6 However, sections of the amyloid deposits in the myocardium and adrenals were positive for AA protein and negative for kappa and lambda light chains by immunochemical staining. DISCUSSION The association of amyloidosis and autoimmune connective tissue disease is mostly restricted to rheumatoid arthritis and ankylosing spondylitis. In 1982, Horwitz et al stated that amyloidosis is not a complication of scleroderma.4 Nevertheless, we were able to find references to seven cases with this association. Sackner’ reported an @?-year-old woman with scleroderma in whom an autopsy revealed carcinoma of the esophagus and generalized amyloidosis. Lowe’ described a 45-yearold white man with PSS and the nephrotic syndrome who showed generalized amyloidosis at autopsy. Three patients with typical clinical scleroderma were reported by Holzmann et al9 Two of these patients developed amyloid skin lesions and the third patient showed generalized amyloidosis at autopsy. Horwitz et al4 described a 58-year-old patient with Raynaud’s phenomenon, mild pulmonary fibrosis, and an atonic esophagus who developed rupture of the extensor tendon due to amyloidosis involving the tendon sheath. Potassium permanganate treatment of the sections did not reveal a loss of the birefringence, favoring the diagnosis of primary amyloidosis. Focan et als reported a 70-year-old white man with diffuse arthralgia, asthma, and aplastic anemia. A skin biopsy showed scleroderma, a bone marrow aspiration, and a plasmacytosis of 11%. Autopsy revealed PSS and amyloidosis involving the gastrointestinal tract and bone marrow. A small squamous cell carcinoma was discovered in the lung. The seven previously described cases thus showed an association of PSS with amyloidosis localized to the skin in two cases,’ to a tendon in one,4 and to the gastrointestinal tract and bone marrow in one,’ and with systemic amyloidosis in thee cases.7.9 In our patient with PSS autopsy revealed lung
From the Institute of Pathology and Internal Medicine D, the Soroka Medical Center and Facultv of Health Sciences, Ben-Gut-ion University of the Negev. Beer-She&, Israel. Accepted fir publication December 2, 1991. Key wordtr progressive systemic sclerosis, bronchio)oalveolar carcinoma, amyloidosis. Address correspondence and reprint requests to D. Benharroch, MD, Institute of Pathology, the Soroka Medical Center, PO Box 151, Beer-Sheva 84 i 0 1, Israel. Copyright 0 1992 by W.B. Saunders Company 0046-8177/92/2307-0021$5.00/O
839
HUMAN PATHOLOGY
Volume 23, No. 7 (July 1992)
FIGURE 1. Section from the left upper lobe showing bronchioloalveolar carcinoma. (Hematoxylin-eosin stain; magnification x 150.)
cancer and generalized amyloidosis. This is the second report of the association of these three conditions in the same patient.’ The association of PSS and cancer is well recognized. Most investigators accept the predominance of lung cancer, mainly bronchioloalveolar carcinoma, and agree that the malignancy is almost inevitably superimposed on chronic pulmonary fibrosis in these cases.‘“.‘i Amyloidosis developing in patients with cancer has been well described in multiple myeloma and is of the AL type.‘” Amyloidosis complicating solid tumors occurs most frequently with hypernephromas and is described as being of the AA type.‘3.‘4 Amyloidosis rarely has been associated with other solid tumors, such as uterine or urinary bladder carcinomas. We are aware of three reports of amyloidosis in bronchogenic carcinomas; in one of these reports the amyloid was identified as AA protein.3,‘5,‘”
The only case of PSS in which biochemical definition of the amyloid fibril protein was attempted was the patient with amyloidosis of the tendon.4 In our patient amyloidosis was generalized and probably secondary to PSS, although we cannot exclude the possibility of its being related to the lung carcinoma. With regard to the nature of the amyloid fibril protein in our patients, the findings of some of the special studies at first glance seem to be contradictory. The results of the permanganate oxidative treatment and the acrylamide sodium dodecyl sulfate electrophoresis strongly favor AL amyloid. The predominant involvement of the myocardium is also more in favor of this type of amyloid. The negative immunostaining for kappa and lambda light chains may be due to alteration in the tertiary structure of the beta-pleated fibril and does not exclude the possibility of AL amyloid.” The positive immunostaining of the amyloid deposits
FIGURE 2. Section from the myocardium featuring the green birefringence of amyloid. Polarized microscopy of a congo red stained section. (Magnification X350.)
840
CASE STUDIES
for AA protein is more difficult to explain, but A4 protein has been found as a minor component in some cases of primary and of myeloma-associated amyloidosis.” We believe that most of the evidence favors an AL origin of the amyloid deposits in our patient. The apparently contradictory results in some of the special investigations, however, emphasize the need for further studies of the amyloid deposits associated with PSS or with malignant tumors.
5. Wright JR, Calkins E, Humphrey RL: Potassium pennanganate reaction in amyloidosis. Lab Invest 35:274-281, 1977 6. Shtrasburn S. Pras M. Lawevitch P. et al: Demonstration of AA protein in formalin-fixed Faiaffin-embeddYed tissues. Am J Pathol 106: 141-144: 1982 7. Sackner MA: Scleroderma. New York, NY, Grune & Stratton, 1966, p 54 8. Lowe MC: Sclerodennaandamyloidosis. Mit Med 134:1430-1433,1969 9. Holzmann H, Korting GW, Missmahl HP: Perikoliagene amyloidablagerungen in Haut und inneren Organen bei Sklerodetmie. Klin Wochenschr 47:390-391, 1969 10. Trotta F, Potena A, Marchi M, et al: Progressive systemic sclerosis and pulmonary malignancy. J Rheumatol9:970-973, 1982 11. Medsger TA: Systemic sclerosis and malignancy-Are they related? J Rheumatol 12:1041-1043, 1985 (editorial) 12. CPC: Case 43-1985. New Engl J Med 313:1070-1079. 1985 13. Hind CRK, Trennent GA, Evans DJ, et al: Demonstration of amyloid A (AA) protein and amyloid P component (AP) in deposits of systemic amyloidosis associated with renal adenocarcinoma. J Pathol 139: 159-l 66, 1983 14. Vanatta PR, Silva FG, Taylor WE, et al: Renal cell carcinoma and systemic amyloidosis: Demonstration of AA protein and review of the literature. HUM PATHOL 14:195-201, 1983 15. Kimball KG: Amyloidosis in association with neoplastic disease. Ann Intern Med 55:958-974, 1961 16. Richmond I, Hasleton PS, Samadian S: Systemic amyloidosis associated with carcinoma of the bronchus. Thorax 45:156-157, 1990 17. Chen KTK, Flam MS, Workman RD: Amyloid tumor of the spleen. Am J Surg Pathol 11:723-725, 1987 18. Falck HM. Westermark P: Protein AA in primary and myeloma associated amyloidosis. Clin Exp Immunol 54:259-264. 1983
Acknowledgment. The authors thank Professor M. Pras for carrying out the acrylamide sodium dodecyl sulfate electrophoresis and Dr S. Argov, V. Hirsh, and P. Gabrieli for the immunostaining.
REFERENCES 1. Kyle RA, Bayrd ED: Amyloidosis: Review of 236 cases. Medicine 54: 271-299, 1975 2. Brandwein SR, Medsger TA, Skinner M, et al: Serum amyloid A protein concentration in progressive systemic sclerosis (scleroderma). Ann Rheum Dis 43:586-589, 1984 3. Focan C, Swale JL, Borlee-Hermans G, et al: Systemic sclerosis aplastic anemia and amyloidosis associated with lung carcinoma. Acta Clin Belg 40:204205, 1985 4. Horwitr HM, DiBeneditto JD, Allegra SR, et al: Scleroderma, amyloidosis and extensor tendon rupture. Arthritis Rheum 25:1141-1143, 1982
BOOK REVIEWS state of understanding and controversies are simply and well described. References include 1989 and 1990 publications and vary in number from 12 (clear cell sarcoma) to 244 (fibrous and fibrohistiocytic lesions). They represent a thorough effort to offer more complete information as a supplement to the distilled information in the text. I find the book helpfully “streamlined” but sometimes a bit superficial; this is occasionally true with regard to areas of frequent differential diagnostic difficulty. This, then, is a book for the diagnostic surgical pathologist. It should find its best use as a quick, concise reference in instances for which the textbook by Enzinger and Weiss is felt to be too encyclopedic.
Tumors and Tumorlike Lesions of Soft Tissue. Vito Ninfo, E. B. Chung, Andrea 0. Cavazanna (eds). New York, NY, Churchill Livingstone, 1991, 285 pages, $79.95. Although it is difficult to write a textbook about a subject for which an encyclopedic, authoritative work already exists, this well-written and readable book effectively achieves its stated purpose: to provide a “. . . quick, concise reference tool and a handy companion to the microscope.” It does not provide comprehensive coverage of its subject, but rather focuses on the differential diagnosis of the more commonly seen unusual lesions, omitting for the most part both the commonplace and the exotic. Consequently, it consistently assumes a basic working knowledge of soft tissue lesions and is thus somewhat unsuitable for the pathologist-in-training who is reading for education. The book is organized around histogenesis (as currently understood) and includes chapters on mesothelial processes, neuroectodermal tumors, and lesions of uncertain histogenesis. Immunohistochemical characterization is briefly described for most tumors and is presented as an adjunct to the more definitive H and E morphology, a principle stated in the first chapter (with which I enthusiastically agree). Common pitfalls and areas of controversy with respect to this technique are also offered in specific instances. Electron microscopic description is given for entities in which it is distinctive. Useful tables in each chapter present demographic, differential diagnostic, and prognostic information in readily accessible form. One helpful feature is the use of bold type within a table to indicate the entities dealt with in the text. Photographs are numerous, black and white, and consistently of good quality, demonstrating effectively the characteristic light microscopic features of each entity. Particularly strong chapters include those dealing with peripheral nerve tumors and PNETs, in which the current
Pathology of the Gastrointestinal Tract. S-C. Ming and H. Goldman (eds). Philadelphia, PA, Saunders, 1992, 945 pages. Ming and Goldman have assembled an excellent volume on the gastrointestinal tract from the esophagus to the anus. Written by 34 authors representing both senior experts in the field and younger investigators, this book blends rich experience and modern methods. The work is arranged into three sections: “General Principles, ” “Disorders Common to All Areas of the Gastrointestinal Tract,” and “A Systematic Review of Individual Organs.” Detailed attention to handling, dissecting, and processing large and biopsy specimens is included. Aspects of embryology, genetics, and cytology are addressed. Common subjects are treated in detail, and uncommon entities are represented, making this a good reference source. The bibliography includes both classic papers several decades old and recent literature. Etiology and the pathogenesis of disorders are well described, particularly in Dr Ming’s discussion of esophageal, gastric, and colonic carcinomas. Areas in which one wishes there were more etiologic details, such as inflam-
841
CARCINOMA SCLEROSIS
D. BENHARROCH, MD, S. SUKENIK, MD,
AND
AND GENERALIZED
AMY LOIDOSIS
COMPLICATING
M. SACKS, MB, CHB, FRCPATH
We report a patient with progressive systemic sclerosis in whom an autopsy, performed 13 years after diagnosis, revealed the presence of ~o~hio~oa~~eo~ar carcinoma and of generalized amyloidosis. Characterization of the amyloid jib& protein suggested an immunoglobulin light chain (AL) origin. HUM PATHOL 23:839841. Copyright 0 I992 by W.B. Saunders Company Amyloidosis is a well-recognized complication in the autoimmune connective tissue group of diseases, particularly rheumatoid arthritis,’ but only occasionally has it been described in progressive systemic sclerosis (PSS). In an extensive review of the literature, Brandwein et al found only six reports of amyloidosis in PSS.” More recently, a case of PSS and amyloidosis associated with lung cancer has been reported.3 In this report we describe a patient with PSS in whom autopsy revealed systemic amyloidosis. An unexpected finding was a bronchioloalveolar carcinoma. The relationship among PSS, bronchioloalveolar carcinoma, and amyloidosis is discussed. An attempt was made to define the nature of the amyloid fibril protein by the use of congo red staining after oxidation with potassium permanganate, acrylamide sodium dodecyl sulfate electrophoresis on paraffin blocks, and immunohistochemical staining for kappa and lambda immunoglobulin light chains and for amyloid A protein.4-6
CASE REPORT A 51-year-old white woman who suffered from longstanding PSS was diagnosed 13 years before her death. When she was first examined at our hospital the positive findings included diffuse typical skin changes affecting the hands, arms, feet, upper chest, back, and face associated with areas of hypopigmentation, hyperpigmentation, and multiple telangiectases. In addition to sclerodactyly, there were multiple scars and occasional ulcers on the fingertips. There was a deforming arthritis of the wrists and metacarpophalangeal joints. Three years after diagnosis of PSS the patient gradually developed exertional dyspnea and a nonproductive cough. Pulmonary function tests revealed restrictive ventilatory defects with reduction of vital capacity and decreased lung compliance. The patient later developed severe pulmonary arterial hypertension leading to car pulmonale. Pericarditis was successfully treated with systemic steroids. Thirteen years‘after the diagnosis of PSS renal failure appeared abruptly and was associated with malignant hypertension and acute renal failure, which led to the patient’s death within 2 weeks. At autopsy, the diagnosis of PSS was confirmed by the drawn mask appearance of the face. The hands showed sclerodactyly. The visceral involvement included dilatation of the distal third of the esophagus and focal fibrosis of the small intestine. The kidneys showed vascular scars. Foci of fibrosis
were scattered in the myocardium in the complete absence of coronary artery disease. The lungs were involved by PSS and showed interstitial fibrosis mostly involving the lower lobes and honeycomb changes that were most marked in the right upper lobe. Cubical metaplasia of the alveolar lining was marked. Multiple whitish nodules were scattered throughout the left lung; in these foci the airspaces were lined by tall columnar cells with atypical hyperchromatic nuclei typical of bronchioloalveolar carcinoma (Fig 1). In addition to the multiple foci of fibrosis, the myocardium showed a homogenous hyaline material surrounding and partially replacing the myocardial fibers, which stained strongly positive for congo red and showed the typical emerald green birefringence of amyloid on polarized microscopy (Fig 2). Similar deposits were present in the endocardium and in multiple small vessels in many organs. A congo red stain of the myocardium, performed after potassium permanganate treatment, showed persistence of the green birefringence, a finding that favors the presence of immunoglobulin light chain (AL) amyloid.5 An acrylamide sodium dodecyl sulfate electrophoresis performed on myocardial tissue from the paraffin blocks was negative for amyloid A (AA) protein.6 However, sections of the amyloid deposits in the myocardium and adrenals were positive for AA protein and negative for kappa and lambda light chains by immunochemical staining. DISCUSSION The association of amyloidosis and autoimmune connective tissue disease is mostly restricted to rheumatoid arthritis and ankylosing spondylitis. In 1982, Horwitz et al stated that amyloidosis is not a complication of scleroderma.4 Nevertheless, we were able to find references to seven cases with this association. Sackner’ reported an @?-year-old woman with scleroderma in whom an autopsy revealed carcinoma of the esophagus and generalized amyloidosis. Lowe’ described a 45-yearold white man with PSS and the nephrotic syndrome who showed generalized amyloidosis at autopsy. Three patients with typical clinical scleroderma were reported by Holzmann et al9 Two of these patients developed amyloid skin lesions and the third patient showed generalized amyloidosis at autopsy. Horwitz et al4 described a 58-year-old patient with Raynaud’s phenomenon, mild pulmonary fibrosis, and an atonic esophagus who developed rupture of the extensor tendon due to amyloidosis involving the tendon sheath. Potassium permanganate treatment of the sections did not reveal a loss of the birefringence, favoring the diagnosis of primary amyloidosis. Focan et als reported a 70-year-old white man with diffuse arthralgia, asthma, and aplastic anemia. A skin biopsy showed scleroderma, a bone marrow aspiration, and a plasmacytosis of 11%. Autopsy revealed PSS and amyloidosis involving the gastrointestinal tract and bone marrow. A small squamous cell carcinoma was discovered in the lung. The seven previously described cases thus showed an association of PSS with amyloidosis localized to the skin in two cases,’ to a tendon in one,4 and to the gastrointestinal tract and bone marrow in one,’ and with systemic amyloidosis in thee cases.7.9 In our patient with PSS autopsy revealed lung
From the Institute of Pathology and Internal Medicine D, the Soroka Medical Center and Facultv of Health Sciences, Ben-Gut-ion University of the Negev. Beer-She&, Israel. Accepted fir publication December 2, 1991. Key wordtr progressive systemic sclerosis, bronchio)oalveolar carcinoma, amyloidosis. Address correspondence and reprint requests to D. Benharroch, MD, Institute of Pathology, the Soroka Medical Center, PO Box 151, Beer-Sheva 84 i 0 1, Israel. Copyright 0 1992 by W.B. Saunders Company 0046-8177/92/2307-0021$5.00/O
839
HUMAN PATHOLOGY
Volume 23, No. 7 (July 1992)
FIGURE 1. Section from the left upper lobe showing bronchioloalveolar carcinoma. (Hematoxylin-eosin stain; magnification x 150.)
cancer and generalized amyloidosis. This is the second report of the association of these three conditions in the same patient.’ The association of PSS and cancer is well recognized. Most investigators accept the predominance of lung cancer, mainly bronchioloalveolar carcinoma, and agree that the malignancy is almost inevitably superimposed on chronic pulmonary fibrosis in these cases.‘“.‘i Amyloidosis developing in patients with cancer has been well described in multiple myeloma and is of the AL type.‘” Amyloidosis complicating solid tumors occurs most frequently with hypernephromas and is described as being of the AA type.‘3.‘4 Amyloidosis rarely has been associated with other solid tumors, such as uterine or urinary bladder carcinomas. We are aware of three reports of amyloidosis in bronchogenic carcinomas; in one of these reports the amyloid was identified as AA protein.3,‘5,‘”
The only case of PSS in which biochemical definition of the amyloid fibril protein was attempted was the patient with amyloidosis of the tendon.4 In our patient amyloidosis was generalized and probably secondary to PSS, although we cannot exclude the possibility of its being related to the lung carcinoma. With regard to the nature of the amyloid fibril protein in our patients, the findings of some of the special studies at first glance seem to be contradictory. The results of the permanganate oxidative treatment and the acrylamide sodium dodecyl sulfate electrophoresis strongly favor AL amyloid. The predominant involvement of the myocardium is also more in favor of this type of amyloid. The negative immunostaining for kappa and lambda light chains may be due to alteration in the tertiary structure of the beta-pleated fibril and does not exclude the possibility of AL amyloid.” The positive immunostaining of the amyloid deposits
FIGURE 2. Section from the myocardium featuring the green birefringence of amyloid. Polarized microscopy of a congo red stained section. (Magnification X350.)
840
CASE STUDIES
for AA protein is more difficult to explain, but A4 protein has been found as a minor component in some cases of primary and of myeloma-associated amyloidosis.” We believe that most of the evidence favors an AL origin of the amyloid deposits in our patient. The apparently contradictory results in some of the special investigations, however, emphasize the need for further studies of the amyloid deposits associated with PSS or with malignant tumors.
5. Wright JR, Calkins E, Humphrey RL: Potassium pennanganate reaction in amyloidosis. Lab Invest 35:274-281, 1977 6. Shtrasburn S. Pras M. Lawevitch P. et al: Demonstration of AA protein in formalin-fixed Faiaffin-embeddYed tissues. Am J Pathol 106: 141-144: 1982 7. Sackner MA: Scleroderma. New York, NY, Grune & Stratton, 1966, p 54 8. Lowe MC: Sclerodennaandamyloidosis. Mit Med 134:1430-1433,1969 9. Holzmann H, Korting GW, Missmahl HP: Perikoliagene amyloidablagerungen in Haut und inneren Organen bei Sklerodetmie. Klin Wochenschr 47:390-391, 1969 10. Trotta F, Potena A, Marchi M, et al: Progressive systemic sclerosis and pulmonary malignancy. J Rheumatol9:970-973, 1982 11. Medsger TA: Systemic sclerosis and malignancy-Are they related? J Rheumatol 12:1041-1043, 1985 (editorial) 12. CPC: Case 43-1985. New Engl J Med 313:1070-1079. 1985 13. Hind CRK, Trennent GA, Evans DJ, et al: Demonstration of amyloid A (AA) protein and amyloid P component (AP) in deposits of systemic amyloidosis associated with renal adenocarcinoma. J Pathol 139: 159-l 66, 1983 14. Vanatta PR, Silva FG, Taylor WE, et al: Renal cell carcinoma and systemic amyloidosis: Demonstration of AA protein and review of the literature. HUM PATHOL 14:195-201, 1983 15. Kimball KG: Amyloidosis in association with neoplastic disease. Ann Intern Med 55:958-974, 1961 16. Richmond I, Hasleton PS, Samadian S: Systemic amyloidosis associated with carcinoma of the bronchus. Thorax 45:156-157, 1990 17. Chen KTK, Flam MS, Workman RD: Amyloid tumor of the spleen. Am J Surg Pathol 11:723-725, 1987 18. Falck HM. Westermark P: Protein AA in primary and myeloma associated amyloidosis. Clin Exp Immunol 54:259-264. 1983
Acknowledgment. The authors thank Professor M. Pras for carrying out the acrylamide sodium dodecyl sulfate electrophoresis and Dr S. Argov, V. Hirsh, and P. Gabrieli for the immunostaining.
REFERENCES 1. Kyle RA, Bayrd ED: Amyloidosis: Review of 236 cases. Medicine 54: 271-299, 1975 2. Brandwein SR, Medsger TA, Skinner M, et al: Serum amyloid A protein concentration in progressive systemic sclerosis (scleroderma). Ann Rheum Dis 43:586-589, 1984 3. Focan C, Swale JL, Borlee-Hermans G, et al: Systemic sclerosis aplastic anemia and amyloidosis associated with lung carcinoma. Acta Clin Belg 40:204205, 1985 4. Horwitr HM, DiBeneditto JD, Allegra SR, et al: Scleroderma, amyloidosis and extensor tendon rupture. Arthritis Rheum 25:1141-1143, 1982
BOOK REVIEWS state of understanding and controversies are simply and well described. References include 1989 and 1990 publications and vary in number from 12 (clear cell sarcoma) to 244 (fibrous and fibrohistiocytic lesions). They represent a thorough effort to offer more complete information as a supplement to the distilled information in the text. I find the book helpfully “streamlined” but sometimes a bit superficial; this is occasionally true with regard to areas of frequent differential diagnostic difficulty. This, then, is a book for the diagnostic surgical pathologist. It should find its best use as a quick, concise reference in instances for which the textbook by Enzinger and Weiss is felt to be too encyclopedic.
Tumors and Tumorlike Lesions of Soft Tissue. Vito Ninfo, E. B. Chung, Andrea 0. Cavazanna (eds). New York, NY, Churchill Livingstone, 1991, 285 pages, $79.95. Although it is difficult to write a textbook about a subject for which an encyclopedic, authoritative work already exists, this well-written and readable book effectively achieves its stated purpose: to provide a “. . . quick, concise reference tool and a handy companion to the microscope.” It does not provide comprehensive coverage of its subject, but rather focuses on the differential diagnosis of the more commonly seen unusual lesions, omitting for the most part both the commonplace and the exotic. Consequently, it consistently assumes a basic working knowledge of soft tissue lesions and is thus somewhat unsuitable for the pathologist-in-training who is reading for education. The book is organized around histogenesis (as currently understood) and includes chapters on mesothelial processes, neuroectodermal tumors, and lesions of uncertain histogenesis. Immunohistochemical characterization is briefly described for most tumors and is presented as an adjunct to the more definitive H and E morphology, a principle stated in the first chapter (with which I enthusiastically agree). Common pitfalls and areas of controversy with respect to this technique are also offered in specific instances. Electron microscopic description is given for entities in which it is distinctive. Useful tables in each chapter present demographic, differential diagnostic, and prognostic information in readily accessible form. One helpful feature is the use of bold type within a table to indicate the entities dealt with in the text. Photographs are numerous, black and white, and consistently of good quality, demonstrating effectively the characteristic light microscopic features of each entity. Particularly strong chapters include those dealing with peripheral nerve tumors and PNETs, in which the current
Pathology of the Gastrointestinal Tract. S-C. Ming and H. Goldman (eds). Philadelphia, PA, Saunders, 1992, 945 pages. Ming and Goldman have assembled an excellent volume on the gastrointestinal tract from the esophagus to the anus. Written by 34 authors representing both senior experts in the field and younger investigators, this book blends rich experience and modern methods. The work is arranged into three sections: “General Principles, ” “Disorders Common to All Areas of the Gastrointestinal Tract,” and “A Systematic Review of Individual Organs.” Detailed attention to handling, dissecting, and processing large and biopsy specimens is included. Aspects of embryology, genetics, and cytology are addressed. Common subjects are treated in detail, and uncommon entities are represented, making this a good reference source. The bibliography includes both classic papers several decades old and recent literature. Etiology and the pathogenesis of disorders are well described, particularly in Dr Ming’s discussion of esophageal, gastric, and colonic carcinomas. Areas in which one wishes there were more etiologic details, such as inflam-
841
