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LINKS
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CORDOMA
LINK
citogenetica
- Tumore maligno che deriva da residui di
notocorda fetale
WHO 9370/3
Si presenta prevalentemente lungo l'asse spinale a livello
sfeno-occipitale, vertebrale e sacro-coccigeo.
PROFILO
IMMUNOFENOTIPICO E DIAGNOSI DIFFERENZIALE
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CORDOMA |
PARACORDOMA |
CONDROSARCOMA |
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| Citocheratina (CK8/18) |
+ |
+ |
- |
| EMA |
+ |
+ |
- |
| vimentina |
+ |
+ |
+ |
| S100 |
+ |
+ |
+ |
| GFAP |
+ |
- |
- |
| a-SMA |
- |
- |
- |
-
Hum Pathol 1998 Feb;29(2):119-26
Keratin subsets and monoclonal antibody HBME-1 in
chordoma: immunohistochemical differential diagnosis between tumors
simulating chordoma.
O'Hara BJ, Paetau A, Miettinen M.
Department of Anatomy, Pathology and Cell Biology, Jefferson Medical College
of Thomas Jefferson University, Philadelphia, PA, USA.
Thirty-five chordomas and more than 100 other tumors that have to be
considered in the differential diagnosis, were immunohistochemically
analyzed using a panel of antibodies including those to subsets of keratins
(K), HBME-1, a monoclonal antibody recognizing an unknown antigen on
mesothelial cells, and neuroendocrine markers. The patterns of
immunoreactivities in chordoma were compared with those in renal cell
carcinoma, colorectal mucinous adenocarcinoma, pituitary adenoma, skeletal
chondrosarcoma, and extraskeletal myxoid chondrosarcoma (ESMC). Chordomas
were consistently positive for keratin cocktail AE1/AE3, and for the
individual keratins K8 and K19, and nearly always positive for K5, but they
showed negative or only sporadic reactivity for K7 and K20. The keratin K8
and K19 reactivity was retained in those chordomas showing solid sheets of
epithelioid, spindle cells, or cartilaginous metaplasia, and in one of two
cases showing overtly sarcomatous transformation. In comparison, keratins
were never present in skeletal chondrosarcoma, although K8 and to a lesser
extent K19 were seen in occasional cases of ESMC with chordoid features. HBME-1
reacted strongly with chordoma and skeletal chondrosarcoma but
was almost never positive in renal or colorectal carcinoma. These carcinomas
lacked K5-reactivity, in contrast to chordoma. Chordomas were also
consistently positive for neuron-specific enolase and occasionally focally
for synaptophysin, but never for chromogranin. In contrast, pituitary
adenomas regularly expressed the full spectrum of neuroendocrine markers and
differed from chordoma by having a narrower repertoire of keratins, often
showing negative or focal keratin 8- or AE1/AE3 reactivity and being almost
always K19-negative. These findings indicate that chordoma can be
immunohistochemically separated from tumors that can resemble it.
Immunohistochemistry is especially useful in the diagnosis of small biopsy
specimens that offer limited material for morphological observation.
J Cutan Pathol 1998 May;25(5):279-84
Cutaneous parachordoma. A light microscopic and
immunohistochemical report of two cases and review of the literature.
Imlay SP, Argenyi ZB, Stone MS, McCollough ML, Henghold WB.
Department of Pathology, University of Iowa Hospital and Clinics, Iowa City
52242, USA.
Parachordomas are rare cutaneous tumors that show
virtually identical histologic findings to chordomas. Therefore, the
major differential diagnosis in a case of parchordoma is metastatic chordoma.
Parachordomas are benign neoplasms and most often develop on the extremities
adjacent to tendons, synovium or osseous structures, as opposed to chordomas,
which are malignant tumors located along the craniospinal axis. While
recurrences may occur in cases of parachordoma, metastases have not been
reported. In this report, two cases of parachordomas are reported and the
literature reviewed. By light microscopy, parachordomas show eosinophilic
bands of fibrous tissue separating lobules of cells with variably vacuolated
cytoplasm (physaliphorous cells) admixed with more epithelioid cells in a
myxoid stroma. Parachordomas and chordomas share immunohistochemical and
ultrastructural features. Both stain with S-100 protein and vimentin, and
ultrastructurally both demonstrate cytoplasmic vacuoles, intermediate
filaments, pinocytotic vesicles, celljunctions, and cytoplasmic membranes
with microvillous processes. Chordomas more frequently express cytokeratin
(98% vs. 66% in parachordomas) and epithelial membrane antigen (90% vs. 20%
in parachordomas) and chordomas have a larger number of rough endoplasmic
reticulum-mitochondrial complexes. Thus, positive staining with epithelial
membrane antigen and the identification of a large number of rough
endoplasmic reticulum-mitochondrial complexes are suggestive of metastatic
chordoma. However, the definitive distinction remains a clinical one after
appropriate radiologic studies of the skull and spinal chord.
Am J Surg Pathol 1999 Sep;23(9):1059-67
Parachordoma is immunohistochemically and cytogenetically
distinct from axial chordoma and extraskeletal myxoid chondrosarcoma.
Folpe AL, Agoff SN, Willis J, Weiss SW.
Emory University Hospital, Atlanta, Georgia, USA.
Parachordoma is a rare soft-tissue tumor resembling
extraskeletal myxoid chondrosarcoma and chordoma. Because fewer than
30 cases have been reported and precisely characterized, we studied the
clinicopathologic features of seven new cases, comparing the
immunohistochemical (six cases) and cytogenetic (one case) profiles with 15
cases of chordoma and six cases of extraskeletal myxoid chondrosarcoma.
Patients with these tumors ranged in age from 7 to 62 years (mean, 35 years)
and included four women and three men. The tumors presented as subfascial
masses of the thigh (two cases), arm (three cases), chest wall (one cases),
and buttocks (one case). In six of seven cases, there was neither recurrence
nor metastasis within the follow-up, which ranged from 4 months to 7 years.
The tumors were composed of vague nodules of large, rounded eosinophilic
cells embedded in a matrix that varied from myxoid to densely hyaline, and
the latter areas occasionally resembled primitive cartilage. Transitions
between the large eosinophilic cells and smaller rounded and shorter
spindled ones were often noted. Multivacuolated (physaliferouslike) cells
were noted in all cases but were usually few in number. The matrix stained
with Alcian blue (pH 2.5), and this staining was abolished with
hyaluronidase predigestion. Immunohistochemistry for a variety of
cytokeratins (CKs) (8/18, 1/10, 7, and 20), epithelial membrane antigen
(EMA), S-100 protein, vimentin CD34, type IV collagen, smooth muscle actin,
smooth muscle myosin heavy chain, calponin, and glial fibrillary acid
protein was performed. All parachordomas strongly expressed CK 8/18, but not
the other cytokeratins. Additionally, they expressed EMA (five of six).
S-100 protein (six of six), and vimentin (six of six) and had a linear
pattern of type IV collagen immunoreactivity around nests of cells (four of
five). Calponin was noted in one case, but no cases expressed smooth muscle
actin, smooth muscle myosin heavy chain, or glial fibrillary acid protein.
In contrast, chordoma expressed CK 8/18 (15 of 15) and CK 1/10 (14 of 15),
whereas extraskeletal myxoid chondrosarcoma consistently lacked CK. Although
chordoma and extraskeletal myxoid chondrosarcoma showed considerable overlap
with parachordoma, with respect to EMA and S-100 protein, they infrequently
displayed type IV collagen, as was seen in parachordoma. One case of
parachordoma studied cytogenetically disclosed trisomy 15, and monosomies of
1, 16, and 17 in contrast to the t(9;22) reported in extraskeletal myxoid
chondrosarcoma and the monosomies of 3, 4, 10, and 13 seen in chordoma. We
conclude that the immunohistochemical and cytogenetic profile distinguishes
parachordoma from extraskeletal myxoid chondrosarcoma and chordoma. Lack of
myoepithelial markers, furthermore, suggests parachordoma is not a deeply
situated adnexal tumor. Because of these differences, parachordoma is best
regarded as a distinct lesion without a clear relationship to other
well-characterized tumors.
J
Clin Pathol 2001 Dec;54(12):945-50
Immunohistochemical
analysis of E-cadherin, alpha-catenin, beta-catenin, gamma-catenin, and
neural cell adhesion molecule (NCAM) in chordoma.
Naka T, Oda Y, Iwamoto Y, Shinohara N, Chuman H, Fukui M, Tsuneyoshi M.
Department of Anatomic Pathology, Graduate School of Medical Sciences,
Kyushu University, 3-1-1 Maidashi, Higashi-ku, Fukuoka, 812-8582, Japan.
AIMS: The epithelioid features seen in chordoma are unique among mesenchymal
tumours. However, no detailed analysis regarding cell-cell communication has
been conducted in this epithelioid tumour. The aims of this study were to
investigate cell-cell communication in chordoma. METHODS: By means of
immunohistochemical techniques that incorporated a panel of monoclonal
antibodies against cell adhesion molecules (CAMs), including E-cadherin,
alpha-catenin, beta-catenin, gamma-catenin, and neural cell
adhesion molecule (NCAM), the expression of CAMs was studied in 15 specimens
of chordoma and eight specimens of chondrosarcoma. RESULTS: Most chordoma
specimens showed some positive immunoreactivity for all the CAMs examined.
For the various CAMs investigated, between two and five cases showed diffuse
immunoreactions, indicating well preserved expression. Well preserved
expression of all the CAMs examined was limited to only one case, thus
indicating that the expression of CAMs was decreased in most of the chordoma
specimens; however, no significant correlation was found between the
decreased expression of CAMs and the histological grade of malignancy,
cellular growth pattern, or clinical parameters in chordoma. In
chondrosarcoma, only a few specimens showed positive immunoreactivity for
CAMs and the expression of E-cadherin, beta-catenin, gamma-catenin, and NCAM
was seen more frequently in the chordoma specimens than in the
chondrosarcoma specimens. CONCLUSIONS: These results suggest that the
expression of CAMs is associated with the formation and maintenance of
chordoma tissue architecture, just as it is in other epithelial tumours or
normal tissue. Immunohistochemistry for CAMs was found to be of diagnostic
value for discriminating chordoma from chondrosarcoma, and these markers
could be used along with the cytokeratins, which are already used for this
purpose.
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