Pepsinogen C Expression in Tumors of Extragastric Origin

2000 ◽  
Vol 15 (2) ◽  
pp. 165-170 ◽  
Author(s):  
A.M. Merino ◽  
J. Vázquez ◽  
J.C. Rodríguez ◽  
R. Fernández ◽  
I. Quintela ◽  
...  

We have examined by immunohistochemistry the ability of human carcinomas of various origin to produce pepsinogen C, an aspartyl proteinase mainly involved in the digestion of proteins in the stomach and recently found to be associated with breast carcinomas. Of the 268 tumors analyzed 80 (29.8%) showed positive staining for pepsinogen C. These positive tumors included 12 gastric (38.7% of the 31 examined cases), nine pancreatic (42.8%), two renal (20%), 12 prostatic (40%), three bladder (27.3%), 14 endometrial (29.7%) and 18 ovarian (40%) carcinomas. We also detected 10 melanomas (50%) that were positive for pepsinogen C. By contrast, immunohistochemical staining for the proteinase was not detected in colorectal, cervical, lung and basal cell skin carcinomas. These results demonstrate that pepsinogen C, a proteolytic enzyme of highly restricted expression in human tissues, can also be expressed by a wide variety of human carcinomas. In addition, and similar to pepsinogen C expression in breast carcinomas, the production of this enzyme by different human tumors might be related to putative hormonal alterations associated with the development and progression of these tumors.

2014 ◽  
Vol 139 (4) ◽  
pp. 530-536 ◽  
Author(s):  
David Tacha ◽  
Weimin Qi ◽  
Seong Ra ◽  
Ryan Bremer ◽  
Charlie Yu ◽  
...  

Context Recent immunohistochemical studies have demonstrated Sry-related HMG-Box gene 10 (SOX10) expression in malignant melanomas, malignant peripheral nerve sheath tumors, a subset of breast carcinomas, and gliomas. SOX10 has shown important clinical utility in its ability to detect desmoplastic and spindle cell melanomas. To date, most publications have employed a research use–only goat polyclonal SOX10 antibody for immunohistochemical staining. Objective To describe the development of a new mouse monoclonal SOX10 antibody (BC34) and evaluate its immunohistochemical staining profile in a wide range of normal and neoplastic tissues, with an emphasis on melanoma. Design SOX10 antibody was optimized for staining using a polymer detection system and visualization with diaminobenzidine. Results In normal tissues, SOX10 was expressed in skin melanocytes and eccrine cells, breast myoepithelial and lobular epithelial cells, salivary gland myoepithelial cells, peripheral nerve Schwann cells, and central nervous system glial cells. SOX10 was expressed in 238 of 257 melanomas (92.6%), including 50 of 51 of both spindle cell and desmoplastic melanomas (98%). SOX10 was expressed in 100% of nevi (20 of 20) and schwannomas (28 of 28). In other neoplasms, SOX10 was expressed in 18 of 109 invasive ductal breast carcinomas (16.5%). All other carcinomas were negative for SOX10. SOX10 was identified in 25 of 52 central nervous system neoplasms, primarily in astrocytomas (22 of 41; 53.7%), and in 4 of 99 various sarcomas examined (4.0%). Conclusions The newly developed mouse monoclonal SOX10 antibody BC34 is highly sensitive and specific for malignant melanoma, including desmoplastic and spindle cell variants, and appears highly suitable for clinical use.


1990 ◽  
Vol 5 (3) ◽  
pp. 138-144 ◽  
Author(s):  
M. Martinazzi ◽  
F. Crivelli ◽  
C. Grassi ◽  
C. Zampatti

The present study reports the immunohistochemical reactivity of the monoclonal antibody b-12 (MAb b-12) with malignant human tissues. 173 neoplastic tissues were tested: MAb b-12 stained all breast carcinomas independently of their histology, with different patterns within the various type of cancer. Some other carcinomas (stomach, bowel, ovary, lung, endometrium), were also reactive even if the fraction of positive cells was lower. A comparison between the histological localization of MCA and that of CEA was performed; anti-CEA antibodies stained the cancer tissues with different reactivity and showed different percentages of positivity. MCA expression was also compared with other biological parameters such as the presence of estrogen receptors (ER), progesterone receptors (PgR), epithelial growth factor receptors (EGF-R), and oncoprotein p-53 which is encoded by the oncogene N-myc. The proliferative activity was also evaluated by measuring the growth fraction (GF) using the antibody Ki67. Any correlation was demonstrated between MCA and these parameters except for growth fraction as revealed by Ki67 antibody.


2019 ◽  
Vol 27 (7) ◽  
pp. 744-752
Author(s):  
Canan Kelten Talu ◽  
Taha Cumhan Savli ◽  
Gulben Erdem Huq ◽  
Cem Leblebici

We aimed to determine the histopathological differences between primary breast carcinomas with neuroendocrine features (NEBC) and carcinomas mimicking neuroendocrine features (NEBC-like). Twenty-three cases with NEBC, all showing positive staining for synaptophysin and/or chromogranin-A in ≥50% of tumor cells and 36 cases with NEBC-like (no staining for neuroendocrine [NE] markers but suspicious for NE morphology in terms of solid/trabecular growth patterns) were included in the study. Significant differences were found between the groups in terms of the patients’ ages, histologic/nuclear grade of tumor, lymphovascular invasion, comedo-type ductal carcinoma in situ (DCIS), microcalcification, Ki-67 proliferation index, nuclear shape, and level of peritumoral lymphocytic infiltration. The presence of large-size solid cohesive groups of tumor cells; plasmocytoid, spindle, and/or columnar shapes of tumor cells; and eosinophilic-granular appearance of cytoplasm were mostly noted in the NEBC group. The presence of small- to medium-sized solid cohesive groups of tumor cells; high-grade histologic and nuclear features; clear cytoplasm; and round to ovoid nucleus were mostly noted in the NEBC-like group. No significant differences were found in terms of tumor size, ER/PR/HER2 status, as well as the presence of DCIS, elastosis, extracellular/intracellular mucin, signet ring cells, apocrine features, and accompanying papilloma or ductal ectasia. In conclusion, small- to medium-sized solid cohesive groups of tumor cells, high-grade features, clear cytoplasm, round to ovoid shape of nucleus, lymphovascular invasion, comedo-type DCIS, microcalcification, high level of Ki-67 proliferation index (≥20%), and moderate/strong level of peritumoral lymphocytic infiltration might support non-NE features in breast carcinomas.


2018 ◽  
Vol 4 (4) ◽  
Author(s):  
Vladimír Bartoš ◽  
Millada Kullová

Purpose: Overexpression of antiapoptotic B-cell lymphoma-2 (Bcl-2) protein is one of the major contributors to oncogenesis and high levels have been identified in a variety of tumour types. We investigated an immunohistochemicalexpression of Bcl-2 protein in cutaneous basal cell carcinomas (BCCs) to elucidate whether there are differences in the expression pattern related to tumour growth phenotype.Materials and Methods: The study group consisted of 45 cutaneous BCCs, which were categorised into the nonaggressive (NA-BCCs; 31 cases) and aggressive histologic variants (A-BCCs; 14 cases).Results: There were 3 tumours (6.6%) with negative staining and 42 tumours (93.4%) with positive staining for Bcl-2 protein, 10 of which (23.8%) displayed low and remaining 32 cases (76.2%) exhibited high expression. All three “Bcl-2 negative” BCCs showed aggressive-growth features (infiltrative subtypes). When Bcl-2 values were evaluated as negative/low versus high expression, there was significantly lower Bcl-2 protein expression in the A-BCCs comparedto the NA-BCCs. Even an intensity of immunostaining showed a tendency of being weaker in the A-BCCs. In spite of that, three infiltrative BCCs showed a diffuse strong immunoreactivity.Conclusion: An immunohistochemical positivity of Bcl-2 protein in the neoplastic cells of cutaneous BCC was nearly constant feature, and its decreased staining was associated with an infiltrative growth pattern. It suggests that a lowBcl-2 protein expression in tumor tissue might be considered an unfavorable prognostic indicator.Key words: Basal cell carcinoma, B-cell lymphoma-2 protein, biological behavior


Blood ◽  
2004 ◽  
Vol 104 (11) ◽  
pp. 3949-3949
Author(s):  
Weiqiang Gao ◽  
Jiang Su ◽  
Xia Bai ◽  
Fei Shen ◽  
Changgeng Ruan

Abstract von Willebrand factor-cleaving protease/ADAMTS13 is a plasma metalloproteinase that degrades unusually large von Willebrand factor multimers (UL-vWF) derived from endothelial cells (ECs) and megakaryocytes (MCs) into small peptides circulating in blood. It is documented that transcript mRNAs of the protease are present in many human tissues; however, the protein expression of ADAMTS13 remains to be elucidated. In the present work, the gene of metalloproteinase domain of human ADAMTS13 was cloned into the multiclone site of pET28a(+). After induced by IPTG, the recombinant protein was purified using a Ni-NTA column and the Bal b/c mice were immunized with the protein. Screened with ELISA, three monoclonal antibodies against the metalloproteinase domain of ADAMTS13 were obtained and two of them, SZ-112 and SZ-113, were further evaluated. Both of them belonged to IgG1 subclass. The quantity of them in ascites were 4 mg/ml, and their titers were as high as 1×10−5. The data of competitive ELISA showed that SZ-112 and SZ-113 recognized different epitopes of the recombinant protein. Western blot results demonstrated that SZ-112 not only reacted against the recombinant protein, but also recognized the full-length recombinant ADAMTS13 protein that expressed in CHO cell line (the vectors containing the ADAMTS13 cDNA sequences were provided by Prof. Sadler JE). The immunoprecipitation results showed that the two antibodies could react to an approximately 200 KDa protein in platelet lysate. Then, the expression panels of ADAMTS13 in human normal tissues were investigated using immunohistochemistry with the monoclonal antibodies. And the protease was found to be present in many kinds of tissues such as liver, spleen, ovary, prostate, bladder, small intestine, thyroid and thymus with significantly positive staining. The protease was also present in lung, uterus, large intestine and heart but stained weakly. We did not found the protease in brain. In most of these organs, the protease was expressed in epithelium of the tissues. While in liver, spleen and thymus, it was mainly presented in a subgroup of the solid tissue cells. Moreover, the preliminary results showed that the expression of ADAMTS13 slightly decreased in liver tissues of patients suffering form hepatitis type B and cirrhosis. In conclusion, our data indicated that two novel monoclonal antibodies against the metalloproteinase domain of human ADAMTS13 were successfully prepared, and the expression of ADAMTS13 in different tissue and specific locality might be associated with the regulation and function of the protease, which would contribute to the further research of the deficiency mechanism of the proteases in some disorders.


1999 ◽  
Vol 23 (5) ◽  
pp. 439-445 ◽  
Author(s):  
Carlos Serra Díaz ◽  
Francisco Vizoso ◽  
Juan C. Rodríguez ◽  
Antonio M. Merino ◽  
Luis O. González ◽  
...  

1985 ◽  
Vol 33 (4) ◽  
pp. 295-302 ◽  
Author(s):  
T N Wight ◽  
G J Raugi ◽  
S M Mumby ◽  
P Bornstein

Affinity-purified antisera against thrombospondin were used to locate the presence of this glycoprotein in frozen sections of several human tissues by immunofluorescence techniques. Immunostaining was observed in the peritubular connective tissue and in basement membrane regions beneath glandular epithelium in skin and lung. Intense immunostaining was observed at the dermal-epidermal junction in skin and in small blood vessels throughout this tissue. Skeletal muscle exhibited positive staining with anti-thrombospondin antisera within interstitial areas. Immunostaining was confined to the luminal portions of large blood vessels such as aorta. In large blood vessels that contained lesions of atherosclerosis, immunostaining was observed throughout the lesion area and was especially prominent surrounding some of the lesion cells. These results indicate that thrombospondin is located within the matrix of a variety of human tissues and supports the suggestion that this glycoprotein is an endogenous component of some extracellular matrices.


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