Fibrin formation on vessel walls in hyperplastic and malignant prostate tissue

Wojtukiewicz, Marek Z.; Zacharski, Leo R.; Memoli, Vincent A.; Kisiel, Walter; Kudryk, Bohdan J.; Möritz, Thomas; Rousseau, Sandra M.; Stump, David C.

doi:10.1002/1097-0142(19910301)67:5<1377::aid-cncr2820670517>3.0.co;2-2

Cited by 39 publications

(27 citation statements)

References 54 publications

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“…These results renew interest in evaluating the role of specific coagulation proteases in cancer specific molecular pathways in prostate cancer as previously a lack of expression of coagulation pathway proteins in malignant prostatic tissue had been suggested. In an extensive evaluation of several coagulation factors in prostate tissue, no expression of F VII, FXa, factor XIII, protein S, and protein C was detected (17), while prothrombin–thrombin expression in prostatic tissue had not been reported. This led to generally concluding that prostate tumor cells lack expression of coagulation proteins unlike several other tumor types.…”

Section: Discussionmentioning

confidence: 99%

Thrombin Expression in Prostate: A Novel Finding

Kohli

Williams

Yao

et al. 2010

Cancer Investigation

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Introduction A variable repertoire of coagulation protein expression is observed in different cancers. We evaluated expression of thrombin in prostate tissue. Methods Detection of thrombin was performed using quantitative real-time PCR in fresh tissue and in situ hybridization (ISH) in archival prostate tissue and by immunohistochemistry of prostate tissue microarrays. Results (Pro)thrombin mRNA expression was detected in cancer tissue and localized to prostatic epithelium and stroma by ISH. Thrombin protein was detected in stroma of benign and malignant epithelium (p <.05). Conclusions Prostate tissue is a rich reservoir of thrombin. This may have potential for developing antithrombin-based cancer therapy.

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Section: Discussionmentioning

confidence: 99%

Thrombin Expression in Prostate: A Novel Finding

Kohli

Williams

Yao

et al. 2010

Cancer Investigation

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“…Associated with fibrin and clot formation, Factor XIIIA was increased in bone relative to liver and lymph node metastases. Factor XIIIA expression has not been observed in benign hyperplastic and neoplastic prostate tissue [26]. Factor XIII is a transglutaminase activated by thrombin producing factor XIIIA that can cross-link fibrin, stabilizing the clot [27].…”

Section: Discussionmentioning

confidence: 99%

“…Strong PAI-1 expression in carcinoma cells was seen in high-grade tumors, but only fibroblastic expression was related to invasion [37]. Wojtukiewicz et al [26], observed no tissue staining for PAI-1 in benign hyperplastic and neoplastic prostate tissue. It should also be noted that Usher et al [35], have investigated the expression of uPA and PAI-1 mRNAs by in situ hybridization, as well as the expression of PAI-1 proteins by immunohistochemistry and found that these components are expressed only in stromal cells in PCa and benign prostatic hyperplasia.…”

Section: Discussionmentioning

confidence: 99%

Differential expression of angiogenesis associated genes in prostate cancer bone, liver and lymph node metastases

Morrissey

True

Roudier

et al. 2007

Clin Exp Metastasis

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Our objective was to elucidate phenotypic differences between prostate cancer (PCa) liver, lymph node, and bone metastases. PCa metastases were obtained through a rapid tissue acquisition necropsy protocol. We grossly dissected metastatic foci from frozen samples and performed expression analyses using cDNA microarrays. Immunohistochemical analyses using a tissue microarray from thirty individuals with PCa metastases to lymph nodes, liver, and bone was used to confirm the gene expression changes associated with each metastatic site. Transcript alterations statistically-associated with bone metastases included increased expression of IBSP (Bone sialoprotein), F13A1 (factor XIII), and decreased expression of EFNA1 (ephrin-A1) and ANGPT2 (angiopoietin-2) when compared to liver and lymph node metastases. The metastasis-associated changes in proteins involved in coagulation and angiogenesis prompted further analysis of additional factors known to participate in the clotting cascade and blood vessel formation (angiopoitein-1, PAI-1, uPA, PAI-RBP-1 and hepsin). We also assessed tumor-associated microvessel density and distribution in liver, lymph node, and bone metastasis. Intense fibrin(ogen) and fibulin-1 staining was localized to epithelial cells at the periphery of metastatic tumors possibly to facilitate angiogenesis. The expression of hepsin, uPA, PAI-RBP1, PAI-1, and factor XIII may influence fibrinolysis and are regulated by the tumor microenvironment. The expression of angiopoietin-2 and apparent silencing of angiopoietin-1 in PCa bone, liver, and lymph node metastases may be critical for angiogenesis in this tumor type. In addition, the resulting tumor-associated microvessel density and distribution was significantly different between liver and bone metastasis possibly in response to the protein expression changes detailed above.

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“…Both FBG and fibrin have been localized to the tumor‐host cell interface 7,8. Fibrin is abundant in different types of tumors9–13 such as primary brain lesions14 and prostate cancer 15. Tumor cell associated fibrin deposition is also found in small cell carcinoma of the lung, renal carcinoma and malignant melanoma in association with activated coagulation factors such as Factor XIIIa or Xa, indicative of thrombin generation at the primary tumor site.…”

Section: Fibrin(ogen) and Cancermentioning

confidence: 99%

Tumors and Fibrinogen

Simpson-Haidaris

Rybarczyk

2001

Annals of the New York Academy of Sciences

249

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The progression of a tumor from benign and localized to invasive and metastatic growth is the major cause of poor clinical outcome in cancer patients. Much like in a healing wound, the deposition of fibrin(ogen), along with other adhesive glycoproteins, into the extracellular matrix (ECM) serves as a scaffold to support binding of growth factors and to promote the cellular responses of adhesion, proliferation, and migration during angiogenesis and tumor cell growth. Inappropriate synthesis and deposition of ECM constituents is linked to altered regulation of cell proliferation, leading to tumor cell growth and malignant transformation. Fibrin deposition occurs within the stroma of a majority of tumor types. In contrast, abundant FBG, not fibrin, is present within the stroma of breast cancers. It is thought to originate from exudation of plasma FBG and subsequent deposition into the tumor stroma and not endogenous synthesis and secretion of FBG by breast tumor cells. However, we show that MCF‐7 human breast cancer cells synthesize and secrete FBG polypeptides, suggesting that the origin of FBG in the stroma of breast carcinoma may be due to endogenous synthesis and deposition. Moreover, FBG assembles into ECM as conformationally altered FBG, not as fibrin. Studies in our laboratory demonstrate that FBG alters the ability of breast cancer cells to migrate. Together, the results of studies from our laboratory, as well as the laboratories of others, indicate that the presence of fibrin(ogen) within the tumor stroma likely affects the progression of tumor cell growth and metastasis. This review focuses on FBG within tumors and its relationship with other tumor constituents, ultimately focusing on the role of FBG in breast cancer.

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Fibrin formation on vessel walls in hyperplastic and malignant prostate tissue

Cited by 39 publications

References 54 publications

Thrombin Expression in Prostate: A Novel Finding

Thrombin Expression in Prostate: A Novel Finding

Differential expression of angiogenesis associated genes in prostate cancer bone, liver and lymph node metastases

Tumors and Fibrinogen

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