The coagulative factors of normal human and human cancer tissue

Boggust, W. A.; O'Brien, D.; O’Meara, R. A. Q.; Thornes, R. D.

doi:10.1007/bf02948555

Cited by 47 publications

(16 citation statements)

References 4 publications

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“…Evidence from several laboratories has suggested that malignant cells produce higher levels of "thromboplastic" coagulation factors than normal cells (41)(42)(43), but clear definition of these factors has been difficult to obtain. Although there is evidence that suggests that malignant cells produce an abnormal coagulation activity that is not associated with normal cells (9-13),6 it has not been clear whether this is a known coagulation factor or whether it is something unique to the malignant state.…”

Section: Introductionmentioning

confidence: 99%

A factor X-activating cysteine protease from malignant tissue.

Gordon¹,

Cross²

1981

J. Clin. Invest.

224

109

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A B S T R A C T A proteolytic procoagulant has been identified in extracts of human and animal tumors and in cultured malignant cells. It directly activated Factor X but its similarity to other Factor X-activating serine proteases was not clear. This study describes work done to determine whether this enzyme, cancer procoagulant, is a serine or cysteine protease. Purified cancer procoagulant from rabbit V2 carcinoma was bound to a p-chloromercurialbenzoate-agarose affinity column and was eluted with dithiothreitol. The initiation of recalcified, citrated plasma coagulation activity by cancer procoagulant was inhibited by 5 mM diisopropylfluorophosphate, 1 mM phenylmethylsulfonylfluoride, 0.1 mM HgCl2, and 1 mM iodoacetamide. Activity was restored in the diisopropylfluorophosphate-, phenylmethylsulfonylfluoride-, and HgCl2-inhibited samples by 5 mM dithiothreitol; iodoacetamide inhibition was irreversible. Russell's viper venom, a control Factor Xactivating serine protease, was not inhibited by either 0.1 mM HgCl2 or 1 mM iodoacetamide. The direct activation ofFactor X by cancer procoagulant in a two-stage assay was inhibited by diisopropylfluorophosphate and iodoacetamide. Diisopropylfluorophosphate inhibits serine proteases, and an undefined impurity in most commercial preparations inhibits cysteine proteases. Hydrolysis of diisopropylfluorophosphate with CuS04 and imidazole virtually eliminated inhibition of thrombin, but cancer procoagulant inhibition remained complete, suggesting that cancer procoagulant was inhibited by the undefined impurity. These results suggest that cancer procoagulant is a cysteine endopeptidase, which distinguishes it from other coagulation factors including tissue factor. This and other data suggest that neoplastic cells produce this unique cysteine protease which may initiate blood coagulation.

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Section: Introductionmentioning

confidence: 99%

A factor X-activating cysteine protease from malignant tissue.

Gordon¹,

Cross²

1981

J. Clin. Invest.

224

109

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“…The nature of the Cancer Coagulative Factor, or CCF, as described by O'Meara, has been elaborated upon since its early description (O'Meara, 1960;O'Meara and Thornes, 1961;Thornes and O'Meara, 1961 ;Boggust et al, 1963;Thornes, 1967). Ambrus (1966) has found an increase in overall thromboplastin activity in neoplastic tissue compared with adjacent normal tissue in a variety of human tumors.…”

mentioning

confidence: 97%

Tumor fluid thromboplastin activity

Frank

1968

Intl Journal of Cancer

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The thromboplastin activity of T‐241 Lewis sarcoma peripheral fluid and control subcutaneous fluid in C57BL/6Ja male mice was measured, using a calcium reconstitution assay. The material was collected in Millipore filter chambers. At low dilutions of the collected material there was a statistically significant increase in clotting activity of the tumor peripheral fluid. The calcium ion concentration of the collected fluid was also measured. It was also noted that gels were found more frequently, and in larger amounts, in the chambers in tumor‐bearing animals than in the controls.

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“…The implication of thrombin in tumor cell-induced platelet activation has long been known since tumor tissue and extracts were known to possess greater procoagulant activ ity than normal tissues [ 17]; there are several early investigations on this subject [18,19] that, together with more recent experimental evidence, indicate that the generation of thrombin is a crucial step in tumor-cellinduced platelet activation.…”

Section: Generation O F Thrombinmentioning

confidence: 99%

Platelet Contribution to the Formation of Metastatic Foci: The Role of Cancer Cell-Induced Platelet Activation

Bastida¹,

Ordinas²

1988

Pathophysiol Haemos Thromb

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Platelets are thought to be involved in the development of blood borne metastasis. Ultrastructural and experimental studies demonstrate that association between tumor cells and platelets with subsequent activation of the coagulation cascade takes place in malignancy. Several hypotheses have been proposed to explain the mechanisms by which tumor cells activate platelets including generation of thrombin, ADP release and involvement of arachidonate metabolism. Perfusion studies with human homologous systems showed that intact tumor cells and tumor cell microvesicles were able to induce platelet thrombogenicity under defined flow conditions. The presence of divalent cations and plasma factors was necessary for the cancer cells to exert their activating capacity. These results suggest a role for platelets in the development of secondary metastasis as well as in the thrombotic events of malignancy.

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The coagulative factors of normal human and human cancer tissue

Cited by 47 publications

References 4 publications

A factor X-activating cysteine protease from malignant tissue.

A factor X-activating cysteine protease from malignant tissue.

Tumor fluid thromboplastin activity

Platelet Contribution to the Formation of Metastatic Foci: The Role of Cancer Cell-Induced Platelet Activation

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