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2.
J Mol Biomark Diagn ; 1(Suppl 2)2016 Jun.
Artículo en Inglés | MEDLINE | ID: mdl-27358750

RESUMEN

BACKGROUND: The finding of new biomarkers is needed to have a better sub-classification of primary renal tumors (RCC) as well as more reliable predictors of outcome and therapy response. In this study, we evaluated the role of circulating FGF21, an endocrine factor, as a diagnostic and prognostic biomarker for ccRCC. MATERIALS AND METHODS: Serum samples from healthy controls (HC), clear cell and chromophobe RCC cancer patients were obtained from the serum biobank "Biobanco Público de Muestras Séricas Oncológicas" (BPMSO) of the "Instituto de Oncología "Ángel H. Roffo". Serum FGF21 and leptin were measured by ELISA while other metabolic markers were measured following routinely clinical procedures. RESULTS: One of our major findings was that FGF21 levels were significantly increased in ccRCC patients compared with HC. Moreover, we showed an association between the increased serum FGF21 levels and the shorter disease free survival in a cohort of 98 ccRCC patients, after adjustment for other predictors of outcome. CONCLUSION: Our results suggest that higher FGF21 serum level is an independent prognostic biomarker, associated with worse free-disease survival.

3.
Oncol Rep ; 27(4): 1041-8, 2012 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-22246562

RESUMEN

Colorectal cancer (CRC) is the third most common malignant neoplasm worldwide. The objective of this study was to examine whether carnosic acid (CA), the main antioxidant compound of Rosmarinus officinalis L., would inhibit the cell viability of three CRC cell lines: Caco-2, HT29 and LoVo in a dose-dependent manner, with IC50 values in the range of 24-96 µM. CA induced cell death by apoptosis in Caco-2 line after 24 h of treatment and inhibited cell adhesion and migration, possibly by reducing the activity of secreted proteases such as urokinase plasminogen activator (uPA) and metalloproteinases (MMPs). These effects may be associated through a mechanism involving the inhibition of the COX-2 pathway, because we have determined that CA downregulates the expression of COX-2 in Caco-2 cells at both the mRNA and protein levels. Therefore, CA modulates different targets involved in the development of CRC. These findings indicate that carnosic acid may have anticancer activity and may be useful as a novel chemotherapeutic agent.


Asunto(s)
Abietanos/farmacología , Antineoplásicos Fitogénicos/farmacología , Movimiento Celular/efectos de los fármacos , Proliferación Celular/efectos de los fármacos , Neoplasias Colorrectales/patología , Extractos Vegetales/farmacología , Inhibidores de Proteasas/farmacología , Apoptosis/efectos de los fármacos , Células CACO-2 , Adhesión Celular/efectos de los fármacos , Supervivencia Celular/efectos de los fármacos , Neoplasias Colorrectales/genética , Neoplasias Colorrectales/metabolismo , Ciclooxigenasa 2/genética , Ciclooxigenasa 2/metabolismo , Relación Dosis-Respuesta a Droga , Regulación hacia Abajo , Células HT29 , Humanos , Concentración 50 Inhibidora , Metaloproteinasa 2 de la Matriz/metabolismo , Metaloproteinasa 9 de la Matriz/metabolismo , Inhibidores de la Metaloproteinasa de la Matriz , ARN Mensajero/metabolismo , Factores de Tiempo , Activador de Plasminógeno de Tipo Uroquinasa/antagonistas & inhibidores , Activador de Plasminógeno de Tipo Uroquinasa/metabolismo
4.
Curr Pharm Biotechnol ; 12(11): 1900-8, 2011 Nov.
Artículo en Inglés | MEDLINE | ID: mdl-21470134

RESUMEN

This review presents recent information about the cross-talk between the tumor cells and the microenvironment in the target organ of metastasis at the premetastatic and metastatic stage. The development of metastatic foci is driven not only by the tumor cells intrinsic properties, but also by the interplay with resident and foreign cells located at particular niches in the target organ. The primary tumor modulates the metastatic target through the production of soluble factors that mobilize cells from distant organs like the bone marrow, which in turn localize in the metastatic niche. There is also strong evidence indicating that some primary tumors induce a fertile ground for the tumor cell at the target organ even before the arrival of the disseminated tumor cell (premetastatic niche). The relationship between the players of the metastatic setting is dynamic and shows a high degree of plasticity. Tumor cells change through the acquisition of genetic and/or epigenetic alterations that provide adaptive advantages and the metastatic niche is remodeled by incoming cell types or newly secreted soluble mediators, as a result a reciprocal dialogue is established that invokes new levels of molecular and cellular complexity. Unraveling the mechanisms that sustain the metastatic niche will allow a better understanding of the biology of the disseminated tumor cell, the design of new therapeutic approaches and, hopefully, the improvement of cancer patients' survival.


Asunto(s)
Células de la Médula Ósea , Comunicación Celular , Metástasis de la Neoplasia/patología , Células Neoplásicas Circulantes , Lesiones Precancerosas/patología , Microambiente Tumoral , Animales , Células de la Médula Ósea/metabolismo , Células de la Médula Ósea/patología , Progresión de la Enfermedad , Humanos , Células Neoplásicas Circulantes/metabolismo , Células Neoplásicas Circulantes/patología , Especificidad de Órganos , Lesiones Precancerosas/metabolismo
5.
Breast Cancer Res Treat ; 119(3): 559-74, 2010 Feb.
Artículo en Inglés | MEDLINE | ID: mdl-19288189

RESUMEN

Glypican-3 (GPC3) is a proteoglycan involved in proliferation and cell survival. Several reports demonstrated that GPC3 is downregulated in some tumors, such as breast cancer. Previously, we determined that GPC3 reexpression in the murine mammary adenocarcinoma LM3 cells induced an impairment of their invasive and metastatic capacities, associated with a decrease of their motility and an increase of their cell death. We demonstrated that GPC3 inhibits canonical Wnt signaling, as well as it activates non canonical pathway. Now, we identified signaling pathways responsible for the pro-apoptotic role of GPC3 in LM3 cells. We found for the first time that GPC3 inhibits the PI3K/Akt anti-apoptotic pathway while it stimulates the p38MAPK stress-activated one. We report a concomitant modulation of CDK inhibitors as well as of pro- and anti-apoptotic molecules. Our results provide new clues regarding the mechanism involved in the modulation induced by GPC3 of mammary tumor cell growth and survival.


Asunto(s)
Adenocarcinoma/metabolismo , Apoptosis/fisiología , Neoplasias de la Mama/metabolismo , Glipicanos/metabolismo , Transducción de Señal/fisiología , Adenocarcinoma/genética , Animales , Western Blotting , Neoplasias de la Mama/genética , Línea Celular Tumoral , Separación Celular , Femenino , Citometría de Flujo , Expresión Génica , Regulación Neoplásica de la Expresión Génica , Glipicanos/genética , Inmunohistoquímica , Ratones , Fosfatidilinositol 3-Quinasas/metabolismo , Proteínas Proto-Oncogénicas c-akt/metabolismo , Reacción en Cadena de la Polimerasa de Transcriptasa Inversa , Proteínas Quinasas p38 Activadas por Mitógenos/metabolismo
6.
Diabetes Metab Res Rev ; 26(1): 50-8, 2010 Jan.
Artículo en Inglés | MEDLINE | ID: mdl-19943326

RESUMEN

BACKGROUND: Although hyperfibrinogenemia and insulin resistance are common in obesity and diabetes mellitus, the impact of obesity per se on fibrinogen turnover and the insulin effects on fibrinogen and protein kinetics is unknown. METHODS: We measured fibrinogen and albumin fractional (FSR) and absolute (ASR) synthesis rates, as well as protein turnover, in non-diabetic, obese and in control male subjects both before and following an euglycemic, euaminoacidemic, hyperinsulinemic clamp, using L-[(2)H(3)]-Leucine isotope infusion. RESULTS: In the obese, basal fibrinogen concentrations was approximately 25% greater (p < 0.035), and fibrinogen pool approximately 45% greater (p < 0.005), than in controls. Both FSR and ASR of fibrinogen were similar to control values. With hyperinsulinemia, although fibrinogen FSR and ASR were not significantly modified with respect to baseline in either group, fibrinogen ASR resulted to be approximately 50% greater in the obese than in controls (p < 0.015). Hyperinsulinemia equally stimulated albumin synthesis and suppressed leucine appearance from endogenous proteolysis in both groups. Amino acid clearance was also similar. In the obese, the insulin-mediated glucose disposal was approximately 50% lower (p < 0.03) than in controls, and it was inversely correlated with fibrinogen ASR during the clamp in both groups (r = - 0.58). CONCLUSIONS: In obese, non-diabetic males, post absorptive fibrinogen production is normal. Whole-body amino acid disposal, basal and insulin-responsive protein degradation, and albumin synthesis are also normal. However, the greater fibrinogen ASR in the obese with hyperinsulinemia, and the inverse relationship between insulin sensitivity and clamp fibrinogen production, suggest a role for hyperinsulinemia and/or insulin resistance on fibrinogen production in obesity.


Asunto(s)
Fibrinógeno/metabolismo , Insulina/farmacología , Obesidad/metabolismo , Adulto , Aminoácidos/metabolismo , Glucemia/metabolismo , Presión Sanguínea , Índice de Masa Corporal , Superficie Corporal , Proteína C-Reactiva/metabolismo , Colesterol/sangre , Fibrinógeno/efectos de los fármacos , Humanos , Insulina/sangre , Molécula 1 de Adhesión Intercelular/sangre , Interleucina-6/sangre , Masculino , Persona de Mediana Edad , Obesidad/sangre , Obesidad/fisiopatología , Valores de Referencia , Trombomodulina/sangre , Factor de Necrosis Tumoral alfa/sangre , Molécula 1 de Adhesión Celular Vascular/sangre
7.
Nutr Metab Cardiovasc Dis ; 19(11): 789-96, 2009 Dec.
Artículo en Inglés | MEDLINE | ID: mdl-19346115

RESUMEN

BACKGROUND AND AIM: Hyperfibrinogenemia, a cardiovascular risk factor, is frequent in hypertension and largely unexplained. In this study, we measured fibrinogen production and whole-body protein turnover under both basal and hyperinsulinemic states, in hypertensive [H] and control [C] subjects, using a leucine stable isotope tracer and precursor-product relationships. METHODS AND RESULTS: Since hypertension is often a feature of the "metabolic", insulin resistance syndrome, which in turn affects both fibrinogen kinetics and whole-body protein turnover, we selected hypertensive subjects without the metabolic syndrome. Following basal measurements, an euglycemic, approximately euaminoacidemic, hyperinsulinemic clamp was performed, with plasma insulin raised to 700-900 pmol/L. In H, rates of the fractional and absolute synthesis (FSR and ASR, respectively) of fibrinogen were 30%-40% greater (p<0.05 or less) than in C in both states, whereas leucine turnover was normal. Hyperinsulinemia did not modify fibrinogen synthesis in either group with respect to baseline, whereas it suppressed leucine appearance from endogenous proteolysis by approximately 40% to same extent in both groups. Amino acid clearance was similar in both the H and C subjects. In H, the insulin-mediated glucose disposal (M) was approximately 25% lower, (although insignificantly) than in controls, showing no overall insulin resistance. There was an inverse correlation between M and fibrinogen FSR during the clamp. CONCLUSIONS: In essential hypertension fibrinogen production is increased, is not further stimulated by insulin, and is inversely related to insulin sensitivity at high-physiological insulin concentrations. Amino acid disposal and basal as well as insulin-responsive protein degradation rates are instead normal.


Asunto(s)
Fibrinógeno/metabolismo , Hiperinsulinismo/metabolismo , Hipertensión/metabolismo , Insulina/administración & dosificación , Adulto , Biomarcadores/metabolismo , Glucemia/metabolismo , Estudios de Casos y Controles , Deuterio , Fibrinógeno/biosíntesis , Glucosa/administración & dosificación , Técnica de Clampeo de la Glucosa , Humanos , Hiperinsulinismo/sangre , Hipertensión/sangre , Técnicas de Dilución del Indicador , Infusiones Intravenosas , Insulina/sangre , Cinética , Leucina/administración & dosificación , Masculino , Persona de Mediana Edad , Péptido Hidrolasas/metabolismo , Regulación hacia Arriba
8.
Amino Acids ; 34(3): 507-9, 2008 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-17514490

RESUMEN

In plasma and serum, the presence of high-abundance proteins can overwhelm the signals of low-abundance proteins, which then become undetectable either by two-dimensional gels or chromatographic techniques. Therefore, depletion of abundant proteins is a prerequisite to detect low-abundance components. Furthermore, the regeneration of pre-purification tools could be money-saving. We applied an affinity chromatography kit to remove albumin and the immunoglobulin chains from plasma and propose a simple and effective technical procedure for the regeneration of these affinity columns.


Asunto(s)
Inmunoglobulina G/sangre , Proteómica/métodos , Albúmina Sérica/análisis , Albúmina Sérica/metabolismo , Cromatografía de Afinidad , Electroforesis en Gel Bidimensional , Humanos , Factores de Tiempo
9.
Breast Cancer Res Treat ; 80(2): 221-32, 2003 Jul.
Artículo en Inglés | MEDLINE | ID: mdl-12908826

RESUMEN

Glypican-3 (GPC3), a proteoglycan bound to the cell membrane through a GPI anchor, is widely expressed in the embryo but down regulated in most adult tissues, with some exceptions as mammary cells. GPC3 is involved in the regulation of cell proliferation and survival in specific cell types. LM3, a murine mammary tumor cell line unable to express GPC3, was stably transfected with the rat GPC3 gene to analyze its role in tumor progression. Upon injection into syngeneic BALB/c mice LM3-GPC3 clones showed less local invasiveness and developed fewer spontaneous and experimental lung metastasis than controls. GPC3-expressing cells were more sensitive to apoptosis induced by serum depletion, exhibited a delay in the first steps of spreading and were less motile than controls. On the other hand, LM3-GPC3 cells were significantly more adherent to FN than control ones. We observed that GPC3 transfectants presented a higher expression of E-cadherin and beta-catenin, molecules whose down regulation has been associated with tumor progression. Exogenous TGF-beta increased MMP-9 activity in both control and GPC3-expressing cells, but did not modulate MMP-2. Contrarily, GPC3 expression prevented the increase of MMP-2 activity induced by IGF-II. Our results suggest that GPC3 has a protective role against mammary cancer progression.


Asunto(s)
Proteoglicanos de Heparán Sulfato/genética , Neoplasias Pulmonares/metabolismo , Neoplasias Mamarias Animales/metabolismo , Animales , Northern Blotting , Western Blotting , Cadherinas/metabolismo , Línea Celular Tumoral , Proteínas del Citoesqueleto/metabolismo , Modelos Animales de Enfermedad , Femenino , Glipicanos , Proteoglicanos de Heparán Sulfato/metabolismo , Inmunohistoquímica , Factor II del Crecimiento Similar a la Insulina/farmacología , Neoplasias Pulmonares/secundario , Neoplasias Mamarias Animales/patología , Ratones , Ratones Endogámicos BALB C , Invasividad Neoplásica , Metástasis de la Neoplasia , Ratas , Transactivadores/metabolismo , Transfección , Factor de Crecimiento Transformador beta/farmacología , beta Catenina
10.
Oncol Rep ; 10(5): 1647-52, 2003.
Artículo en Inglés | MEDLINE | ID: mdl-12883753

RESUMEN

During tumor development, growth factors may act in autocrine manner stimulating cell proliferation, or in paracrine manner affecting the microenvironment of the tumor and modulating the immune system. Murine mammary adenocarcinoma M3 tumor bearers develop lung metastases and leukocytosis during its evolution. Previously we described that M3 conditioned media enhanced metastasis incidence, when it was inoculated in tumor-operated mice. In the present study we determine that spleen cells from M3 tumor operated mice treated with M3 conditioned media, were able to transfer the capacity to enhance metastasis to other tumor operated mice. Spleen cells have immune suppressor activity that could be reversed by cyclophosfamide treatment. M3 tumor cells secrete GM-CSF, which is able to promote in vitro proliferation of M3 cells as well as spleen cells. This proliferation could be abrogated by the addition of anti-GM-CSF. We report that the GM-CSF secreted by M3 tumor cells had stimulatory activity on M3 tumor cell and lymphocyte proliferation.


Asunto(s)
Adenocarcinoma/inmunología , Adenocarcinoma/metabolismo , Factor Estimulante de Colonias de Granulocitos y Macrófagos/metabolismo , Neoplasias Mamarias Animales/inmunología , Neoplasias Mamarias Animales/metabolismo , Adenocarcinoma/patología , Animales , Antineoplásicos Alquilantes/farmacología , Células de la Médula Ósea/metabolismo , División Celular , Células Cultivadas , Ensayo de Unidades Formadoras de Colonias , Medios de Cultivo Condicionados/farmacología , Ciclofosfamida/farmacología , Progresión de la Enfermedad , Femenino , Neoplasias Pulmonares/secundario , Masculino , Ratones , Ratones Endogámicos BALB C , Metástasis de la Neoplasia , Bazo/citología , Bazo/metabolismo
16.
Nat Prod Lett ; 16(2): 95-100, 2002 Apr.
Artículo en Inglés | MEDLINE | ID: mdl-11990434

RESUMEN

A protocol for shoot induction from callus of Haplophyllum patavinum was established. Two known furoquinoline (skimmianine and haplopine), and three quinolone (edulinine, ribalinine and isoplatydesmine) alkaloids were isolated for the first time from plant material, callus and shoot cultures of this species. The structures of these compounds have been characterised on the basis of spectroscopic evidence.


Asunto(s)
Alcaloides/aislamiento & purificación , Compuestos Heterocíclicos con 3 Anillos/aislamiento & purificación , Plantas Medicinales/química , Quinolinas/aislamiento & purificación , Quinolonas/aislamiento & purificación , Rutaceae/química , Alcaloides/química , Técnicas de Cultivo , Compuestos Heterocíclicos con 3 Anillos/química , Italia , Espectrometría de Masas , Estructura Molecular , Quinolinas/química , Quinolonas/química , Espectrometría de Masa por Ionización de Electrospray
17.
Int J Oncol ; 18(3): 639-47, 2001 Mar.
Artículo en Inglés | MEDLINE | ID: mdl-11179499

RESUMEN

LP07 is a new cell line derived from P07 lung tumor, spontaneously arisen in a BALB/c mouse. LP07 is composed of heterogeneous epithelioid polyhedric cells that proliferate at a slow rate, have low plating efficiency and are unable to grow in soft agar. Only some LP07 cells expressed cytokeratins while most of them were positive for vimentin. Ultrastructure studies showed that LP07 cells established rudimentary intercellular unions, formed glandular-like conducts and presented conspicuous secretory granules, suggesting an epithelial-glandular origin, with neuroendocrine components. Upon injection LP07 cells formed poorly differentiated non-invasive adenocarcinomas, and tumor bearing mice developed leukocytosis, hypercalcemia and cachexia. This tumor cell line constitutes a useful tool to study lung tumor biology and paraneoplastic syndromes.


Asunto(s)
Adenocarcinoma/patología , División Celular/fisiología , Neoplasias Pulmonares/patología , Síndromes Paraneoplásicos/patología , Adenocarcinoma/sangre , Animales , Recuento de Células Sanguíneas , Peso Corporal , Calcio/sangre , Pruebas de Carcinogenicidad , Adhesión Celular , Linaje de la Célula , Movimiento Celular , Cromosomas/genética , Análisis Citogenético , Modelos Animales de Enfermedad , Femenino , Técnicas para Inmunoenzimas , Neoplasias Pulmonares/sangre , Neoplasias Pulmonares/secundario , Ratones , Ratones Endogámicos BALB C , Microscopía Electrónica , Trasplante de Neoplasias , Síndromes Paraneoplásicos/sangre , Células Tumorales Cultivadas , Activador de Plasminógeno de Tipo Uroquinasa/metabolismo
18.
Breast Cancer Res Treat ; 69(1): 39-51, 2001 Sep.
Artículo en Inglés | MEDLINE | ID: mdl-11759827

RESUMEN

Target organ of metastasis determines the fate of metastasis. The soluble factors released from one or more cell types in the new stroma may influence growth and survival of metastatic cells. In the present study, we used conditioned media from the kidney, liver and lung, the latter being the target organ of metastasis of murine mammary adenocarcinoma cell lines LM3, LMM3 and F3II, to assess whether the soluble factors released from these organs could modulate in vitro survival of these cell lines after apoptosis-inducing treatments and to investigate the mechanisms involved in this effect. We demonstrate that conditioned medium from lung, but not from liver or kidney, promotes survival of these cells after doxorubicin, cisplatin, agonistic anti-Fas antibody and serum withdrawal treatments. Furthermore, LMM3 cells treated with lung conditioned medium after doxorubicin exposure maintained their tumorigenic capacity and metastatic potential. Neither IGF nor EGF could promote survival but, surprisingly, TGF-beta could reduce sensitivity of LMM3 cells to doxorubicin in vitro. Doxorubicin treatment induced Bax expression and down-regulated Bcl-2 expression. In contrast, lung conditioned medium increased Bcl-2 expression and inhibited doxorubicin-mediated Bcl-2 down-regulation. Neither of those treatments alone modified Bcl-X(L) expression, although co-treatment induced a 3- to 5-fold increase of its expression. These results suggest that the lung microenvironment could promote metastasis of these adenocarcinoma cell lines by increasing survival of metastatic cells, possibly by modulation of Bcl-2 protein family expression.


Asunto(s)
Adenocarcinoma/patología , Apoptosis , Regulación Neoplásica de la Expresión Génica , Riñón/patología , Hígado/patología , Pulmón/patología , Neoplasias Mamarias Animales/patología , Metástasis de la Neoplasia/patología , Proteínas Proto-Oncogénicas c-bcl-2/biosíntesis , Animales , Antineoplásicos/farmacología , Supervivencia Celular , Medios de Cultivo , Doxorrubicina/farmacología , Femenino , Masculino , Ratones , Ratones Endogámicos BALB C , Solubilidad , Células del Estroma , Células Tumorales Cultivadas
19.
Oncol Rep ; 7(6): 1395-9, 2000.
Artículo en Inglés | MEDLINE | ID: mdl-11032951

RESUMEN

There is accumulating evidence that cysteine proteinase activity plays an important role in cancer cell invasion and metastasis. Previously we demonstrated that cathepsin B (CB) plasma activity is increased in patients with transitional bladder cancer (TCC). In this work we have attempted to determine whether urine CB protein levels could be used as tumor marker in bladder cancer patients. Urine CB levels were evaluated employing a dot blot method, in 30 patients with TCC, 21 patients successfully treated from TCC without evidence of disease at the moment of urine collection (NED) and in 30 healthy volunteers. The median value (Md) of the control group was 3.8 microg CB/ml. Significantly higher urine CB values (Md: 5.9 microg/ml) were found in the TCC group. A high CB value was also found in the NED group (5.0 microg/ml). Urine CB values over the 5.2 microg/ml (cut-off point) were observed in 63% of TCC patients, 48% of NED and 8% of the control group. Only 4% NED patients had CB values over 13.0 microg/ml while 33% of TCC patients surpassed this value. Thus, urine CB might be a potential marker for transitional bladder cancer diagnosis.


Asunto(s)
Biomarcadores de Tumor/orina , Carcinoma de Células Transicionales/orina , Catepsina B/orina , Neoplasias de la Vejiga Urinaria/orina , Adulto , Anciano , Anciano de 80 o más Años , Carcinoma de Células Transicionales/patología , Carcinoma de Células Transicionales/terapia , Supervivencia sin Enfermedad , Femenino , Humanos , Immunoblotting , Masculino , Persona de Mediana Edad , Análisis Multivariante , Sensibilidad y Especificidad , Neoplasias de la Vejiga Urinaria/patología , Neoplasias de la Vejiga Urinaria/terapia
20.
Int J Cancer ; 89(4): 389-94, 2000 Jul 20.
Artículo en Inglés | MEDLINE | ID: mdl-10956415

RESUMEN

Matrix metalloproteinases (MMP) have been implicated in tumor invasion and metastasis. We verified, by gelatin zymography, MMP activity in the euglobulin plasma fraction of 82 healthy controls, 66 patients with benign diseases and 149 patients with breast, lung, colon or brain cancer. The euglobulin fractions assayed showed 4 gelatinolytic bands of 62, 92, 120 and 200 kDa. The median (Md) value for 92 kDa-MMP activity was significantly increased in breast (Md 1.34 arbitrary units [AU]/ml plasma, range 0.0-7.2) and lung cancer patients (Md 1.43 AU/ml, range 0.0-3.6) compared with the controls (Md 0.48 AU/ml, range 0.0-1.8). Patients with colon cancer or gliomas presented values of MMP-9 similar to those of the healthy population. Multivariate analysis indicated that plasma MMP-9 activity was not predicted by the known clinicopathological parameters such as age, stage, tumor size, number of positive lymph nodes, histologic grade, histologic type, nuclear grade or mitotic index. Lung cancer patients also presented high values of MMP-9 (Md 1.43, range 0.0-3.6 [n = 26]), without association with tumor stage or histologic type. The levels of 92 kDa-MMP activity in the plasma euglobulin fraction could be a potentially useful tumor marker in breast and lung cancer.


Asunto(s)
Biomarcadores de Tumor/sangre , Neoplasias de la Mama/enzimología , Neoplasias Pulmonares/enzimología , Metaloproteinasa 2 de la Matriz/sangre , Metaloproteinasa 9 de la Matriz/sangre , Seroglobulinas/metabolismo , Adenocarcinoma/sangre , Adenocarcinoma/enzimología , Adulto , Anciano , Anciano de 80 o más Años , Astrocitoma/sangre , Astrocitoma/enzimología , Neoplasias Encefálicas/sangre , Neoplasias Encefálicas/enzimología , Neoplasias de la Mama/sangre , Neoplasias del Colon/sangre , Neoplasias del Colon/enzimología , Femenino , Glioblastoma/sangre , Glioblastoma/enzimología , Humanos , Neoplasias Pulmonares/sangre , Masculino , Persona de Mediana Edad
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