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Vol. 45. Núm. 3.
Páginas 87-95 (Enero 2002)
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Vol. 45. Núm. 3.
Páginas 87-95 (Enero 2002)
Acceso a texto completo
Expresión y significación clínica del pepsinógeno C y la colagenasa-3 en el carcinoma de endometrio
Expression and clinical significance of pepsinogen C and collagenase-3 in endometrial carcinoma
Visitas
3172
J. Vázqueza,
Autor para correspondencia
jvrojo@eresmas.com

Correspondencia: Servicio de Ginecología. Hospital de Jove.Avda. Eduardo Castro, s/n. 33290 Gijón. Asturias.
, F. Vizosob, L.O. Gonzálezc, P. Vérezd, M. Mulerod, M.L. Lamelasa, A.M. Merinoe
a Servicios de Ginecología. Hospital de Jove. Gijón. Asturias.
b Servicios de Cirugía General. Hospital de Jove. Gijón. Asturias.
c Servicios de Anatomía Patológica. Hospital de Jove. Gijón. Asturias.
d Servicios de Medicina Interna. Hospital de Jove. Gijón. Asturias.
e Servicio de Anatomía Patológica. Hospital de Cabueñes de Gijón. Asturias.
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Resumen
Objetivo

Analizar la expresión tumoral del pepsinógeno C y de la colagenasa-3 en el adenocarcinoma de endometrio y la relación con las características de las pacientes y de sus tumores

Sujetos y métodos

Analizamos retrospectivamente mediante análisis inmunohistoquímico, utilizando anticuerpos monoclonales, 58 pacientes diagnosticadas y tratadas de adenocarcinoma de endometrio

Resultados

Se detectó pepsinógeno C en 21 tumores (36%) y colagenasa-3 en 30 (51%). La expresión de estas proteínas se asoció significativamente con la profundidad de la invasión miometrial, de forma que a mayor invasión del miometrio, menor expresión de pepsinógeno C y mayor de colagenasa-3 (p < 0,005 y p < 0,02, respectivamente). El análisis combinado de ambas enzimas proteolíticas predijo significativamente el grado de invasión miometrial (p < 0,001)

Conclusión

Un porcentaje significativo de adenocarcinomas de endometrio expresan pepsinógeno C y colagenasa-3, lo cual refleja un comportamiento biológico diferente, y pueden ser útiles en la predicción preoperatoria de la invasión miometrial en el cáncer de endometrio

Palabras clave:
Pepsinógeno C
Colagenasa-3
Invasión miometrial
Cáncer de endometrio
Receptores de andrógenos
Abstract
Objective

To analyze pepsinogen C and collagenase-3 expression in endometrial adenocarcinoma and their relationship with patient and tumoral characteristics

Subjects And Methods

We retrospectively analyzed 58 patients with endometrial adenocarcinomas through immunohistochemical assays using monoclonal antibodies

Results

Pepsinogen C expression was found in 21 tumors (36%) and collagenase-3 expression was found in 30 (51%). Expression of these proteins was significantly associated with myometrial invasion. The deeper the myometrial invasion, the lesser the pepsinogen C expression and the greater the collagenase-3 expression (p < 0.005 and p < 0.02, respectively). The combined assays of pepsinogen C and collagenase-3 significantly predicted the depth of myometrial invasion (p < 0.001)

Conclusions

Pepsinogen C and collagenase-3 are expressed in a significant percentage of endometrial adenocarcinomas. These proteolytic enzymes behave differently in this type of tumor and might be useful in the preoperative diagnosis of myometrial invasion

Keywords:
Pepsinogen C
Collagenase-3
Myometrial invasion
Endometrial cancer
Androgen receptor
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Bibliografía
[1.]
C.E. Platz, J.A. Benda.
Female genital tract cancer.
Cancer, 75 (1995), pp. 270-294
[2.]
I.M. Samloff.
Peptic ulcer: the many proteinases of aggression.
Gastroenterology, 96 (1989), pp. 586-595
[3.]
I. Díez-Itza, A.M. Merino, J. Tolivia, F. Vizoso, L.M. Sánchez, C. López- Otín.
Expression of pepsinogen C in human breast tumors and correlation with clinopathologic parameters.
Br J Cancer, 68 (1993), pp. 637-640
[4.]
A.M. Merino, J. Vázquez, J.C. Rodríguez, R. Fernández, I. Quintela, L.O. González, et al.
Pepsinogen C expression in tumors of extragastric origen.
Int J Biol Markers, 15 (2000), pp. 165-170
[5.]
F. Vizoso, L.M. Sánchez, I. Díez-Itza, A.M. Merino, López-Otín.
Pepsinogen C is a new prognostic marker in primary breast cancer.
J Clin Oncol, 13 (1995), pp. 54-61
[6.]
A. Scorilas, E.P. Diamandis, M.A. Levesque, A. Papanastasiou Diamandi, M.J. Khosravi, M. Giai, et al.
Immunoenzymatically determined pepsinogen C concentration in breast cytosols: an independent favourable prognosis factor in node-positive patients.
Clin Cancer Res, 5 (1999), pp. 1778-1785
[7.]
M. Balbín, C. López-Otín.
Hormonal regulation of the human pepsinogen C gene in breast cancer cells.
J Biol Chem, 271 (1996), pp. 15175-15181
[8.]
J.M.P. Freije, I. Díez-Itza, M. Balbín, L.M. Sánchez, R. Blasco, J. Tolivia, et al.
Molecular cloning and expression of collagenase-3, a novel human matrix metalloproteinase produced by breast carcinomas.
J Biol Chem, 24 (1994), pp. 16766-16773
[9.]
M. Stahle-Bäckdahl, B. Sandsted, K. Bruce, A. Lindhal, M.G. Jimenez, J.A. Vega, et al.
Collagenase-3 (MMP13) is expressed during human fetal ossification and re-expressed in postnatal bone remodeling and in rheumatoid arthritis.
Lab Invest, 76 (1997), pp. 717-728
[10.]
M. Balbín, A. Fueyo, J.M. López, I. Díez Itza, G. Velasco, C. López- Otín.
Expression of collagenase-3 in the rat ovary during the ovulatory process.
J Endocrinol, 149 (1996), pp. 405-415
[11.]
L.R. Lund, J. Romer, T.H. Bugge, B.S. Nielsen, T.L. Frandsen, J.L. Degen, et al.
Functional overlap between two classes of matrix degrading proteases in wound healing.
Embo J, 18 (1999), pp. 4645-4656
[12.]
D. Mao, J.K. Lee, S.J. VanVickle, R.W. Thompson.
Expression of collagenase-3 (MMP-13) in human abdominal aortic aneurysm and vascular smooth muscle cells in culture.
Biochem Biophys Res Commun, 261 (1999), pp. 904-910
[13.]
P.G. Mitchell, H.A. Magna, L.M. Reeves, L.L. Lopresti-Morrow, S.A. Yocum, P.J. Rosner, et al.
Cloning, expression and type II collagenolytic activity if matrix metalloproteinase-13 from human osteoarthritic cartilage.
J Clin Invest, 97 (1996), pp. 761-768
[14.]
V. Knäuper, C. López-Otín, B. Smith, G. Knight, G. Murphy.
Biochemical characterization of human collagenase-3.
J Biol Chem, 271 (1996), pp. 1544-1550
[15.]
J.L. Ashworth, G. Murphy, M.J. Rock, M.J. Sherratt, S.D. Shapiro, C.A. Shuttleworth, et al.
Fibrillin degradation by matrix metalloproteinases implications for connective tissue remodeling.
Biochem J, 340 (1999), pp. 171-181
[16.]
K. Airola, N. Johansson, A.L. Kariniemi, V.M. Kähäri, U.K. Saarialho-Kere.
Human collagenase-3 is expressed in malignant squamous epithelium of the skin.
J Invest Dermatol, 109 (1997), pp. 225-231
[17.]
M. Cazorla, L. Hernández, A. Nadal, M. Balbín, J.M. López, F. Vizoso, et al.
Collagenase-3 overexpression is associated with advanced local extension in human squamous cell carcinomas of the larynx.
[18.]
N. Johansson, M. Vaalamo, S. Grenman, S. Hietanen, P. Klemi, U. Saarialho-Kere, et al.
Collagenase-3 (MMP-13) is expressed by tumor cells in invasive vulvar squamous cell carcinomas.
Am J Pathol, 154 (1999), pp. 469-480
[19.]
J.A. Uría, M. Balbín, C. López Otín, J. Álvarez, F. Vizoso, M. Takigawa, et al.
Collagenase-3 expression in chondrosarcoma cells and its regulation by basic fibroblast growth factor.
Am J Pathol, 153 (1998), pp. 91-101
[20.]
K. Airola, T. Karonen, M. Vaalamo, K. Lehti, J. Lohi, A.L. Kariniemi, et al.
Expression of collagenase-1 and –3 and their ainhibitors TIMP-1 and –3 correlates with the level of invasion in malignant melanomas.
Br J Cancer, 80 (1999), pp. 733-743
[21.]
L.A. Liotta, K. Tryggvason, S. Garbisa, I. Hart, C.M. Foltz.
Metastatic potential correlates with enzimatic degradation of basement membrane collagen.
Nature, 284 (1980), pp. 67-68
[22.]
W. Creasman, F. Odicino, P. Maisonneuve, J. Bendet, J. Shepherd, M. Sideri, et al.
Carcinoma of the corpus uteri.
J Epidemiol Biostat, 1 (1998), pp. 35-61
[23.]
B. Foltmann, A.L. Jensen.
Human Prograstricsin. Analysis of intermediates during activation into gastricsin and determination of the aminoacid sequence of the propart.
Eur J Biochem, 128 (1982), pp. 63-70
[24.]
P.J. Boström, L. Ravanti, N. Reunanen, V. Aaltonen, K. Söderström, V. Kähäri, et al.
Expression of collagenase-3 (matrix metalloproteinase-13) in transitional-cell carcinoma of the urinary bladder.
Int J Cancer, 88 (2000), pp. 417-423
[25.]
C.Y.F. Young, B.T. Montgomery, P.E. Andrews, S. Qiu, D.L. Bilhartz, D.J. Thindall.
Hormonal regulation of prostate-specific antigen messenger RNA in human prostatic adenocarcinoma cell line LNCaP.
Cancer Res, 51 (1991), pp. 3748-3752
[26.]
P. Murtha, D.J. Thindall, C.Y.F. Young.
Androgen induction of a human prostate-specific kallikrein, hKLK2: characterization of an androgen response element in the 5' promoter region of the gene.
Biochemistry, 32 (1993), pp. 6459-6464
[27.]
P.B. Szecsi, H. Halgreeen, R.N.S. Wong, T. Kjaer, J. Tang.
Cellular origin, complementary deoxyribonucleic acid and N-terminal amino acid sequences of human seminal progastricsin.
Biol Reprod, 53 (1995), pp. 227-233
[28.]
G. Prodi, G. Nicoletti, C. De Giovanni, M.C. Galli, S. Grilli, P. Nanni, et al.
Multiple steroid hormone receptors in normal and abnormal human endometrium.
J Cancer Res Clin Oncol, 98 (1980), pp. 173-183
[29.]
R. Hackenberg, K.D. Schulz.
Androgen receptor mediated growth control of breast cancer and endometrial cancer modulated by antiandrogen- and androgen-like steroids.
J Steroid Biochem Mol, 56 (1996), pp. 113-117
[30.]
X. Zhu, A.A.I. Daffada, C.M.W. Chan, M. Dowsett.
Identification of an exon 3 deletion splice variant androgen receptor mRNA in human breast cancer.
Int J Cancer, 72 (1997), pp. 574-580
[31.]
W.H. Rodgers, L.M. Matrisian, L.C. Gludice, B. Dsupin, P. Cannon, C. Svitek, et al.
Patterns of matrix metalloproteinase expression in cycling endometrium imply differential functions and regulation by steroid hormones.
J Clin Invest, 94 (1994), pp. 946-953
[32.]
E. Marbaix, I. Kokorine, J. Donnez, Y. Eeckhout, P.J. Courtoy.
Regulation and restricted expression of interstitial collagenase suggest a pivotal role in the initiation of menstruation.
Hum Reprod, 11 (1996), pp. 134-143
[33.]
K. Wolf, P. Sandner, A. Kurtz, W. Moll.
Messenger ribonucleic acid levels of collagenase (MMP-13) and matrilisin (MMP-7) in virgin, pregnant and postpartum uterus and cervix of rat.
Endocrinology, 137 (1996), pp. 5429-5434
[34.]
F. Vizoso, M.L. Lamelas, A.M. Merino, L. González, J.C. Rodríguez, J. Vázquez, et al.
Colagenasa-3: un nuevo marcador pronóstico de evolución desfavorable en el cáncer de mama. XXI Congreso Nacional de Cirugía. Madrid, (4-8 de noviembre de 1996),
[35.]
A. Uría, M. Stahle-Bäckdahl, M. Seiki, A. Fueyo, C. López-Otín.
Regulation of collagenase-3 expression in human breast carcinomas is mediated by stromal-epithelial cell interactions.
Cancer Res, 57 (1997), pp. 4882-4888
[36.]
N. Johansson, K. Airola, R. Grénman, A.L. Kariniemi, U. Saarialho- Kere, V.M. Kähäri.
Expression of collagenase-3 (matrix metalloproteinase-13) in squamous cell carcinomas of the head and neck.
Am J Pathol, 151 (1997), pp. 499-508
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