Cathepsin B in infiltrated lymph nodes is of prognostic significance for patients with nonsmall cell lung carcinoma

Werle, Bernd; Kraft, Clemens; Lah, Tamara T.; Kos, Janko; Schanzenbächer, Ulrike; Kayser, Klaus; Ébert, W.; Spieß, Eberhard

doi:10.1002/1097-0142(20001201)89:11<2282::aid-cncr17>3.3.co;2-w

Cited by 7 publications

(6 citation statements)

References 7 publications

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“…Control experiments in the absence of primary antibodies were run in parallel using the same procedure. The specificity of the antibodies was controlled with preincubation with the antigen as reported [46,47]. Fluorescence microscopy was performed using a Zeiss LSM 510 confocal microscope.…”

Section: Immunofluorescencementioning

confidence: 99%

Inhibitory properties of cystatin F and its localization in U937 promonocyte cells

et al. 2005

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Human papain-like cathepsins were long believed to be responsible for terminal protein degradation in the lysosomes. This view changed dramatically when they were found to be involved in a number of important cellular processes, such as antigen presentation [7]. Their high proteolytic potential, which can be very harmful, requires the activity of papain-like cathepsins to be strictly regulated. Their endogenous protein inhibitors act as one of the main means of regulation [8]. The best characterized are the cystatins, which comprise a superfamily of evolutionarily related proteins, each consisting of at least one domain of 100-120 amino acid residues with conserved sequence motifs [8][9][10][11]. Type I cystatins (the stefins), stefins A and B, are cytosolic, % 100 amino acid residue-long proteins lacking disulfide bridges. Type II cystatins, cystatins C, D, E ⁄ M, F, S, SA, SN are longer extracellular proteins, consisting of % 120 amino acid residues and containing two disulfide bridges. Type III cystatins, the kininogens, are large multifunctional plasma proteins, containing three type II cystatin-like domains.Cystatin F was discovered recently by three independent groups. Two of them identified it by cDNA cloning and named the new inhibitor leukocystatin [12]

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Section: Immunofluorescencementioning

confidence: 99%

Inhibitory properties of cystatin F and its localization in U937 promonocyte cells

et al. 2005

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“…The cysteine proteases of the papain family, particularly cathepsins B, H and L, have been closely linked to tumor progression in multiple tumor types [2-4]. The prognosis of several major cancers has also been correlated with tumor cysteine proteinase expression in several recent studies [5,6]. Although the specific roles of cysteine proteases in metastasis remain unclear, undoubtedly these proteases participate in invasive degradation of extracellular matrix components in conjunction with other classes of proteases [7].…”

Section: Introductionmentioning

confidence: 99%

Cathepsin L increases invasion and migration of B16 melanoma

Yang

Cox

2007

Cancer Cell Int

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Background: Most cancers express elevated protease levels which contribute to certain aspects of tumor behavior such as growth, metastatic spread, and angiogenesis. Elevation of the cathepsins of the cysteine protease family correlates with increased invasion of tumor cells. Cysteine proteases such as cathepsins B, H and L type participate in tumor cell invasion as extracellular proteases, yet are enzymes whose exact roles in metastasis are still being elucidated.

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“…Cathepsin B is a lysosomal cysteine proteinase with broad substrate specificity and which, among other functions, appears to play a role in cancer progression due to its matrix-degrading properties by catalyzing the breakdown of several components of the ECM (Yan et al, 1998). Cathepsin B protein levels and activity levels have been found to be higher in many human tumors, including breast, lung, head and neck, melanoma, prostate, colon, glioma and lung Demchik et al, 1999;McKerrow et al, 2000;Werle et al, 2000;Harbeck et al, 2001;Fernandez et al, 2001). Although a few studies have observed a correlation between cathepsin B mRNA overexpression and tumor invasion, numerous studies have focused on cathepsin B expression at the level of protein and activity.…”

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Determination of Cathepsin B Expression May Offer Additional Prognostic Information for Ovarian Cancer Patients

Scorilas

Fotiou²,

Tsiambas³

et al. 2002

Biological Chemistry

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The lysosomal cysteine proteinase cathepsin B has been implicated in the progression of various human tumors including ovarian cancer. Included in this study were 63 patients with epithelial ovarian carcinoma. Follow-up information (median follow-up period 7 years) was available for all patients, among whom 42 (66.7%) had relapsed and 32 (50.8%) had died. The immunohistochemistry method was adopted for the detection of cathepsin B using paraffin embedded specimens. Results were compared to clinico-pathological data. Statistical analysis showed cathepsin B expression to be significantly associated with the stage of disease, debulking success and interestingly, with progesterone receptors. It was also inversely related to progression-free survival (PFS) and overall survival (OS). Accordingly, cathepsin B can be regarded as unfavorable and as an independent tumor marker for progression-free survival and overall survival in ovarian cancer patients with long follow-up.

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Cathepsin B in infiltrated lymph nodes is of prognostic significance for patients with nonsmall cell lung carcinoma

Cited by 7 publications

References 7 publications

Inhibitory properties of cystatin F and its localization in U937 promonocyte cells

Inhibitory properties of cystatin F and its localization in U937 promonocyte cells

Cathepsin L increases invasion and migration of B16 melanoma

Determination of Cathepsin B Expression May Offer Additional Prognostic Information for Ovarian Cancer Patients

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