Concentrations of lysosomal cysteine proteases are decreased in renal cell carcinoma compared with normal kidney

Kirschke, H.; Clausen, Tobias; Göhring, Barbara; Günther, Dagmar; Heucke, Edwin; Laube, Friedemann; Löwe, Eckhard; Neef, H; Papesch, Henriette; Peinze, Skadi; Plehn, Gunnar; Rebmann, U.; Rinne, Ari; Rüdrich, Roland; Weber, Ekkehard

doi:10.1007/s004320050078

Cited by 4 publications

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“…Combined elevations of CatB and CatL appear to be common in patients with gastric carcinoma40, 41 and a combination of CatB, CatD, and CatL elevations appear to be common in patients with colorectal and breast carcinoma 42–45. However, reduced activities or immunoreactivities of CatB, CatH, and CatL in neoplasms have been reported: Prostate carcinoma and renal carcinoma tissue display decreased activities and immunoreactivities 26, 27. Other investigators found higher immunoreactivity for CatD in prostate carcinoma,16 suggesting that not all of the lysosomal proteases are regulated similarly and that the decrease or increase of one cathepsin activity or immunoreactivity does not simply reflect an increased number of lysosomes in the cells.…”

Section: Discussionmentioning

confidence: 99%

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Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma

Frőhlich¹,

Schlagenhauff²,

Möhrle

et al. 2001

Cancer

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BACKGROUND Increased activity of the protease cathepsin B has been demonstrated in many tumor cells. A correlation of cathepsin B activity and metastatic potential of melanoma has been well established. METHODS The cathepsins B, D, H, and L were evaluated in normal skin, nevi, and melanoma samples to obtain information about their role and their regulation in melanoma. The authors localized specific proteolytic activity with histochemistry, cathepsin protein immunohistochemistry, and mRNA with in situ hybridization. RESULTS Activities and immunoreactivities of the cathepsins B and L were found to be increased in all melanocytic lesions. However, the staining for the corresponding mRNA levels was elevated only in melanomas. Cathepsin D protein and mRNA were expressed to a higher degree only in the dysplastic nevus and in melanomas. The increase was due to tumor cells and cells of the surrounding tissue. Cathepsin H activity, immunoreactivity, and mRNA appeared to be correlated inversely with the invasive potential of the lesion. CONCLUSIONS It may be relevant for the malignant potential of the lesion whether the increase in activity is accompanied by an increase in the mRNA level. Two different mechanisms—the existence of different mRNAs and the higher transcription rate of the cathepsin gene—have been proposed for the regulation of cathepsin B activity in tumor cells. The current data suggest that, depending on the thickness of the melanoma, cathepsin activity is regulated by different mechanisms. The up‐regulation of cathepsin gene transcription appears to be characteristic for more invasive tumor cells. Cancer 2001;91:972–82. © 2001 American Cancer Society.

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Section: Discussionmentioning

confidence: 99%

“…Elevated levels of mRNA for CatD, CatH, or CatL have been detected in malignancies of bone, thyroid, breast, colon, and endometrium 22–25. In contrast to these reports, decreased cathepsin activities or immunoreactivities have been found in prostate and renal carcinomas 26, 27…”

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confidence: 93%

Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma

Frőhlich¹,

Schlagenhauff²,

Möhrle

et al. 2001

Cancer

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“…For the cathepsin B staining, free‐floating sections were quenched for 20 min in 3% hydrogen peroxide and 10% methanol before pre‐incubation with 5% goat serum in 0.25% Triton X‐100 for 1 h, followed by incubation at 4 °C overnight with rabbit anti‐(rat cathepsin B) antibody (1 : 5000; prepared from rat liver lysosomes, electrophoretically homogeneous, and no cross‐reactivities with other related lysosomal cysteine proteinases, i.e. cathepsin L, S, and H; Kirschke et al. , 1997; Fiebiger et al.…”

Section: Methodsmentioning

confidence: 99%

Caspase‐mediated death of newly formed neurons in the adult rat dentate gyrus following status epilepticus

Ekdahl

Mohapel

Weber

et al. 2002

Eur J of Neuroscience

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A large proportion of cells that proliferate in the adult dentate gyrus under normal conditions or in response to brain insults exhibit only short-term survival. Here, we sought to determine which cell death pathways are involved in the degeneration of newly formed neurons in the rat dentate gyrus following 2 h of electrically induced status epilepticus. We investigated the role of three families of cysteine proteases, caspases, calpains, and cathepsins, which can all participate in apoptotic cell death. Status epilepticus increased the number of bromodeoxyuridine (BrdU)-positive proliferated cells in the subgranular zone of the dentate gyrus. At the time of maximum cell proliferation, immunohistochemical analyses revealed protein expression of active caspase-cleaved poly (ADP-ribose) polymerase (PARP) in approximately 66% of the BrdU-positive cells, while none of them expressed cathepsin B or the 150-kDa calpain-produced fodrin breakdown product. To evaluate the importance of cysteine proteases in regulating survival of the newly formed neurons, we administered intracerebroventricular infusions of a caspase inhibitor cocktail (zVAD-fmk, zDEVD-fmk and zLEHD-fmk) over a 2-week period, sufficient to allow for neuronal differentiation, starting 1 week after the epileptic insult. Increased numbers of cells double-labelled with BrdU and neuron-specific nuclear protein (NeuN) marker were detected in the subgranular zone and granule cell layer of the caspase inhibitor-treated rats. Our data indicate that caspase-mediated cell death pathways are active in progenitor cell progeny generated by status epilepticus and compromise survival during neuronal differentiation.

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“…The measurements are often performed with the dipeptide Z-Phe-Arg-Amc as a substrate, which is specific for all papain-like cysteine proteases. Determination of the activity of particular enzymes present in (samples from) cell homogenates or physiological fluids requires the use of complex indirect methods, for instance with the use of specific inhibitors [11,12]. A different, simpler way would be to employ substrates specific for the chosen enzyme.…”

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Influence of Me2SO and incubation time on papain activity studied using fluorogenic substrates.

Szabelski

Stachowiak²,

Wiczk³

2001

Acta Biochim Pol

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Papain activity in a buffer containing Me2SO was studied using fluorogenic substrates. It was found that the number of active sites of papain decreases with increasing Me2SO concentration whereas the incubation time, in a buffer containing 3% Me2SO does not affect the number of active sites. However, an increase of papain incubation time in the buffer with 3% Me2SO decreased the initial rate of hydrolysis of Z-Phe-Arg-Amc as well as Dabcyl-Lys-Phe-Gly-Gly-Ala-Ala-Edans. Moreover, an increase of Me2SO concentration in working buffer decreased the initial rate of papain-catalysed hydrolysis of both substrates. A rapid decrease of the initial rate (by up to 30%) was observed between 1 and 2% Me2SO. Application of the Michaelis-Menten equation revealed that at the higher Me2SO concentrations the apparent values of k(cat)/Km decreased as a result of Km increase and kcat decrease. However, Me2SO changed the substrate binding process more effectively (Km) than the rate of catalysis k(cat).

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Concentrations of lysosomal cysteine proteases are decreased in renal cell carcinoma compared with normal kidney

Cited by 4 publications

References 0 publications

Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma

Activity, expression, and transcription rate of the cathepsins B, D, H, and L in cutaneous malignant melanoma

Caspase‐mediated death of newly formed neurons in the adult rat dentate gyrus following status epilepticus

Influence of Me2SO and incubation time on papain activity studied using fluorogenic substrates.

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