The Prevalence of Neoplasm Diseases and Investigation of Some Biochemical Serum Parameters

Aim: The aim of this work, investigating the skin, lung, and bone marrow-related cancer prevalence and biochemical serum parameters of all these cancer patients. Materials and Methods: The skin, lung, and bone marrow cancer patient's biochemical serum data were examined retrospectively using a hospital information system. Results: Basal cell carcinoma patients number were recorded as 155 with 63%, squamous cell carcinoma patients number were enrolled in73 with 30% and malign melanoma patients number were noted as 10 with 4%. Skin cancers were recorded to be the most seen cancer type in 246 patients with 22% between 2013-2017 years. All types of cancer patient's numbers were calculated as 1134 between these years. The very common incidences of basal cell carcinoma and squamous cell carcinoma cancers were observed on the upper part of the body, respectively on the face-cheek, nose, ear, eyelid, and lip. In this study, there was seen a statistically significant difference between skin cancer patient’s serum glucose, aspartate aminotransferase, alanine aminotransferase, sodium, bilirubin direct, bilirubin total, creatinine, urea level, and control group serum parameters level, p lt;0.05. The lung cancer patient numbers were recorded as 119 with 10.4 %, bone marrow patients numbers were enrolled in 113 with 10%. Two cancer groups were statistically different in terms of 5-years survival. Log Rank X2 = 8.68, p = 0.003, p lt;0.05. Conclusions: We recorded that skin cancer types and regions on the upper parts of the body were more because of exposure to the sun. The lung cancer survival rate was lower than bone marrow cancer. Moreover, we strongly emphasized that measuring the biochemical serum parameters was statistically significant in the diagnosis of cancer patients

A case of acromegaly in the presence of coincidental liver cirrhosis

Context: Acromegaly is a rare and serious syndrome and commonly associated with pituitary neoplasm. Classic cause of acromegaly in adults is the tumors of the somatotrophs that secrete growth hormone. Cirrhosis is the end stage of chronic liver disease and commonly a cause of death. It is characterized by diffuse hepatic fibrosis resulting in altered construction of the lobular parenchyma with widespread connective tissue scptae, circumscribed regenerative nodules of hepatocytcs and anastomoses between vascular channels linking portal and central vessels. Objective: To report the simultaneous cases of acromegaly and cirrhosis. Case report: A 62-year old, male patient came to the hospital complaining of severe abdominal swelling. Laboratory and imaging findings were compatible with the presence of hepatitis B virus related cirrhosis together with acromegaly. In this case, he had high GH level but lower IGF-1 level because of hepatic failure which can impair IGF-1 production by the liver. Definitive diagnosis was made by pituitary MR and a 1 cm in diameter tumor was detected. Conclusion: This paper showed that cirrhosis can result in a low IGF-I level in patients with acromegaly. There is no previous report available of the in the presence of coincidental combination of acromegaly and cirrhosis in a patient

INHIBITORY EFFECTS OF SOME PESTICIDES AND METALS ON CARBONIC ANHYDRASE PURIFIED FROM SHABUT FISH BARBUS GRYPUS ) GILL TISSUE

Carbonic anhydrase enzyme catalyzes the reversible inter-conversion of CO2 and HCO3. The enzyme is crucial for the osmotic balance and acid–base regulation in the fish. It is well-known that gills of fish play the most important role in acid–base relevant ion transfer, the transfer of H+ and/or HCO3, for the maintenance of systemic pH. Many researches have shown that fish are the species that is the most susceptible to environmental toxins. In addition, these toxins firstly encounter the gill tissue in fish. In this study, the carbonic anhydrase enzyme was purified 198.6-folds with 58.8% yield from Shabut Fish (Barbus grypus) gill tissue by Sepharose-4B-L-tyrosine-sulfanilamide affinity column. The specific activity was determined as 2.92 EU/mg protein. The molecular weight determined by sodium dodecyl sulfate–polyacrylamide gel electrophoresis was found to be about 29.9 kDa. Inhibitory effects of some pesticides (Spinosad and Dimethoate) and metal ions (Al3+, Cu2+, Ba2+, Fe2+, Mn2+, Se2+) were examined on the purified carbonic anhydrase enzyme. Inhibition graphics were drawn in order to find the IC50 values of metals and pesticides showing inhibition. The kinetic parameters of this enzyme were determined for its esterase activity, with 4-nitrophenyl acetate as substrate

An investigation of the mechanisms underlying the proteasome inhibitor bortezomib resistance in PC3 prostate cancer cell line

The phenomenon of acquired resistance to chemotherapeutic agents is a long-standing conundrum in cancer treatment. To help delineate drug resistance mechanisms and pave the way for the development of novel strategies, we generated a PC3 prostate cancer cell line resistant to proteasome inhibitor bortezomib for the first time. The resistant cells were found to have an IC50 value of 359.6 nM, whereas the IC50 value of parental cells was 82.6 nM after 24 h of treatment with varying doses of bortezomib. The resistant cells were also partly cross-resistant to the novel proteasome inhibitor carfilzomib; however, they were not resistant to widely used chemotherapeutic agent vincristine sulfate, indicating that enhanced cellular drug efflux via the multidrug resistance (MDR) transporters is not the molecular basis of the resistance. Since both bortezomib and carfilzomib target and inhibit the chymotrypsin-related activity residing in the beta 5 subunit of the proteasome (PSMB5), we next examined its expression and found surprisingly no significant alteration in the expression profile of the mature form. However, a significant increase in the accumulation of the precursor form of PSMB5 in response to 100 nM bortezomib was observed in the parental cells without a significant accumulation in the resistant cells. The results presented here thus suggest that the molecular mechanisms causing resistance to proteasome inhibitors need to be examined in-depth to overcome the resistance to ubiquitin-proteasome pathway inhibitors in cancer treatment

The p53-independent induction of apoptosis in breast cancer cells in response to proteasome inhibitor bortezomib

An important hallmark of cancer cells is acquired resistance toward apoptosis. The apoptotic pathway is the most well-defined cell death program and is characterized by several morphological and biochemical features. The tumor suppressor protein p53 is a critical regulator of apoptosis in many cell types. p53 stimulates a wide network of signals that act through either extrinsic or intrinsic pathways of apoptosis. However, a number of studies have shown that apoptosis can be induced in a p53-independent manner as well. In this study, we examined the mechanism of apoptosis in p53-null breast cancer cells in response to the proteasome inhibitor bortezomib. Initially, we determined the p53 status of 4T1 breast carcinoma and 4THMpc (a highly mestatic derivative of 4T1) cells and verified that both cells are p53 deficient. It was subsequently shown that apoptosis can be induced in both cells in a dose-dependent manner in response to bortezomib treatment, based on DNA fragmentation evidence. Western blot analyses of ubiquitin-protein conjugates additionally showed that the proteasome is potently inhibited by bortezomib in p53-null 4T1 and 4THMpc cells. The results presented in the current study also show that caspase-3 is significantly activated in response to the treatment with bortezomib, implying that induction of apoptosis in these p53-deficient cells is occuring via caspase-3. The additional results presented here suggest that the pro-apoptotic proteins Bad, Noxa, and Puma are not critical regulators of apoptosis induction in p53-null 4T1 and 4THMpc cells. Similarly, there was no difference in the expression level of Mcl-1 in treated cells, suggesting that this anti-apoptotic protein is also uninvolved in the apoptotic response resulting from bortezomib treatment. In contrast, a very significant upregulation of the anti-apoptotic protein Hsp25/27 was detected in these p53-deficient cells after treatment with bortezomib. If the increased expression of Hsp25/27 protein levels are muting the apoptotic effects of the bortezomib treatment, then the apoptosis-inducing effects of such proteasome inhibitors might be increased with approaches simultaneously inhibiting Hsp25/27 protein in p53-deficient cells