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At least 19 recordsLinked to original sources
PubMed2005

Expression of N-acetyl transferase human and human Arrest defective 1 proteins in thyroid neoplasms.

Protein acetylation is an important posttranslational modification regulating oncogenesis, apoptosis and cell cycle. NATH (N-acetyl transferase human) is overexpressed at the mRNA level in papillary thyroid carcinomas relative to non-neoplastic thyroid tissue. The NATH protein has recently been demonstrated to be the partner of hARD1 (human Arrest defective 1) and this complex acetylates the N-termini of proteins. ARD1 has also been implicated in the destabilization of the transcription factor HIF-1alpha (hypoxia inducible factor-1alpha). Using human thyroid papillary carcinoma biopsies and NATH- and hARD1-specific antibodies, we examined the levels of endogenous NATH and hARD1 proteins in 27 patients. We demonstrate that NATH protein level is upregulated in neoplastic versus non-neoplastic tissue in good accordance with our previous mRNA findings. In all tumors in which NATH was downregulated compared to non-neoplastic tissue, the hARD1 protein level was concomitantly reduced. SiRNA-mediated knockdown of NATH resulted in decreased levels of hARD1 protein. Taken together, these results suggest that NATH positively affects the level of hARD1 protein both in vivo and in cell cultures.

Acetyltransferases↗
PubMed2004

[Role of S100B protein in neoplasms and other diseases].

The S100 protein family constitutes the largest subgroup of the Ca binding proteins. To date 20 members of the family were discovered. S100 proteins regulate intracellular processes such as cell growth and motility, cell cycle regulation, transcription and differentiation. S100B protein is expressed constitutively by brain astrocytes. Serum S100B protein concentration in Stage II-III-IV melanoma is a reliable prognostic marker. The serum level of S100B protein is significant independent prognostic marker in respect to disease specific survival, it is a relevant marker for therapy monitoring and patient follow-up. It is recommended to determine the S100B expression pattern and intensity of the primary tumour of melanoma before therapy monitoring. Elevated S100B levels were published after head trauma, subarachnoidal haemorrhage and stroke. Furthermore, it indicates blood-brain barrier dysfunction. S100B protein was used to determine the cerebral damage after cardiovascular surgery as well.

Animals↗
PubMed1997

Immunoreaction at 43 kDa with anti-ubiquitin antibody in breast neoplasms.

Protein ubiquitination has been implicated in ATP-dependent protein turnover and normal cell proliferation. To investigate whether the ubiquitin-mediated system is functionally involved in the cancerous state, we examined changes in protein ubiquitination in 52 surgically resected primary breast tumors. Immunohistochemically, ubiquitin (Ub) was identified in the cytoplasm of cancer cells, which were stained more strongly than adjacent normal ductal epithelium. Corresponding immunoblot analysis of normal and neoplastic regions of human breast showed that the immunoreaction for Ub at about 43 kDa was increased in all of the tumors (100%), regardless of the clinical stage or histologic grade. This protein, which gave a single spot on two-dimensional gel electrophoresis, had partial amino acid sequences which were identical to those of actin family members. Our results suggest that ubiquitination of this 43-kDa protein may be involved in the carcinogenesis or biological characteristics of human breast neoplasms.

Amino Acid Sequence↗
PubMed2003

Expression and cellular localization of p8 protein in thyroid neoplasms.

OBJECTIVES: p8 protein has mitogenic activity and is linked to the development of pancreatic carcinoma. However, little is known about the expression and physiological significance of this protein in other human carcinomas. METHODS: In this study, we immunohistochemically investigated p8 expression in thyroid neoplasms as well as in the normal thyroid gland. RESULTS: p8 was expressed in normal follicular cells, but no normal thyroid was regarded as overexpressing p8. On the other hand, 44.3% of papillary carcinoma overexpressed p8 and the incidence was directly linked to the tumor size (p=0.0340) and lymph node metastasis (p=0.0145). In follicular tumors, the incidence of p8 overexpression did not depend on histological type. In anaplastic (undifferentiated) carcinoma, p8 was overexpressed only in 5.0%, which was significantly lower than in papillary (p=0.0006) and follicular carcinomas (p=0.0049). In normal follicules and follicular tumors, p8 was localized mainly in the nucleus except for two adenomas. On the other hand, p8 localization was more cytoplasmic in papillary carcinoma larger than 1.0 cm (p=0.0186) and with a poorly differentiated lesion (p=0.0313). CONCLUSIONS: These results suggest that the overexpression and cytoplasmic localization of p8 protein may reflect disease progression of papillary carcinoma, whereas this protein plays little part in thyroid carcinoma after anaplastic transformation.

Adenocarcinoma, Follicular↗
PubMed2003

Nuclear shift of hnRNP K protein in neoplasms and other states of enhanced cell proliferation.

The heterogeneous nuclear ribonucleoprotein K (hnRNP K), is a ubiquitously expressed protein that interacts with signal transducers, proteins that modulate gene expression and selective RNA and DNA motifs. K protein is modified in response to extracellular signals and directly regulates rates of transcription and translation. We used serum-treated hepatocyte culture, liver after partial hepatectomy and hepatic neoplasms as systems to compare expression, subcellular distribution and tyrosine phosphorylation of K protein in quiescent and dividing cells. The results show that expression of K protein mRNA was increased in states of enhanced proliferation. Levels of nuclear K protein were also higher in proliferating compared to resting cells. In contrast, levels of cytoplasmic K protein were the same or lower in dividing compared to quiescent cells. States of enhanced proliferation were also associated with increased levels of K protein tyrosine phosphorylation. Nuclear shift of K protein in dividing cells may reflect involvement of K protein in signalling multiple events that regulate expression of genes in proliferating cells.

Cell Culture Techniques↗
PubMedDate not supplied

[Immunohistochemical study of neoplasm-associated proteins in cerebellum medulloblastomas].

Tumor-associated proteins are studied immunohistochemically in 86 medulloblastomas (MB). Three main variants of their coexpression (70% of all cases studied) are distinguished. The 1st variant (24 cases): expression of Rb and nm23 proteins and the lack of tenascin expression. The 2nd variant (25 cases): tenascin expression and lack of Rb and nm23 expression. The 3rd variant (12 cases): the expression of tenascin, Rb, p53 and/or bc12. Tenascin-positive MB much more frequently expressed oncoproteins p53, bc12, c-erb B-2 and p30/32, and had higher indices of "growth fraction". Tenascin immunoreactivity and that of other oncoproteins prevailed in MB with desmoplasia and in tumors with immunohistochemical features of neuronal differentiation.

Adolescent↗
PubMed2000

Expression of promyelocytic leukaemia protein in thyroid neoplasms.

AIMS: Promyelocytic leukaemia protein (PML) is an oncoprotein involved in the pathogenesis of acute promyelocytic leukaemia and is localized in distinct PML nuclear bodies. Our previous observation of overexpression of the PML in hormone-sensitive normal tissues and malignant solid tumours, including the thyroid, led to this analysis of the PML expression in various thyroid neoplasms to characterize the importance of the PML in thyroid carcinogenesis. METHODS AND RESULTS: Immunohistochemistry was performed on paraffin-embedded tissue samples from 106 thyroid neoplasms after antigen retrieval by microwave. Immunoblotting was done with fresh frozen tissues in a few tumours. The PML was strongly expressed in all papillary carcinomas in diffuse or ball-shaped patterns. In the follicular neoplasms, the PML expression was variable, but there was no significant difference between adenomas and carcinomas. In the medullary carcinomas, the PML expression was either not detectable or was lower than in non-neoplastic thyroids. Quantitatively different expression of the PML in various thyroid neoplasms was confirmed by immunoblotting. CONCLUSION: A significant difference of the PML expression according to the type of thyroid neoplasms suggests that the PML is important in papillary thyroid carcinomas, and furthermore, that PML expression may be used in differential diagnosis of thyroid neoplasms.

Adenocarcinoma↗
PubMed2000

Mutations in the beta-propeller domain of the Drosophila brain tumor (brat) protein induce neoplasm in the larval brain.

Inactivation of both alleles of the fruit fly D. melanogaster brain tumor (brat) gene results in the production of a tumor-like neoplasm in the larval brain, and lethality in the larval third instar and pupal stages. We cloned the brat gene from a transposon-tagged allele and identified its gene product. brat encodes for an 1037 amino acid protein with an N-terminal B-boxl zinc finger followed by a B-box2 zinc finger, a coiled-coil domain, and a C-terminal beta-propeller domain with six blades. All these motifs are known to mediate protein-protein interactions. Sequence analysis of four brat alleles revealed that all of them are mutated at the beta-propeller domain. The clustering of mutations in this domain strongly suggests that it has a crucial role in the normal function of Brat, and defines a novel protein motif involved in tumor suppression activity. The brat gene is expressed in the embryonic central and peripheral nervous systems including the embryonic brain. In third instar larva brat expression was detected in the larval central nervous system including the brain and the ventral ganglion, in two glands - the ring gland and the salivary gland, and in parts of the foregut - the gastric caecae and the proventriculus. A second brat-like gene was found in D. melanogaster, and homologs were identified in the nematode, mouse, rat, and human. Accumulated data suggests that Brat may regulate proliferation and differentiation by secretion/transport-mediated processes.

Amino Acid Sequence↗
PubMed2000

Heat-shock proteins inhibit induction of prostate cancer cell apoptosis.

BACKGROUND: Resistance to apoptosis remains a significant problem in the treatment of prostate cancer. Heat-shock proteins (HSP) have been correlated with tumor progression. The role of HSP in prostate cancer resistance to apoptosis is unknown. METHODS: PC-3 and LNCaP prostate cancer cells were heat-shocked and then treated with or without diethyl-maleate, etoposide, cycloheximide, or 3 Gray irradiation. Percent apoptosis was assessed by propidium iodide DNA incorporation. Protein was also extracted for analysis by SDS-PAGE Western blotting. RESULTS: Western blotting confirmed an increase in HSP 27 and 72. These cells were resistant to both chemical- and radiation-induced apoptosis. Cycloheximide and specific oligonucleotides to HSP 72 blocked the increased expression of HSP 72 and the resistance to apoptosis. Mcl-1, Bcl-2, Bcl-X(L), and glutathione-S-transferase (GST) expression were increased in a time-dependent manner after heat shock. CONCLUSIONS: This study demonstrates that HSP expression, specifically HSP 72, inhibits apoptosis in prostate tumor cell lines, which may be mediated by the production of survival factors.

Antineoplastic Agents, Phytogenic↗