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PubMedDate not supplied

[Study of calcium ion binding by merlang parvalbumin according to changes in the parameters of the proteins own fluorescence].

The binding of Ca+ to whiting parvalbumin has been studied by intrinsic (tryptophan) protein fluorescence. It has been shown that parvalbumin can exist in three states, which are interpreted as the protein without Ca2+ (P), with one bound Ca2+ (PC) and with two bound Ca2+ (CPC). The spectra of the states have been identified and the protein fluorescence spectra at different Ca2+ concentration have been decomposed on the components corresponding to these states. Relative populations of the P, PC and CPC states have been plotted against Ca2+ concentration. On the basis of a scheme of the successive Ca2+ binding; P+Ck1 in equilibrium PC; PC+Ck2 in equilibrium CPC, corresponding theoretical dependences have been computed and fitted to the experimental ones. The fitted equilibrium constants K1 and K2, are 5.10(8) and 6.10(6)M-1, correspondingly. The schemes are in a good agreement with the experimental data on EGTA-titration of Ca2+-saturated parvalbumin and on pH-titration of parvalbumin in the presence of EGTA.

Animals↗
PubMed1993

Immunocytological detection of bone marrow micrometastasis in operable non-small cell lung cancer.

Present diagnostic techniques do not allow the detection of early metastatic spread of tumor cells, although this spread largely determines the clinical course of patients with small primary cancers. By use of monoclonal antibody CK2 to the epithelial cytokeratin component number 18 (CK18), individual disseminated carcinoma cells present in bone marrow of cancer patients can now be identified (G. Schlimok, I. Funke, B. Holzmann, G. Göttlinger, G. Schmidt, H. Häuser, S. Swierkot, H. H. Warnecke, B. Schneider, H. Koprowski, and G. Riethmüller, Proc. Natl. Acad. Sci. USA, 84: 8672-8676, 1987; F. Lindemann, G. Schlimok, P. Dirschedl, J. Witte, and G. Riethmüller, Lancet, 340: 685-689, 1992). In the present study, we applied this approach to patients with operable non-small cell lung cancer. CK18 was expressed on 84 of 88 (95.5%) primary adenocarcinomas and squamous cell carcinomas. Irrespective of primary tumor histology, single aspirates of iliac bone marrow from 18 of 82 (21.9%) lung cancer patients exhibited between 1 and 531 CK18+ cells/4 x 10(5) nucleated marrow cells. The specificity of our assay is underlined by the small rate of "false-positive" cells being observed in only 2 of 117 (1.7%) marrow samples from control patients with no evidence for an epithelial malignancy at the time of aspiration. Comparison with established risk factors demonstrated positive correlations (P < 0.05) between the size and histological grade of the primary carcinoma and cytokeratin positivity in iliac bone marrow. In contrast, the association with the metastatic involvement of regional lymph nodes was only weak (P = 0.09). Following a median observation period of 13 months, patients who displayed cytokeratin-positive cells in iliac bone marrow at the time of primary surgery relapsed more frequently as compared to patients with a negative marrow finding (66.7 versus 36.6%; P < 0.05). This difference was even more pronounced by comparing the rates of manifest skeleton metastasis observed in both groups (26.7 versus 2.4%; P < 0.005). Finally, colabeling of CK18+ cells in marrow with monoclonal antibodies to proliferation-associated markers, such as the nucleolar antigen p120 or the tyrosine kinase receptor erbB2, exemplified the oncogenic capacity of CK18+ micrometastatic cells. In conclusion, CK18+ cells present in the bone marrow of patients with apparently operable non-small cell lung cancer exhibit the potential to form solid metastases. Therefore, the approach presented here may be used to determine the risk of early relapse in operable non-small cell lung cancer with potential consequences for adjuvant therapy.

Adult↗
PubMed1993

Overexpression of mitogen-activated protein kinase (ERK1) enhances T-cell cytokine gene expression: role of AP1, NF-AT, and NF-KB.

Transfected Jurkat cells overexpressing extracellular signal-regulated kinase (ERK1), also referred to as mitogen-activated protein (MAP) kinase, were selected by Western blotting assay using anti-ERK1 and antiphosphotyrosine antibodies in combination with a functional MAP kinase assay. We then asked whether enhanced ERK1 expression had any effect on induction of T-cell cytokine genes. The results show that overexpression of ERK1 enhances expression of T-cell interleukin-2 (IL-2), IL-3, and granulocyte-macrophage colony-stimulating factor mRNA; no change was seen in expression of the alpha-actin gene. DNA-binding activities of the transcription factors AP1, NF-AT, and NF-kB were specifically increased twofold to fourfold in ERK1-overexpressing clones relative to nontransformed or vector-transformed cells, whereas no enhancement of CK1-CK2 protein DNA binding activity was detected after ERK1 overexpression. Additionally, increased NF-AT DNA binding activity was associated with functional enhancement of NF-AT transactivating activity in ERK1-overexpressing cells. These results provide direct evidence for the role of MAP kinase in the regulation of cytokine gene expression and indicate that such regulation is likely mediated through the enhanced DNA binding activity of specific nuclear transcription factors.

Base Sequence↗
PubMed1996

Disseminated epithelial tumor cells in bone marrow of patients with esophageal cancer: detection and prognostic significance.

Minimal residual disease in patients with operable esophageal cancer is frequently missed by current noninvasive tumor staging. Here we applied an immunocytochemical cytokeratin assay that allows identification of individual esophageal carcinoma cells disseminated to bone marrow. Prior to therapy, bone marrow was aspirated from the upper iliac crest of 71 patients with esophageal cancer at various disease stages as well as an age-matched control group of 20 noncarcinoma patients. Tumor cells in cytologic bone marrow preparations were detected with monoclonal antibodies (mAbs) CK2, KL1, and A45-B/B3 to epithelial cytokeratins (CKs) using the alkaline phosphatase antialkaline phosphatase method. CK-positive cells were found in 14 (36.8%) of 38 cancer patients treated with curative intent and 16 (48.5%) of 33 patients with extended disease. The overall frequency of these cells was 1 per 4 x 10(5) to 82 per 4 x 10(5) mononuclear cells with no significant differences between patients at different tumor stages. After a short median follow-up of 9.5 months (3-24 months), 7 of 11 patients who underwent complete surgical resection but had tumor cells in bone marrow presented with tumor relapse compared to 2 of 19 corresponding patients without such cells (p < 0.01). It was concluded that although bone marrow is not a preferential site of overt metastasis of esophageal cancer, the frequent occurrence of isolated tumor cells at this distant site indicates that hematogenous dissemination of viable malignant cells occurs early in tumor progression.

Bone Marrow↗
PubMed1996

[Immunocytochemical detection and prognostic significance of epithelial tumor cells in bone marrow of patients with pancreatic carcinoma].

INTRODUCTION: Minimal residual disease in patients with operable pancreas carcinoma is frequently missed by current non-invasive tumor staging. PURPOSE: We applied an immunocytochemical cytokeratin assay that allows the identification of individual pancreas carcinoma cells disseminated to bone marrow. METHODS: Prior to therapy bone marrow was aspirated from the upper iliac crest of 42 patients with pancreas carcinoma and a control group of 30 non-carcinoma patients. Tumor cells in cytologic bone marrow preparations were detected with monoclonal antibodies (mAbs) CK2, KL1 and A45-B/B3 to epithelial cytokeratins (CK), using the APAAP-method. RESULTS: CK-positive cells were found in 14 (58.3%) of 24 cancer patients treated in curative intent and 10 (55.6%) of 18 patients with extended disease. After a mean follow up of 12.7 (3-32) months, 6 (42.8%) out of 14 patients who underwent complete surgical resection presented with tumor relapse and 5 (35.7%) with distant metastases as compared to none of 10 corresponding patients without such cells (p < 0.04). Moreover, patients with epithelial tumor cells in bone marrow showed also a significantly shorter overall survival than those without tumor cells (p < 0.03). CONCLUSION: Immunocytochemical screening for epithelial tumor cells in bone marrow might contribute to an improved staging and is of prognostic relevance for pancreas carcinoma patients.

Adenocarcinoma↗
PubMed1995

Androgenic regulation of protein kinase CK1 in the prostatic cell.

We examined the androgenic regulation of protein kinase CK1 in rat ventral prostate cytosolic and chromatin fractions. On androgen deprivation, CK1 in both the nuclear and cytoplasmic compartments decreases slowly at a similar rate. Stimulation of regrowth in the prostate does not evoke an early differential modulation in the CK1 because it increased in both the cytosol and chromatin only by 24 h after androgenic stimulus. These changes in CK1 relate to its proposed role in cell regulation at mitosis and differ from those in protein kinase CK2 that demonstrates rapid modulations in the nuclear compartment under similar conditions.

Amino Acid Sequence↗
PubMed1997

Phosphorylation of the oncogenic transcription factor interferon regulatory factor 2 (IRF2) in vitro and in vivo.

IRF2 is a transcription factor, possessing oncogenic potential, responsible for both the repression of growth-inhibiting genes (interferon) and the activation of cell cycle-regulated genes (histone H4). Surprisingly little is known about the post-translational modification of this factor. In this study, we analyze the phosphorylation of IRF2 both in vivo and in vitro. Immunoprecipitation of HA-tagged IRF2 expressed in 32P-phosphate labelled COS-7 cells demonstrates that IRF2 is phosphorylated in vivo. Amino acid sequence analysis reveals that several potential phosphorylation sites exist for a variety of serine/threonine protein kinases, including those of the mitogen activated protein (MAP) kinase family. Using a battery of these protein kinases we show that recombinant IRF2 is a substrate for protein kinase A (PKA), protein kinase C (PKC), and casein kinase II (CK2) in vitro. However, other serine/threonine protein kinases, including the MAP kinases JNK1, p38, and ERK2, do not phosphorylate IRF2. Two-dimensional phosphopeptide mapping of the sites phosphorylated by PKA, PKC, and CKII in vitro demonstrates that these enzymes are capable of phosphorylating IRF2 at multiple distinct sites. Phosphoaminoacid analysis of HA-tagged IRF2 immunoprecipitated from an asynchronous population of proliferating, metabolically phosphate-labelled cells indicates that this protein is phosphorylated exclusively upon serine residues in vivo. These results suggest that the oncogenic protein IRF2 may be regulated via multiple pathways during cellular growth.

Animals↗
PubMed1998

Protein kinase C and casein kinase 2 phosphorylate in vitro proteins of the annexin family from eggs of loach Misgurnus fossilis.

A mixture of proteins of the annexin family was obtained from the cytoplasm of mature eggs of loach Misgurnus fossilis (by reprecipitation with acid phospholipids in the presence of Ca2+). This mixture comprised five proteins with molecular weights of 58, 38, 36, 35, and 31 kD. Polyclonal rabbit antibodies against the major 31-kD protein were obtained. Western blot analysis showed that the obtained antibodies exhibit a high specificity towards the 31-kD protein from eggs and other tissues of loach and zebrafish (Brachydanio rerio). The analysis of cDNA corresponding to the 31-kD protein by screening the zebrafish cDNA library confirmed that this protein belongs to the annexin family. Phosphorylation of the obtained annexins in vitro was studied. It is shown that the 58-kD protein is phosphorylated by casein kinase 2 (CK2), whereas the 38-, 36-, 35-, and 31-kD proteins are phosphorylated by protein kinase C (PKC).

Amino Acid Sequence↗
PubMed1996

Elevated keratin 18 protein expression indicates a favorable prognosis in patients with breast cancer.

This study was performed to determine if keratin 18 (K18) has prognostic significance in breast cancer cell lines and patients with breast carcinoma. Paraffin sections of primary breast carcinoma tumors and human breast carcinoma cell lines were examined for K18 expression by immunohistochemical staining with the monoclonal antibody CK2. K18 protein expression was low in highly metastatic cell lines and, conversely, high in weakly metastatic cell lines, suggesting that it may function as a prognostic indicator. K18 expression was consequently examined in 134 patients with breast cancer. The staining intensity was compared with clinicopathological variables and follow-up data spanning 8 years. A definitive positive staining was observed in 22 (16.4%) women. The mortality rate was 4. 5% in the K18-positive group and 44.6% in the K18-negative group. Multivariate analysis found K18 expression to be an independent and significant predictor for overall survival.

Adult↗