Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P06889 (Mol)
 630,302 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Gene-specific probes (3' ends of cDNAs) were obtained from barley cDNAs encoding two types of glycine-rich proteins: HvGRP2, characterized by a cytokeratin-like and a cysteine-rich domain, and HvGRP3, whose main feature was an RNA-binding domain. Expression of genes Hvgrp2 and Hvgrp3, which are present at one (or two) copies per haploid genome, was ubiquitous and gene Hvgrp3 was under light/darkness modulation. Cold treatment increased Hvgrp2 and Hvgrp3 mRNA levels. Methyl jasmonate (10 microM) switched off the two genes. Expression of Hvgrp2, but not that of Hvgrp3, was induced by ethylene treatment (100 ppm). Fungal pathogens Erysiphe graminis and Rhynchosporium secalis increased the mRNAs levels of the two genes, both in compatible and in incompatible interactions, while bacterial pathogens did not.
Plant Mol Biol 1997 Mar
PMID:Differential expression of pathogen-responsive genes encoding two types of glycine-rich proteins in barley. 910 4

The cytokeratin 18 related molecules of human hepatocellular carcinoma have been previously recognized through a series of biochemical and immunological approaches. It is suggested that these molecules undergo modulation from human hepatocyte cytokeratin 18. To prove whether these molecules are produced by modulation or protein degradation, we checked the cytokeratin profile of human hepatoma cell line PLC/PRF/5 with the methods used before. These results revealed that the PLC cells have the same cytokeratin 18 related molecules as human hepatocellular carcinoma tissue. The gene expression of the cytokeratin 18 in non-tumor liver tissues, hepatocellular carcinoma and PLC/PRF/5 cells were investigated. First, the mRNAs of non-tumor liver tissues, hepatocellular carcinoma tissues and PLC/PRF/5 cells were collected by the acid guanidinium thiocyanate phenol chloroform method. After transcription into cDNA by reverse transcriptase polymerase chain reaction, the cDNAs of each specimen were amplified by PCR and then digested by SmaI and BamHI restriction enzymes. The digested cDNA fragments were electrophoresed in agarose gel and the base pairs were found to be the same in length between neoplastic and non-neoplastic hepatocytes.
Res Commun Mol Pathol Pharmacol 1997 Jun
PMID:The alteration of cytokeratin 18 molecule and its mRNA expression during tumor transformation in hepatoma. 926 84

Experimentally induced models of breast carcinogenesis in the rat are widely used for studying the biology of breast cancer and for developing and evaluating cancer prevention and control strategies. However, very little is known about gene expression changes that are associated with experimentally induced mammary carcinogenesis. This paper reports the identification, by differential display of mRNA and molecular cloning, of seven cDNA fragments of gene transcripts overexpressed in mammary carcinomas induced by 1-methyl-1-nitrosourea. These genes included the rat homologues of human galectin-7 gene, the human/mouse melanoma inhibitory activity/bovine chondrocyte-derived retinoic acid sensitive protein gene, the mouse stearoyl-CoA desaturase-2 gene, and the mouse endo B cytokeratin/human cytokeratin-18 gene. Although each of these genes has been implicated in some aspect of carcinogenesis in other organs, this paper is the first report of their overexpression in chemically induced mammary carcinomas. Two previously uncharacterized gene transcripts were also identified. A comparison of the expression levels of several genes in mammary carcinomas with those in the normal mammary gland tissue of virgin rats, mid-stage pregnant rats, and of day 1 postpartum lactating dams indicated that the overexpression of several genes observed in mammary carcinomas could not be accounted for by either a difference in the mammary epithelial content between mammary carcinoma and normal mammary tissue or by mammary epithelium-specific proliferation associated with pregnancy. Several genes were also overexpressed in rat mammary carcinomas induced by 7,12-dimethylbenz[a]anthracene but not in azoxymethane-induced rat colon adenocarcinomas. The genes identified in this study may therefore represent mammary carcinoma-specific molecular markers that may be helpful in investigations of mammary carcinogenesis and its prevention.
Mol Carcinog 1997 Oct
PMID:Gene expression changes associated with chemically induced rat mammary carcinogenesis. 936 10

By immunoblotting and immunocytochemical techniques, we characterized the cytokeratins previously localized by us in the previtellogenic ovarian follicle of Podarcis sicula. Our results show that these cytokeratins correspond to those expressed in the monolayered epithelia. In fact, the immunoblotting analysis showed that the NCL-5D3 antibody, specific for human low molecular weight cytokeratins expressed in monolayered epithelia, reacted with the cytokeratins extracted both from the ovary and from the monolayered intestinal mucosa of Podarcis sicula. Furthermore, this antibody, in this reptile as in humans, clearly immunolabeled sections of corresponding tissues. The organization of the cytokeratin cytoskeleton in the main steps of the ovarian follicle differentiation was also clarified. The reported observations suggest that in Podarcis sicula, the cytokeratin cytoskeleton is absent in the early oocytes. It first appears in the growing oocytes as a thin cortical layer in concomitance with its becoming visible also in the enlarging follicle cells. In the larger follicles, this cytoskeleton appears well organized in intermediate cells and in particular in fully differentiated pyriform cells. In both these cells a cytokeratin network connects the cytoplasm to the oocyte cortex through intercellular bridges. At the end of the previtellogenic oocyte growth, the intense immunolabeling of the apex in the regressing pyriform cells suggests that the cytokeratin, as other cytoplasmic components, may be transferred from these follicle cells to the oocyte. At the end of the oocyte growth, in the larger vitellogenic oocytes surrounded by a monolayer of follicle cells, the cytokeratin constitutes a heavily immunolabeled cortical layer thicker than in the previous stages.
Mol Reprod Dev 1997 Dec
PMID:Cytokeratin cytoskeleton in the differentiating ovarian follicle of the lizard Podarcis sicula Raf. 936 49

The authors report a recurred neoplasm showing distinctive histologic, immunophenotypic, and ultrastructural features characteristic of biphasic synovial sarcoma with neural differentiation. The features include areas with a growth pattern of densely packed spindle cells in irregularly intersecting, broad fascicles, diffuse vimentin and HBA 71 immunoreactivity, expression of S-100 protein, and other neural markers. Moreover, areas with glandular structures and cellular expression of cytokeratin and epithelial membrane antigen were noted. Additionally, areas of neural-like growth pattern were positive for neuron-specific enolase, HNK-1, and protein gene product 9.5. Furthermore, cytogenetic analysis, two-color interphase fluorescence in situ hybridization, and reverse transcription polymerase chain reaction demonstrated the reciprocal translocation between chromosomes X and 18 associated with the different subtypes of tumor cells. The establishment and characterization of the tumor cell line are detailed. This cell line retains the distinct morphologic and genetic characteristics of the original biphasic synovial sarcoma with neural differentiation.
Diagn Mol Pathol 1998 Feb
PMID:Translocation (X;18) in a biphasic synovial sarcoma with morphologic features of neural differentiation. 991 34

Tumour suppressor genes may have a role in the control of trophoblast cell population expansion as trophoblast invasion occurs. To investigate this hypothesis, the location of tumour suppressor gene and proto-oncogene products were studied at various stages of trophoblast differentiation and invasion. Trophoblast and decidua were obtained from eight women having a therapeutic termination of pregnancy. Immunohistochemistry was used to localize the products of c-myc, c-erB-2, RB, BCL-2, P21, and P53 genes and anti-cytokeratin was used to identify fetal cells amongst the maternal decidual cells. The most differentiated and furthest invading trophoblast cell type, the multinucleated trophoblast, expressed a combination of genes which may indicate a high apoptotic rate. The other fully differentiated trophoblast, the syncytiotrophoblast, expressed BCL-2 suggesting protection from apoptosis. The co-occurrence of proto-oncogenes and the products of tumour suppressor genes in first trimester trophoblast suggests an important role not only in negative regulation of cellular invasion but also in population expansion through the presence of oncogenes and anti-apoptotic proteins.
Mol Hum Reprod 1998 May
PMID:Oncogene and tumour suppressor gene products during trophoblast differentiation in the first trimester. 966 34

We evaluated a method for extracting cytokeratin (CK) from the normal human submandibular gland and analyzed CK distribution by one- and two-dimensional electrophoresis. Four submandibular glands without histological changes under a light microscope were used as specimens. Intermediate filamentous protein was extracted by a prior modified method CK was not adequately extracted in 1-2% sodium dodecyl sulfate -5% 2-mercaptoethanol solution. On the other hand, 11 bands with molecular weights of 40-58 K were obtained after extraction in 9.5 M urea -5% 2-mercaptoethanol solution. Although fragmentation of cytoskeletal protein was observed, there were no differences in bands according to the strength of homogenization. This fragmentation seemed to be due to restriction degradation by protease. Immunoblotting revealed the reaction of this CK extract to 2 pan-CK antibodies, i.e., K8.13, which recognizes type II basic CK, and C-11, which recognizes CK4, CK5, CK6, CK8, CK10, CK13, CK18. Among monospecific antibodies, anti-CK7 (LDS-68), CK8 (M20), CK13 (KS-1A3), CK18 (CY-90), and CK19 (BA17) antibodies showed positive reactions. Glial fibrillary acidic protein, neurofilament (NF) 68 K, NF160 K, or NF200 K showed no reactions. These results of one- and two-dimensional electrophoretic analysis suggest the presence of CK5, CK7, CK8, CK13, CK14, CK15, CK17, CK18, and CK19 in the normal submandibular gland.
Res Commun Mol Pathol Pharmacol 1998 Aug
PMID:Extraction of cytokeratin from the human submandibular gland and its electrophoretic analysis. 982 Dec 8

Drug-primed mice form Mallory bodies in their liver after various types of liver injury such as heat shock, drug refeeding, or ethanol ingestion. However, the mechanisms involved that lead to Mallory body formation after these different treatments are unknown. There may be a common pathway of Mallory body formation that is initiated by these different types of injuries. Recently it was shown that the phosphatase 1/2A inhibitor okadaic acid induced Mallory body formation, suggesting that the mechanism of formation involves hyperphosphorylation or oxidative stress-induced NFkappaB activation. To test this hypothesis we exposed drug-primed mice to okadaic acid and measured phosphorylation of Mallory body proteins immunohistochemically and by immunoblot chemiluminescence using an antibody specific for phosphothreonine. NFkappaB activation was measured by a gel shift retardation assay of nuclear lysates. Beginning 15 min after okadaic acid injection, complex changes were progressively seen in the liver cells focally including aggregation of cytokeratins 8 and 18 in hepatocytes which otherwise failed to stain normally with cytokeratin antibody. The aggregates stained positive with ubiquitin and phosphothreonine antibodies. Immunoblots showed a progressive increase in positive staining of the Mallory body band with the antibody to phosphothreonine. NFkappaB activation was progressive up to 2 h after okadaic acid treatment but was downregulated 7 days later. In summary we show for the first time the effect of okadaic acid on the liver cytokeratins in vivo. We conclude that hyperphosphorylation and NFkappaB activation may play a role in the early phases of Mallory body formation.
Exp Mol Pathol 1998 Oct
PMID:Mechanisms of mallory body formation induced by okadaic acid in drug-primed mice. 982 50

The degradation of rat hepatic intermediate filament (IF) proteins cytokeratin A (CK-A, 55-kDa) and cytokeratin D (CK-D, 48-kDa) by purified rat liver calcium-activated proteases (calpains I and II) was evaluated in vitro. Calpain-mediated IF proteolysis was monitored by SDS-PAGE and Western blotting with antibodies to CK-A and CK-D and compared to microtubule protein actin. Both cytokeratins underwent rapid yet limited proteolysis by calpain I and II. Despite the conserved nature of cytokeratins and limited substrate specificity for calpains, distinct fragmentation patterns were obtained for calpain I) CK-A, 46- and 43-kDa/CK-D, 41-, and 39-kDa; and calpain II) CK-A, 46- and 43-kDa/CK-D 41-kDa. The 46-kDa CK-A fragment was the predominant fragment for both calpains. Two-dimensional electrophoresis (IEF/SDS-PAGE) of CK fragments revealed the presence of classic "staircase" patterns consistent with endogenous proteases. Furthermore, proteolytic fragments showed a 2-D electrophoretic shift to lower pI suggesting that the limited hydrolysis occurred within the N-terminal arginine-rich region of CK, a region believed essential for IF interactions in vivo. Thus, calpains may represent an initial step in the turnover of these stable and long-lived proteins and as such, may be relevant to diseases characterized by abnormal disruption and bundling of IF such as formation of Mallory bodies in alcoholic hepatitis.
Res Commun Mol Pathol Pharmacol 1998 Sep
PMID:Degradation of cytokeratin intermediate filaments by calcium-activated proteases (calpains) in vitro: implications for formation of Mallory bodies. 987 79

Background: A sensitive and specific method for the detection of occult breast cancer cells may prove clinically useful. The purpose of this study was to investi gate cytokeratin-19 (CK-19) and gross cystic disease fluid protein (GCDFP) as potential reverse transcription-polymerase chain reaction (RT-PCR) targets for the detection of breast micrometastases. Through positive selection of breast epithelial cells by immunomagnetic bead separation, two RT-PCR assays were developed. Methods and Results: Positive selection of breast epithelial cells was performed using Ber-EP4 monoclonal antibody bound to magnetic beads. RNA was isolated and RT-PCR performed using CK-19 and GCDFP as targets. Detection sensitivity was five T47D cells spiked into 10 mL of normal blood for either target. In all, 100% (3 9/39) of normal bloods were negative for CK-19, whereas only 87% (34/39) were negative with GCDFP. In 15 patients with metastatic disease including 3 without treatment and 12 on either tamoxifen or chemotherapy, CK-19 was positive in 67% (10/15) of patients and GCDFP yielded positives in 27% (4/15) of patients tested. Conclusions: The detection of CK-19 and GCDFP in bloods from patients with metastatic breast cancer may be beneficial in determining the course of therapy, as well as having potential prognostic and diagnostic applications. Although CK-19 appears to be the more sensitive and specific marker, further investigation with both targets is warranted.
Mol Diagn 1998 Sep
PMID:Detection of Breast Cancer Cells in Blood Using Immunomagnetic Bead Selection and Reverse Transcription-Polymerase Chain Reaction. 1008 72


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