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At least 649 records · Page 36Linked to original sources
PubMed1995

cDNA sequence identity of a vitamin D-dependent calcium-binding protein in the chick to calbindin D-9K.

1,25-dihydroxy-vitamin D3 [1,25(OH)2D3] is a steroid hormone that modulates the expression of specific proteins by a genomic mechanism of action. Calbindin D-9K is a calcium-binding protein that heretofore has only been found in mammalian tissues and whose gene expression is regulated by 1,25(OH)2D3 in a tissue specific fashion. By combined reverse transcription and polymerase chain reaction, calbindin D-9K gene expression was demonstrated for the first time to be present in several chicken tissues. Subcloning and sequencing of a partial 160 bp-cDNA PCR product revealed that the cDNA corresponds to calbindin D-9K-cDNA. This constitutes the first evidence of calbindin D-9K gene presence and expression in the avian class.

Animals↗
PubMed1996

Adhesive protein cDNA sequence of the mussel Mytilus coruscus and its evolutionary implications.

cDNA encoding the adhesive protein of the mussel Mytilus coruscus (Mcfp1) was isolated. The coding region encoded 848 amino acids (a.a.) comprising the 20-a.a. signal peptide, the 21-a.a. nonrepetitive linker, and the 805-a.a. repetitive domain. Although the first 204 nucleotides and the 3'-untranslated region of Mcfp1 cDNA were homologous to corresponding parts of M. galloprovincialis adhesive protein (Mgfp1) cDNA, the other parts diverged. The representative repeat motif of the repetitive domain, YKPK(I/P)(S/T)YPP(T/S), was similar but slightly different from the repeat motif of Mgfp1. The codon usage patterns for the same amino acids were different in different positions of the decapeptide motif. Almost identical nucleotide sequences encoding the two to 13 repeats appeared several times in the repetitive region, which suggests that the adhesive protein genes of mussels have evolved through the duplication of these repeat units.

Amino Acid Sequence↗
PubMed1995

Full-length cDNA sequence of X-linked G6PD of an Australian marsupial, the wallaroo.

In order to study the mechanism of X Chromosome (Chr) inactivation in marsupials, the cDNA for glucose-6-phosphate dehydrogenase (G6PD) from an Australian marsupial, the wallaroo (Macropus robustus), was cloned. A partial clone containing the 3' half of the cDNA was obtained by screening a liver cDNA library. The majority of the coding region was obtained by polymerase chain reaction of cDNA with primers designed from regions of conservation between human and opossum G6PD. The 5' end was obtained by rapid amplification of cDNA ends. High homology was observed between mammalian species in the coding region. The 5' untranslated region is highly G+C rich, and appears to be part of a CpG island, as is the case in the human and mouse genes. This is the first report of the full sequence of the cDNA for any marsupial X-linked gene.

Amino Acid Sequence↗
PubMed1994

The mouse gene encoding the GM2 activator protein (Gm2a): cDNA sequence, expression, and chromosome mapping.

The GM2 activator protein forms a substrate-complex with GM2 ganglioside, which enables degradation of the ganglioside by beta-hexosaminidase A. Mutations in the human GM2 activator protein gene (GM2A) result in the GM2 gangliosidosis AB variant, a severe neurological disease. We have isolated and sequenced a mouse GM2 activator protein (Gm2a) cDNA with complete protein coding and 3' untranslated regions. Expression of the Gm2a transcript (approximately 2.3 kb) was apparent in all tissues examined and was most abundant in kidney and testis. The Gm2a gene was mapped to a region on mouse chromosome (Chr) 11 that is homologous with a segment of human chromosome 5 containing the orthologous human gene. In addition, a Gm2a-related sequence (Gm2a-rs1) was mapped to mouse Chr 5.

Animals↗
PubMed1996

The cDNA sequence of murine Nkx-2.2.

We isolated and sequenced a 2026-bp murine Nkx-2.2 cDNA clone that contains an open reading frame encoding 273 amino acids (aa). The 273-aa protein includes a homeobox, an NK-2 box and a N-terminal decapeptide found in other Nk family members.

Amino Acid Sequence↗
PubMed1999

cDNA sequencing of guinea pig alpha 2-HS glycoprotein, its expression in various tissues and acute phase expression.

cDNA encoding alpha 2-HS glycoprotein was amplified from guinea pig liver mRNA by reverse-transcription polymerase chain reaction (RT-PCR) and rapid amplification of cDNA ends, cloned and sequenced. By RT-PCR and nested PCR, alpha 2-HS glycoprotein mRNA was detected not only in liver tissue but also in pancreas, stomach, small intestine, colon, spleen, kidney, testis, skeletal muscle, brain, heart and leukocytes, but not in the lung. The alpha 2-HS glycoprotein mRNA levels in the liver were reduced to half at 48 h after subcutaneous injection of turpentine oil.

Acute Disease↗
PubMed1992

Induction of myogenic differentiation by an expression vector encoding the DNA methyltransferase cDNA sequence in the antisense orientation.

To test the hypothesis that DNA methylation controls the state of differentiation of a mammalian cell, we transfected the stable mesenchymal line 10T1/2 with an expression vector encoding sequences from the DNA methyltransferase (DNA MeTase) cDNA in the antisense orientation. 10T1/2 cells transfected with the antisense construct (pZ alpha M), but not with the vector alone, exhibit morphological changes, convert into multinucleated tubular cells, and express the skeletal myosin heavy chain protein. The conversion to myogenic phenotype is a late event and is dependent on the number of replication events that the cell has undergone, suggesting that induction of myogenesis is a multistep process. Demethylation of sequences that are not involved in the myogenic process is detected at early passages, while demethylation and expression of the MyoD gene is a late event. This report establishes for the first time that demethylation is a very early event in commitment to myogenic differentiation, while demethylation and expression of MyoD is a late event. We suggest that other genes serve as the initial targets for demethylation and commitment of mesenchymal cells to myogenesis. The cell lines described in this report can serve as an important system for identifying these genes.

Animals↗
PubMed1994

Cataloging of the genes expressed in human keratinocytes: analysis of 607 randomly isolated cDNA sequences.

The partial nucleotide sequences of 607 cDNAs randomly isolated from a cDNA library of cultured human epidermal keratinocytes were determined by single pass sequencing. Homology search of the sequences to the non-redundant nucleotide databases revealed that 27% of the cDNAs matched registered human-or non-human genes encoding not only keratinocyte specific genes, but also a variety of functional proteins, the expression of which had not been identified in keratinocytes. Non-matching cDNAs covering 49% of the cDNAs were not homologous even to ESTs from other organs, suggesting that these cDNAs include novel genes expressed in the cells. The large scale sequencing of keratinocyte cDNAs provides a useful molecular source for research into biology and diseases of the skin.

Animals↗
PubMed1995

Molecular cloning of two novel rice cDNA sequences encoding putative calcium-dependent protein kinases.

We have isolated, from a cDNA library constructed from rice coleoptiles, two sequences, OSCPK2 and OSCPK11, that encode for putative calcium-dependent protein kinase (CDPK) proteins. OSCPK2 and OSCPK11 cDNAs are related to SPK, another gene encoding a rice CDPK that is specifically expressed in developing seeds [20]. OSCPK2 and OSCPK11-predicted protein sequences are 533 and 542 amino acids (aa) long with a corresponding molecular mass of 59436 and 61079 Da respectively. Within their polypeptide chain, they all contain those conserved features that define a plant CDPK; kinase catalytic sequences are linked to a calmodulin-like regulatory domain through a junction region. The calmodulin-like regulatory domain of the predicted OSCPK2 protein contains 4 EF-hand calcium-binding sites while OSCPK11 has conserved just one canonical EF-hand motif. In addition, OSCPK2- and OSCPK11-predicted proteins contain, at their N-terminal region preceding the catalytic domain, a stretch of 80 or 74 residues highly rich in hydrophilic amino acids. Comparison of the NH2-terminal sequence of all three rice CDPKs so far identified (OSCPK2, OSCPK11 and SPK) indicates the presence of a conserved MGxxC(S/Q)xxT motif that may define a consensus signal for N-myristoylation. OSCPK2 and OSCPK11 proteins are both encoded by a single-copy gene and their polyadenylated transcripts are 2.4 and 3.5 kb long respectively. OSCPK2 and OSCPK11 mRNAs are equally abundant in rice roots and coleoptiles. A 12 h white light treatment of the coleoptiles reduces the amount of OSCPK2 mRNA with only a slight effect on the level of OSCPK11 transcript. With anoxic treatments, OSCPK2 mRNA level declined significantly and promptly while the amount of OSCPK11 transcript remained constant.

Amino Acid Sequence↗
PubMed1998

cDNA sequence and expression of the mouse alpha1(V) collagen gene (Col5a1).

Several overlapping cDNA clones corresponding to the entire coding sequence of the mouse alpha1(V) collagen gene (Col5a1) were isolated. The conceptual amino acid translation indicated a high degree of sequence identity (94%) with the human alpha1(V) chain. All of the important structures previously noted in the human alpha1(V) chain were also conserved in the mouse chain. The alpha1(V) transcripts were easily detected in mouse embryos as early as 11 days post coitum (d.p.c.). The transcripts were widely distributed in non-cartilaginous and cartilaginous tissues. Finally, we calculated the ratio of transcripts of alpha1(V):alpha2(V):alpha1(XI) in the calvaria and tongue of 18 d.p.c. embryos using the competitive reverse transcription-polymerase chain reaction (RT-PCR) technique. The results raised the possibility that there are at least two different kind of types V/XI collagen heterotrimers in mouse embryonic tissues.

Amino Acid Sequence↗
PubMed1999

cDNA sequence and expression of a cold-responsive gene in Citrus unshiu.

A cDNA clone encoding a protein (CuCOR19), the sequence of which is similar to Poncirus COR19, of the dehydrin family was isolated from the epicarp of Citrus unshiu. The molecular mass of the predicted protein was 18,980 daltons. CuCOR19 was highly hydrophilic and contained three repeating elements including Lys-rich motifs. The gene expression in leaves increased by cold stress.

Amino Acid Sequence↗
PubMed1995

cDNA sequences of variant forms of human placenta diamine oxidase.

Genes for two forms of human placenta diamine oxidase (dao) were cloned from a cDNA library and sequenced. One gene, pdao1, is identical in length to human kidney dao but differs from it by two bases in the coding region and differs slightly in the 3'- and 5'-noncoding regions. The second gene, pdao2, is nearly identical to these genes in the coding region, except that it has an extra 57-nucleotide coding segment near the 3' end of this region. This segment corresponds to the contiguous sequence of the 3' end of intron 3 of human kidney dao.pdao2 also differs significantly from pdao1 and human kidney dao in a 13-base sequence in the 5'-noncoding region. It is proposed that pdao1 and human kidney dao are polymorphic forms of the same allele. Whether pdao2 is a polymorph of these two is not certain, because of the significant differences in the coding and noncoding regions. Pdao2 may represent a different allele.

Amine Oxidase (Copper-Containing)↗
PubMed1987

Three cDNA sequences of mouse type I keratins. Cellular localization of the mRNAs in normal and hyperproliferative tissues.

We have constructed cDNA libraries with poly(A)+ RNA from normal mouse footpad epidermis and from a squamous cell carcinoma of mouse back skin. Both libraries were screened for type I keratin clones. We present sequence data of three keratin cDNA clones which selected mRNAs coding for two 52-kDa proteins (clones pke 52 and pkSCC 52) as well as for a 50-kDa protein (clone pkSCC50). According to their carboxyl-terminal sequences, the two 52-kDa keratin proteins belong to a group of keratins with serine-rich subdomains adjacent to the alpha-helix, whereas the short carboxyl-terminus of the 50-kDa protein lacks a distinct substructure. Sequentially the two 52-kDa keratins are more closely related to each other than to any other mouse type I keratin. However, in situ hybridization with specific subclones reveals a distinctly different pattern of expression in mouse epithelia. Clone pkSCC 52 contains sequence information for a 52-kDa keratin present in basal cells of epidermis and other stratified epithelia, whereas the pke 52 cDNA encodes a keratin which is predominantly expressed in suprabasal cells of nonepidermal tissues. In terms of nucleotide sequence identities, it cannot precisely be decided which of the two mouse 52-kDa proteins is the equivalent of the human epidermal 50-kDa keratin protein (Hanukoglu, I., and Fuchs, E. (1982) Cell 31, 243-252). In the case of the bovine keratin VII, however (Jorcano, J.L., Rieger, M., Franz, J.K., Schiller, D.L., Moll, R., and Franke, W.W. (1984) J. Mol. Biol. 179, 257-281) the sequence identity values speak for an equivalence with the mouse ke 52 keratin. Obviously, in situ hybridization experiments would best be suited to unravel the precise interspecies relationship between the four highly similar keratins. The discriminatory efficacy of this technique is further emphasized by the demonstration that the mRNA for a 50-kDa keratin is present not only in hyperproliferative epithelia, but also in normal cells of hair follicles.

Amino Acid Sequence↗
PubMed1992

Arabidopsis thaliana carbonic anhydrase: cDNA sequence and effect of CO2 on mRNA levels.

A full-length cDNA clone encoding carbonic anhydrase was isolated from an Arabidopsis thaliana (Columbia) leaf library. Comparison of the derived amino acid sequence obtained from this clone with those of pea and spinach reveals a considerable degree of identity. The carbonic anhydrase cDNA was used to probe the level of RNA encoding this protein in the leaves of plants grown in elevated CO2 (660 ppm). We have found that under these conditions the steady-state level of carbonic anhydrase mRNA was increased in comparison with control plants grown in normal atmospheric concentrations of CO2 (330 ppm). This raises the intriguing possibility that there exists in higher plants a mechanism for perceiving and responding to changes in environmental CO2 concentrations at the genetic level.

Amino Acid Sequence↗
PubMed2001

Cloning and structural characterization of ECTACC, a new member of the transforming acidic coiled coil (TACC) gene family: cDNA sequence and expression analysis in human microvascular endothelial cells.

Erythropoietin (Epo) transduces mitogenic and chemoattractant signals to human endothelial cells. Identifications of Epo-responsive genes are important for understanding the molecular nature of Epo signaling in endothelial cells. The effects of Epo on differential expression of various genes were examined in human microvascular endothelial cells (HMVEC) by differential display reverse transcriptase polymerase chain reaction (RT-PCR). In the current study we obtained from Epo-treated HMVEC a cDNA fragment with characteristics of the 3' end of mRNA. Using the cDNA fragment, we then selectively isolated a full-length clone by screening an unamplified endothelial cell cDNA library followed by 5' rapid amplification of cDNA ends by polymerase chain reaction (RACE-PCR). The nucleotide sequence of the longest cDNA revealed an open reading frame of 3311 nucleotides that encodes a protein consisting of approximately 906 amino acids with a predicted MW of approximately 100 kDa. The nucleotide sequence of the cDNA is nearly identical to that of transforming acidic coiled coil-containing (TACC2) and anti-zuai-1 (AZU-1) cDNA clones except at the 5'- and 3'-ends. Northern blot analysis showed an increase in endothelial-TACC-related mRNA levels in Epo-treated cells in comparison to that of the control cells. Endothelial-TACC-related mRNA was highly expressed in heart and skeletal muscle tissue. Placenta and brain tissue exhibited low levels of expression of endothelial-TACC-related gene. Southern blot analysis of genomic DNA from somatic cell hybrids showed that endothelial-TACC-related cDNA maps to chromosome 10. Immunofluorescence microscopy and the occurrence of several putative phosphorylation and SH3 binding sites on the deduced protein suggest that endothelial-TACC-related protein may be involved in Epo signaling cascades in endothelial cells.

Amino Acid Sequence↗
PubMed1994

Isolation, cDNA sequences, and biochemical characterization of the major cyclosporin-binding proteins of Toxoplasma gondii.

The activities of the immunosuppressive, antifungal compounds cyclosporin A (CsA), FK-506, and rapamycin are dependent upon high affinity binding proteins collectively termed immunophilins. We report the isolation, biochemical characterization, and amino acid sequences of two major CsA-binding proteins, cyclophilins, from the pathogenic protozoan, Toxoplasma gondii. The 18.5- and 20-kDa molecular mass proteins exhibit peptidylproline cis-trans-isomerase activity, which is inhibitable by 10(-8) M CsA. The amino acid sequences of these two proteins, deduced from cDNA clones, reveal up to 70% amino acid identity to previously isolated cyclophilins. The 18.5-kDa protein appears to be synthesized as a precursor with a 15 amino acid signal peptide. The amino-terminal region of the mature 20-kDa protein has significant homology to the B subunit of the calmodulin-dependent phosphatase, calcineurin. The two T. gondii cyclophilins are products of different genes and appear to have different subcellular distributions.

Amino Acid Isomerases↗
PubMed1994

cDNA sequences encoding human fructose 1,6-bisphosphatase from monocytes, liver and kidney: application of monocytes to molecular analysis of human fructose 1,6-bisphosphatase deficiency.

Fructose 1,6-bisphosphatase deficiency is an autosomal recessive inherited disorder of gluconeogenesis. We could isolate cDNAs encoding human fructose 1,6-bisphosphatase from normal monocytes, liver and kidney, but not from normal lymphocytes. The cDNAs contained an open reading frame coding for 338 amino acids, and their nucleotide sequences in monocytes and liver were identical. G644C645 nucleotides in this sequence were the same as those of cDNA from HL-60 cells, although our result differed from a previous report (M. El-Maghrabi et al. (1993) J. Biol. Chem. 268, 9466-9472) on an alteration to C644G645 nucleotides in human liver cDNA resulting in a change of Gly-214 to Ala-214 in the enzyme. The Gly-214 (GGC) residue was therefore conserved in the enzymes hitherto isolated from humans and other animals. Analysis of monocytes in seven patients with fructose 1,6-bisphosphatase deficiency showed a DNA fragment with apparent normal size in two sisters but no detectable DNA fragment in the other five patients. Monocytes were thus useful as an alternative source for mRNA from human liver for the molecular analysis of fructose 1,6-bisphosphatase deficiency.

Alanine↗
PubMed1986

Primary structure of the beta-subunit of Torpedo californica (Na+ + K+)-ATPase deduced from the cDNA sequence.

DNA complementary to the Torpedo californica electroplax mRNA coding for the beta-subunit of (Na+ + K+)-ATPase has been cloned by screening a cDNA library with an oligodeoxyribonucleotide probe. Nucleotide sequence analysis of the cloned cDNA has revealed that this polypeptide consists of 305 amino acid residues (including the initiating methionine). The transmembrane topology and the potential N-glycosylation sites of this polypeptide are discussed.

Amino Acid Sequence↗