• Biomedical Science Letters
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• v.6 no.1
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• pp.11-17
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• 2000

SNAP-25 was first investigated as a neuron-specific protein preferentially expressed in CA3 pyramidal neurons of mouse hippocampus. It is a presynaptic plasma membrane protein in the nerve cell and plays an important role in the synaptic vesicle membrane docking and fusion pathway. We have recently isolated SNAP-25 cDNA from a rat brain cDNA library using a probe of Z2 cDNA. It consisted of 2,101 bp and an open reading frame (ORF) was identified between nucleotides (nt) 209 and 827. The AUG codon (nt 209∼211) was surrounded by CTACCATGG, which corresponded to the consensus sequence of ribosomal binding site. The ORF was terminated by TAA (nt 827∼829) to encode a polypeptide of 206 amino acid residues. The 3'-untranslated region contained two extensive stretches of repeated (CA)28 and (CA)19 at positions 925∼980 and 1645∼1682. It is noteworthy that cysteine residues were clustered in the span of amino acid residues 84∼991 : Cys-Gly-Leu-Cys-Val-Cys-Pro-Cys. Rat SNAP-25 showed 88% and 97% identity in nucleotide sequences to that of human and mouse, respectively. Amino acid sequence of rat SNAP-25 showed 100% identity to that of mouse and human SNAP-21.

• Biomedical Science Letters
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• v.4 no.2
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• pp.137-142
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• 1998

We examined mRNAs, isolated from the rat brain, to ascertain if there is any polymorphism for S-100 beta protein gene. As templates for polymerase chain reaction (PCR) the reverse-transcribed cDNA from the rat brain or phage DNAs isolated from the rat brain cDNA libraries were used. Although PCR products turned out to be exactly same as the expected size based on the previously reported mRNA sequence a single base substitution (CAT to CAC) was identified at nucleotide level. This change was considered as polymorphism since it did not cause any change of the primary structure for S-100 beta protein. This result should facilitate the understanding of the overall structure of the gene for S-100 beta protein.

• Journal of Life Science
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• v.13 no.3
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• pp.291-297
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• 2003

A human endogenous retroviral family (HERV-W) has recently been described that is related to multiple sclerosis-associated retrovirus (MSRV) sequences that have been identified in particles recovered from monocyte cultures from patients with multiple sclerosis. Two pol fragments (HWP-FB10 and HWP-FBl2) of HERV-W family were identified and analysed by the PCR approach with cDNA library of human fetal brain. They showed 89 percent nucleotide sequence similarity with that of the HERV-W (accession no. AF009668). Deletion/insertion or point mutation in the coding region of the pol fragments from human fetal brain resulted in amino acid frameshift that induced a mutated protein. Phylogenetic analysis of the HERV-W family from GenBank database indicates that the HWP-FB10 is very closely related to the AC000064 derived from human chromosome 7q21-q22. Further studies on the genetic relationship with neighbouring genes and functional role of these new HERV-W pol sequences are indicated.

• Proceedings of the Korean Society of Sericultural Science Conference
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• 2003.10a
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• pp.13-18
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• 2003

Allatotropin is a 13-residue amidated neuropeptide isolated from pharate adult heads of the tobacco hornworm, Manduca serta and strongly stimulates biosynthesis of juvenile hormones in adults, but not larval, lepidopteran corpora allata. From a Bombyx mori midgut cDNA library, a cDNA that encodes a 130-amino-acid polypeptide containing M. sexta allatotropin sequence was isolated. The B. mori allatotropin cDNA consists of 1196 nucleotides. (omitted)

• Fisheries and Aquatic Sciences
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• v.4 no.1
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• pp.25-31
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• 2001

4-Aminobutyrate aminotransferase plays an essential role in the 4-aminobutyric acid shunt, converting 4-aminobutyrate to succinic semi aldehyde. We isolated and sequenced' a fish cDNA fragment that encodes 4-aminobutyrate aminotransferase. A brain cDNA library from flounder (Paralichthys olivaceus) was constructed using the ZAP- III XR vector and screened for the fish 4-aminobutyrate aminotransferase gene using a probe derived from the conserved sequences of known mammalian 4-aminobutyrate aminotransferases. A partial cDNA for 4-aminobutyrate aminotransferase was cloned and found to be 700 bp in length corresponding to 66 amino acids. Nucleotide sequence of the clone was aligned with NCBI (National Center for Biotechnology Information) DNA sequence data base. The result showed high sequence identity with previously reported mammalian 4-aminobutyrate aminotransferases. The trans­criptional level of flounder 4-aminobutyrate aminotransferase was detected with the presence of mRNA at different flounder tissues by reverse transcription-polymerase chain reaction (RT-PCR). The expression of flounder 4-aminobutyrate aminotransferase was also tested and detected from the flounder tissues of the brain, liver, kidney and pancreas.

• Biomedical Science Letters
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• v.13 no.1
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• pp.1-10
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• 2007

Nebulin, a giant modular protein from muscle, is thought to act as molecular ruler in sarcomere assembly. In skeletal muscle, the C-terminal ${\sim}50 kDa$ region of nebulin extends into the Z-line lattice. The most recent studies implicated highlighting its extensive isoform diversity and exciting reports revealed its expression in cardiac and non-muscle tissues containing brain. Also these novel findings are indicating that nebulin is actually a multifunctional filament system, perhaps playing roles in signal transduction, contractile regulation, and myofibril force generation, as well as other not yet defined functions. However the binding protein of nebulin and function in brain is still unknown. A novel binding partner of nebulin C-terminal region was identified by screening a human brain cDNA library using yeast two-hybrid system. Nebulin C-terminus binding protein 51 (NCBP51) was contained a RING-finger domain and identified a new isoform of RING finger protein 125 (RNF125). The interaction was confirmed using the GST pull-down assay. NCBP51 belongs to a family of the RING finger proteins and its function remains to be identified in brain. The role of nebulin and NCBP51 will be studied by loss-of-function using siRNA technique in brain.

• Korean Journal of Cognitive Science
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• v.1 no.2
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• pp.361-376
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• 1989

Norepoine is N-methylated by the enzyme phenly ethanolamine N-metyltransferase(PNMT)to form epinephrine.this enzyme is larhly restructed to the adrenal medulla where epinephrine in mammalian brain where epinephrine function as a neurotransmitter.It seems clear that central epinephrine is involved in the regulation of cardiovacular function and in several forms of hypertension.However,information about the struture of mammalian epinephrine forming enzyme has been limited until now.But recently we isolate bovine and human PNMT cDNA clone using gtll expression library and sequcde total nucleotide composition.To obtain information about the structrue of the human and rat PNMT proteins and gones and to further define the extent of the evolutionary relationships among the PNMT molecules of these species human and rat genomic DNA clones to PNMT were sequentially isolated and characterized.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.733-735
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• 2003

Ornithine decarboxylase (ODC) is a key enzyme on the regulation of cellular polyamines. ODC antizyme is a protein that represses ODC through accelerating enzymatic degradation by the 26S proteasome. We have isolated two distinct antizyme cDNA clones (AZS and AZL) from a brain cDNA library constructed with flounder (Paralichthys olivaceus). AZS and AZL cDNA clones were encoding 221 and 218 residues long respectively and revealed 57.7% amino acids sequence identity. The presence of two antizymes mRNA were detected in brain, kidney, liver, and embryo.

• 한국생물공학회:학술대회논문집
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• 2003.04a
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• pp.736-738
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• 2003

Ornithine decarboxylase (ODC) is the key enzyme in the synthetic pathway of polyamines. This enzyme is a homodimeric and a pyridoxal 5-phosphate (PLP) dependent enzyme. We have isolated, a cDNA clone encoding ODC from brain cDNA library constructed from flounder (Paralichthys olivaceus). The ODC cDNA contained a complete ORF consisting of 460 amino acids and one stop codon with comparison to nucleotide sequences of the flounder, zebrafish and rat ODC genes, the ODC genes were highly conserved. The transcription of ODC was analyzed with reverse transcription-polymerase chain reaction (RT-PCR) species in brain, kidney, liver, and embryo.

• Biomedical Science Letters
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• v.6 no.3
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• pp.165-170
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• 2000

Vacuolar (H$^{+}$)-ATPase (V-ATPase) is an intracellular protein which consists of multiple subunits. It carries out acidification by pumping protons in the cell. This enzyme has also been found in the synaptic vesicles and may play an important role in the neurotransmission. We cloned cDNA fragments encoding the 16 kDa subunit of V-ATPase from the rat brain by RT-PCR and PCR using total RNA or recombinant phage DNA as templates. They contained the full coding sequences (468 bp) and one nucleotide at 3' region turned out to be different (A to C) when compared to the liver counterpart. However, this polymorphic difference did not cause any significant change in the primary structure of the protein because both GCA and GCC code for alanine. Our study would contribute to the understanding of the function of 16 M)a V-ATPase in the brain and of the mechanisms of neurotransmission.