• Bulletin of the Korean Chemical Society
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• 제25권7호
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• pp.1055-1060
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• 2004

A new inhibitor for peptidylprolyl cis-trans isomerase (PPIase) has been isolated from Ganoderma lucidum and purified to homogeneous state by organic solvent extraction. The purified PPIase inhibitor (GPI) is assumed to be a membrane-associated glycoprotein. GPI inhibits specifically the bovine brain PPIase, a cyclophilin, and has no effect on the FKBP activity. The results of our chemical modification study of GPI indicate the presence of Lys residue(s) at or near its binding site. Like CsA-cyclophilin complex, GPI-bovine brain PPIase complex strongly inhibits the calcineurin activity in vitro, suggesting the possible involvement of GPI in immunomodulating pathway by the formation of PPIase-inhibitor-calcineurin complex.

• 한국자원식물학회지
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• 제17권3호
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• pp.239-247
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• 2004

더덕 뿌리에서 유래한 EST cDNA library로부터 cyclophilin 유전자와 높은 상동성을 나타내 는 full clone cDNA를 얻었다. 더덕의 cyclophilin, ClCyP1은 747 bp의 cDNA로 174개의 아미노산을 코딩하는 525 bp의 ORF를 가지고 있다. ClCyP1의 아미노산 서열을 분석한 결과, 기존에 보고된 식물들의 cytosolic cyclophilin들과 높은 상동성을 나타내었으며, 여러 식물의 cytosolic CyP의 공통적인 특징인 7개의 아미노산 잔기(KSGKPLH)를 가지고 있었다. RT-PCR분석 결과, 더덕의 ClCyP1은 식물의 조직 전체에서 발현되며, 저온, 고온, 그리고 염 스트레스에 대해 그 발현량이 증가하였다.

• International Journal of Industrial Entomology and Biomaterials
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• 제23권2호
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• pp.223-229
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• 2011

Cyclophilins are originally identified as cytosolic binding protein of the immunosuppressive drug cyclosporine A. They have an activity of peptidyl prolyl cis/trans-isomerases (PPIase), which may play important roles in protein folding, trafficking, assembly and cell signaling. In this study, we report the cloning and characterization of a Bombyx mori cyclophilin A (bCypA) cDNA. The full-length cDNA of bCypA consist of 947 nucleotides with a polyadenylation signal sequence AATAAA and contain an open reading frame of 498 nucleotides encoding a polypeptide of 166 amino acids. The deduced amino acid sequence of bCypA shares a central peptidyl prolyl cis/trans-isomerase and a cyclosporin-A-binding domain with other cyclophilin sequences. Relative quantification real-time (RT) PCR analysis shows that mRNA transcripts of bCypA are detected in all the investigated tissues and highest expression level in the skin of 3-day-old 5 instar larva. Also, bCypA had PPIase activity on the proline-containing peptides. Accordingly, we suggest that bCypA is a new member of the cyclophilin A (CyPA) family and will be useful for quality control of bioactivity recombinant proteins with proline-containing peptides.

• Bulletin of the Korean Chemical Society
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• 제35권1호
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• pp.83-86
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• 2014

Poly(A) polymerase (PAP) play an essential role for maturation of mRNA by adding the adenylate residues at the 3' end. PAP functions are regulated through protein-protein interaction at its C-terminal region. In this study, cyclophilin A (CypA), a member of the peptidyl-prolyl cis-trans isomerase family, was identified as a partner protein interacting with the C-terminal region PAP. The interaction between PAP and CypA was inhibited by the immunosuppressive drug cyclosporine A. Deletion analysis revealed that the N-terminal 56 residues of CypA are sufficient for the interaction with PAP. Interestingly, we observed that PAP and CypA colocalize in the nucleus during SDF-1-induced chemotaxis, implying that CypA could be involved in the regulation of polyadenylation by PAP in the chemotactic cells.

• The Korean Journal of Physiology and Pharmacology
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• 제17권5호
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• pp.375-383
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• 2013

Hepatocellular carcinoma (HCC) related to hepatitis B virus (HBV) and hepatitis C virus (HCV) infections is thought to account for more than 80% of primary liver cancers. Both HBV and HCV can establish chronic liver inflammatory infections, altering hepatocyte and liver physiology with potential liver disease progression and HCC development. Cyclophilin A (CypA) has been identified as an essential host factor for the HCV replication by physically interacting with the HCV non structural protein NS5A that in turn interacts with RNA-dependent RNA polymerase NS5B. CypA, a cytosolic binding protein of the immunosuppressive drug cyclosporine A, is overexpressed in many cancer types and often associated with malignant transformation. Therefore, CypA can be a good target for molecular cancer therapy. Because of antiviral activity, the CypA inhibitors have been tested for the treatment of chronic hepatitis C. Nonimmunosuppressive Cyp inhibitors such as NIM811, SCY-635, and Alisporivir have attracted more interests for appropriating CypA for antiviral chemotherapeutic target on HCV infection. This review describes CypA inhibitors as a potential HCC treatment tool that is contrived by their obstructing chronic HCV infection and summarizes roles of CypA in cancer development.

• Parasites, Hosts and Diseases
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• 제40권3호
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• pp.131-138
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• 2002

The cyclophilins (Cyps) are family members of proteins that exhibit peptidylprolyl cis-trans isomerase (PPIase, EC 5.2.1.8) activity and bind the immunosuppressive agent cyclosprin A (CsA) in varying degrees. During the process of random sequencing of a cDNA library made from Giardia intestinalis WB strain, the cyclophilin gene (gicypl) was isolated. An open reading frame of gicyp1 gene was 576 nucleotides, which corresponded to a translation product of 176 amino acids (Gicypl). The identity with other Cyps was about 58-71%. The 13 residues that constituted the CsA binding site of human cyclophilin were also detected in the amino acid sequence of Gicypl, including tryptophan residue essential for the drug binding. The single copy of the gicypl gene was detected in the G. intestinalis chromosome by southern hybridization analysis. Recombinant Gicyp 1 protein clearly accelerated the rate of cis ${\rightarrow}$ trans isomerization of the peptide substrate and the catalysis was completely inhibited by the addition of $0.5{\;}{\mu}M$ CsA.

• Journal of Microbiology and Biotechnology
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• 제20권6호
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• pp.974-977
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• 2010

Cyclophilins contain the conserved activity of cis-trans peptidyl-prolyl isomerase, which is implicated in protein folding, and function as molecular chaperones. When the yeast cyclophilin A gene (cpr1) was subcloned into the prokaryotic expression vector pKM260, it was found that the expression of Cpr1 drastically increased the cell viability of E. coli BL21 when under abiotic stress conditions, as in the presence of cadmium, copper, hydrogen peroxide, heat, and SDS. Therefore, this study illustrates the importance of Cpr1 as a molecular chaperone that can improve the cellular stress responses when E. coli cells are exposed to adverse conditions, while also demonstrating its potential to increase the stability of E. coli strains utilized for the production of recombinant proteins.

• 미생물과산업
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• 제33권2호
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• pp.25-26
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• 2007

• 한국동물학회:학술대회논문집
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• 한국동물학회 1998년도 한국생물과학협회 학술발표대회
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• pp.83-83
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• 1998

No Abstract, See Full Text

• International Journal of Oral Biology
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• 제37권4호
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• pp.153-159
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• 2012

The effects of the an immunosuppressive drug cyclosporine A (CsA), on the salivary gland are largely unknown, even though clinical trials for the stimulation of salivation using CsA have been attempted. Cyclophilin A (CypA) is known to be a binding protein for CsA. CypA has cell proliferation and tissue matrix change activities. In our present study, the presence of CypA in the gland and effects of CsA on CypA expression were investigated by immunohistochemistry, immunoblotting and RT-PCR analyses. CypA was immunohistochemically detected in various kinds of ducts in the submandibular glands of Sprague Dawley rats. The CypA mRNA level was highest at postnatal day 1 and gradually decreased in a time-dependent manner up to adulthood. The expression of CypA increased after a 10 day subcutaneous administration of CsA in postnatal day 1 rats. Surgical sections of the chorda-lingual nerve with impaired salivation showed no changes in CypA expression. A cell proliferation assay using PCNA anti-serum showed increased cell division following CsA treatment. These results suggest that CsA and CypA may act on ductal cells to regulate saliva composition rather than salivation levels.