| Project/Area Number |
08457615
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| Research Category |
Grant-in-Aid for Scientific Research (B)
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| Allocation Type | Single-year Grants |
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| Section | 一般 |
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| Research Field |
Biological pharmacy
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| Research Institution | Showa University |
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Principal Investigator |
TOMITA Motowo Showa University, Faculty of Pharmaceutical Sciences, Professor, 薬学部, 教授 (30102370)
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| Project Period (FY) |
1996 – 1998
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| Project Status |
Completed (Fiscal Year 1998)
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| Budget Amount *help |
¥7,900,000 (Direct Cost: ¥7,900,000)
Fiscal Year 1998: ¥1,400,000 (Direct Cost: ¥1,400,000)
Fiscal Year 1997: ¥2,000,000 (Direct Cost: ¥2,000,000)
Fiscal Year 1996: ¥4,500,000 (Direct Cost: ¥4,500,000)
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| Keywords | PHBP / IHRP / Serine Protease / Plasma / Genome Structure / Extracellular Matrix / Inflammation / Cascade Pathway / 血液タンパク質 / アネキシン / ノックアウトマウス / cDNA / ゲノム / 急性期タンパク質 / cDNAクローニング / 遺伝子クローニング |
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| Research Abstract |
We tried to elucidate biological functions of novel human plasma proteins, IHRP and PHBP, discovered by us in 1994 and 1995, respectively.
1. Study on JHRP
(1) Protein structure : human JHRP is a single chain polypeptide of about 900 amino acids. Porcine and mouse IHRP cDNAs were cloned, the amino acid sequence homology was about 70% among all the three species. All IHRPs obtained from the three animal species had a site susceptible to proteases. (2) Genomic structure : human IHRP genome was composed of 24 exons, and homologous to that of the heavy chain of inter-aipha-trypsin inhibitor. (3) Functional analysis : although bovine IHRP has been reported to be a typical acute phase protein, the plasma concentration of humam IHRP did not inrease under inflammation conditions. In mice, IHRP was deposited in the kidney after the induction of inflammation and an annexin was involved in the deposition.
2. Study on PHBP
(1) Protein structure : human and mouse PHBP cDNAs were cloned. The two PHBPs showed a 70% homology in amino acid sequence. (2) Genomic structure : human PHBP genome was composed of 13 exons, and significantly similar to that of the coagulation factor XII.(3)functional analysis : PHBP was a serine protease that specically cleaved the peptide bond at C-terminal side of Arg residue. PHBP is a single chain polypeptide that shows no proteolytic activity under normal conditions, and is activated by the cleavage at a specific position.
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