台灣眼鏡蛇多半胱氨酸分泌蛋白質之立體結構分析與其在血管內皮細胞調控發炎反應機制之研究

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研究生：	王玉玲 Wang, Yu-Ling
論文名稱：	台灣眼鏡蛇多半胱氨酸分泌蛋白質之立體結構分析與其在血管內皮細胞調控發炎反應機制之研究 Cobra CRISP structural determination by X-ray and functions as an inflammatory modulator in endothelial cell
指導教授：	吳文桂 Wu, Wen-Guey 裘正健 Chiu, Jeng-Jiann
口試委員:
學位類別：	博士 Doctor
系所名稱：	生命科學暨醫學院 - 生物資訊與結構生物研究所 Institute of Bioinformatics and Structural Biology
論文出版年：	2010
畢業學年度：	99
語文別：	英文
論文頁數：	100
中文關鍵詞：	台灣眼鏡蛇、發炎反應、半胱氨酸分泌蛋白質、結構、血管內皮細胞、沾黏因子
外文關鍵詞：	Naja Atra, inflammation, CRISP, X-ray structure, Endothelial cells, Adhesion molecule
相關次數：	點閱：2 下載：0
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多半胱氨酸分泌蛋白(CRISPs)廣泛地分布於哺乳動物、爬行動物與兩棲動物，並且分布於許多器官，其中包括副睪、唾腺、蛇毒。CRISPs蛋白質結構由N端的致病相關蛋白組1(PR-1 domain)功能區與C端多半胱氨酸分泌蛋白功能區(CRD)組成。我們研究的蛋白質natrin是純化於台灣眼鏡蛇毒液中,其分子量為25KD，一級結構分析比對結果顯示此蛋白屬於CRISPs家族蛋白。我們使用X光繞射方法分析natrin的三級結構並且研究其在血管內皮細胞中如何調控發炎功能的生理角色及機制。
在此論文，使用X光繞射方法鑑定出natrin蛋白質立體結構，其解析度為1.58Å，ntrin 與鋅離子螯合的蛋白質立體結構為2.54Å。Natrin 蛋白質立體結構的C端與BgK毒素的立體結構相似度高，推測具有阻斷離子活性的功能，根據其他期刊的研究也證實具有此功能，然而N端結構為α-β-α三明治摺疊，包含推測之酵素活性區，此酵素由三個特定胺基酸Ser76-His115-Glu96 組成。在生物物理的特性方面，我們使用了tryptophane螢光分析、圓二光偏極光譜與X光繞射方法鑑定出natrin 蛋白質中兩個鋅離子結合的位置，結合能力較強的位置在酵素活性區(Ser76-His115-Glu96) 的附近並且與His 60 中原子Nε2作結合，鋅離子、單體natrin His 60 Nε2、另一個單體natrin之His 115 Nε2 與一個水分子形成四面體的幾何座標，另一個結合能力較弱的結合位置並沒有很清楚正確的位置，但是知道的是此位置的鋅，與促進HS結合到natrin 有關連，尤其是長鏈的HS。
Natrin蛋白質引起人類血管內皮細胞mitogen-activated protein kinases (MAPKs; i.e., extracellular signal-regulated kinase [ERK], c-Jun-NH2-terminal kinase [JNK], and p38 MAPK) 與 nuclear factor-□B (NF-kB)的訊號傳遞與細胞黏著分子((i.e., intercellular adhesion molecule-1 [ICAM-1], vascular adhesion molecule-1 [VCAM-1], and E-selectin)的表現進而促進單核細胞的黏著。預先給予內皮細胞專一的抑制劑，如ERK 使用PD98059, JNK 使用SP600125, p38 MAPK 使用SB203580以及NF-□B 使用lactacystin，可以抑制natrin所引起的細胞黏著分子表現，同樣的結果也發生在細胞預先使用專一的小干擾RNA。使用表面電槳共振儀器(SPR)測量到HS與natrin有很強的結合能力，基於此實驗發現，我們預先使用酵素heparinase切除細胞表面的醣特定硫化區，使阻斷natrin與細胞表面的HS結合，實驗結果顯示當細胞表面的HS被酵素heparinase切除，natrin 所能引起的訊號傳遞與黏著分子表現明顯下降，所以我們推測natrin所能引起的訊號傳遞與黏著分子與細胞表面HS有很大的關聯。我的研究發現提供了一個方向，CRISPs可以經由細胞表面之HS與鋅離子，活化MAPKs與NF-kB訊號傳遞進而增加內皮細胞上黏著分子的表現而調控細胞發炎反應。

The cysteine-rich secretory proteins (CRISPs) are widely distributed in mammals, reptiles and amphibians and have been identified in diverse organisms, including epididymis, salivary glands, and snake venoms. These proteins containing an N-terminal domain which is also name pathogenesis-related proteins of group 1 (PR-1) domain and a C-terminal cysteine-rich domain (CRD). We have purified natrin from Naja atra venom with molecule mass of 25KD and belong to CRISP family. In the present study, we presented the X-ray structure of natrin and investigated the physiological role in modulating the inflammatory function of vascular endothelial cells (ECs) and its underlying mechanisms.
The 3D structures of natrin without and with zinc soaking are also reported at resolution 1.58 and 2.54 Å in, respectively. In addition to the presence of an ion channel-blocking BgK toxin fold (C-terminal), it comprises an α-β-α sandwich fold (N-terminal) with a Ser76-His115-Glu96 enzymatic triad. Biophysical characterization of natrin by using fluorescence, circular-dichroism, and X-ray crystallographic methods further reveals the presence of two Zn2+-binding sites for natrin. The strong Zn2+ binding site is near the putative Ser76-His115-Glu96 catalytic triad and binds to the Nε2 atoms of His60, His115 and a water molecule in tetrahedral coordination geometry. The weak binding site remains to be characterized, but it may modulate HS binding by enhancing its interaction with long chain HS.
Natrin induced activation of mitogen-activated protein kinases (MAPKs; i.e., extracellular signal-regulated kinase [ERK], c-Jun-NH2-terminal kinase [JNK], and p38 MAPK) and nuclear factor-□B (NF-kB) and expression of adhesion molecules (i.e., intercellular adhesion molecule-1 [ICAM-1], vascular adhesion molecule-1 [VCAM-1], and E-selectin) in ECs and hence monocytic cell adhesion. Pre-treatment of ECs with a specific inhibitor for ERK (PD98059), JNK (SP600125), p38 MAPK (SB203580), or NF-kB (lactacystin), or the MAPK-specific small interfering RNAs (siRNAs) inhibited natrin-induced adhesion molecule expression. Surface plasmon resonance results showed that natrin exhibits strong binding activity to heparin. Pre-treating ECs with heparinase, an enzyme that cleaves the sulfation sites of heparan sulfate on the EC surfaces, resulted in reductions in natrin-induced activations of MAPKs and NF-□B and expressions of adhesion molecules in ECs, suggesting that heparan sulfate on the EC surface plays important roles in EC responses to natrin. Our findings provide insights into the role of CRISP functions as an inflammatory modulator via a novel Zn2+- and heparan sulfate- dependent transcriptional regulation of endothelial cell adhesion molecules

Content
Abstract(English)..............................................................................................................1-2
Abstract(Chinese).............................................................................................................3-4
Abbreviations and Acronyms...............................................................................................5
Chapter  1  Crystal structure of CRISP from Naja atra
Introduction.......................................................................................................................7-8
Materials and methods
Preparation and characterization of natrin..................................................................9
Crystallization ........................................................................................................9-10
X-ray data collection and processing ...................................................................10-11
Determination and Refinement of Crystal Structure .............................................11-12
Results and Discussion.................................................................................................13-18
Table...................................................................................................................................19
Figures...........................................................................................................................20-29

Chapter  2  Novel Function of Cysteine-rich Secretory Protein
from Naja Atra Venom: Natrin Induces Adhesion
Molecule Expression in Vascular Endothelial
Cells through Activations of MAPKs and NF-κB

Introduction...................................................................................................................31-33
Materials and methods
Materials....................................................................................................................34
Preparation and characterization of natrin.................................................................34
EC culture.............................................................................................................34-35
Monocytic cell adherence experiment........................................................................35
RNA isolation and quantitative real-time polymerase chain reaction (PCR).........35-36
Western Blot Analysis................................................................................................36
Flow cytometry...........................................................................................................36
Enzyme Linked Immunosorbent Assay (ELISA)........................................................37
Electrophoretic mobility shift assay (EMSA).........................................................37-38
Pharmaceutical inhibitor treatment and siRNA transfection.......................................38
Results .................................................................................................................39-42
Discussion.............................................................................................................43-44
Figures..................................................................................................................45-58




Chapter  3  Heparan Sulfate Influences natrin-Induce
Proinflammatory Response on Surface of
Vascular Endothelial Cells
Introduction..................................................................................................................59-60
Materials and methods
Materials
RNA isolation and quantitative real-time polymerase chain reaction (PCR)............61
Flow cytometry....................................................................................................61-62
Western Blot Analysis..............................................................................................62
Electrophoretic mobility shift assay (EMSA).......................................................62-63
Surface plasmon resonance (SPR) assay...............................................................63
Results .......................................................................................................................64-65
Discussion...................................................................................................................66-67
Figures........................................................................................................................68-74

Chapter  4  Crystal Structure of Natrin Reveals Zinc Binding site
and Zinc Enhance Natrin-Induce Proinflammatory
response in Vascular Endothelial Cells
Introduction......................................................................................................................75
Materials and methods
Surface plasmon resonance (SPR) assay...............................................................76
RNA isolation and quantitative real-time polymerase chain reaction (PCR).......76-77
Flow cytometry.........................................................................................................77
Fluorescence...........................................................................................................77
Crystal structure determination and refinement...................................................... 78
Results........................................................................................................................79-80
Discussion...................................................................................................................81-82
Table.................................................................................................................................83
Figures........................................................................................................................84-89
Reference..................................................................................................................90-100

                                

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