ࡱ> 5@ 2qbjbj22 +xXX*K4448l$D/("******.......$0R3(. ** .**/''' **.' .'\'0(:$-,-* Z,4b$P- ./0/Z-R94x'F94-94- *V't8***..$d' The Effects of Increased L-Arginine Concentrations on Platelet Thrombus Formation over Fibrinogen and Collagen Kimberly Schipke, Biomedical Engineering Mississippi State University Faculty Advisor: Steven A. Jones, Associate Professor, Louisiana Tech University Randa Eshaq, Biomedical Engineering, Louisiana Tech University August 2005 I. Abstract Myocardial infarctions result from thrombus formation within the coronary artery. Platelets are responsible for arterial thrombosis, and they produce and secrete inhibitors that prevent their function in a control mechanism. L-arginine converts to nitric oxide and L-citruline within the platelets when catalyzed by nitric oxide synthase. The role of platelet-synthesized nitric oxide remains unclear; therefore, a need exists for a clinical device for that can assess the amount of platelet activation, aggregation, and adhesion in an individuals blood with increasing amounts of L-arginine. Experiments were performed to determine how the variation of L-arginine concentrations affects platelet adhesion when exposed to collagen and fibrinogen. A previously designed platelet analyzer was used to test adhesion patterns. Platelet-rich plasma with differing L-arginine levels was pumped across fibrinogen-coated and collagen-coated channels at a shear rate of 1500/s. The channels were stained with acridine orange and observed under fluorescent microscopy. Images were processed through a MATLAB program to determine the percentage of platelet adhesion. The results from the experiment show that an increase in L-arginine production of nitric oxide is directly proportional to the decrease in platelet adhesion on fibrinogen-coated channels. The percent adhesion initially decreased on the collagen-coated channels but the increase of L-arginine had little effect in concentrations higher than 1 mL. II. Introduction Almost all myocardial infarctions are associated with the thrombotic occlusion of the coronary artery. (Prentice) Platelets main function is hemostasis, and they are major contributors of arterial thrombosis. They produce and secrete their own inhibitors, the most effective being nitric oxide. Nitric oxide (NO) is produced within the platelets when NO synthase catalyzes the conversion of L-arginine into L-citruline. Due to its small size, NO has a high diffusivity constant; therefore, it can perfuse through the thrombus in a short period of time, making it an effective inhibitor. (Freedman et al.) Initiation of thrombosis occurs when circulating platelets are activated by exposed collagen and fibrinogen, allowing the accumulation of a single layer of platelets that supports thrombin generation and the formation of platelets into aggregates. Under static conditions, collagen is able to activate platelets and cause shape change, aggregation, and secretion without the assistance of cofactors. The p65 platelet receptor for type I collagen appears to be linked to the generation of nitric oxide. (Michelson, p197-198) As for fibrinogen, its interaction of flowing platelets is predominantly instantaneous and irreversible. Usually less than 10% of platelets that become attached to fibrinogen move from the initial contact site by a distance greater than their own diameter. (Michelson, p216) For these reasons, the adhesion patterns of platelets over fibrinogen and collagen with increasing amounts of L-arginine were investigated. The percent adhesion was expected to decrease with increasing amounts of L-arginine due to an increase of nitric oxide production. The role of platelet-synthesized nitric oxide remains unclear; therefore, experiments were performed to examine its function and compare the amount of adhesion between two different substrates. III. Materials and Methods A. Experimental Design A perfusion system was developed to monitor thrombus formation in a simple, well-controlled manner. The model replicated a blood vessel and allowed the analysis of the effects of specific proteins on platelet thrombus formation. The model was composed of double sealed Plexiglas plates that bound microchannels in place to prevent leakage. Teflon nuts of outer diameter 1/16" were inserted into threaded holes of diameter 1/4.28" in the upper plate. Ferrules with an outer diameter of 1/16" were fixed at the bottom of the nuts, and FEP Teflon tubes with the same diameter were inserted into ferrules to provide inlets and outlets for the injection of blood, as shown in Figure 1. A UV-curable sealant was used to hold the tubing, ferrules, and nuts together. To secure the two plates together, screws were inserted surrounding the microchannels to further prevent leaks.   Figure 1.(A) Side view of micro-fluidic system, (B) top view of micro-fluidic system The microchannels were cut out of plastic silicone elastomer sheets (McMaster) and coated with specific proteins that served as a replica of a blood vessel. Each channel had a width of 2mm, a length of 5cm, and a height of 180m. The silicone elastomer sheets were composed of two 110 mm plastic sheets separated by a 200 mm silicone sheet. In order to construct the channels, the top two layers were cut out and removed, leaving a layer of plastic to deposit collagen and fibrinogen. The top sheet of plastic was then removed to expose silicone so that it could act as a sealant between the channels and Plexiglas plates to prevent leakage shown in Figure 2. (A) (B) (C) Figure 2. Side view of microchannels (A) Uncut elastomer sheet (B) Channels cut and removed (C) Layered with substrate and silicone exposed. To ensure that layers were assembled, the fibrinogen and collagen were tested using a quartz crystal microbalance (QCM). The QCM has a piezoelectric quartz crystal in between a pair of electrodes. The frequency shift of the quartz crystal resonator is directly proportional to the added mass on the electrode (Jonnalagadda et al.). Thus, the change in the frequency was used to assess the change in the thickness of each added layer of mass. 20mM Tris Buffer was made by dissolving 1.21g of TRIS buffer (20% by weight) in 500mL of DI water. TRIS buffer is stable at pH 7.5; therefore, the following polyion solutions and proteins were altered to pH 7.5 as well. To make 3mg/mL of Poly-Sodium 4-Styrene-Sulfonate) (PSS), 45mg of PSS were dissolved in 15mL of TRIS buffer. 1.473mL of 100% Poly Ethylene Imine (PEI) were added to 150mL of TRIS buffer to yield a 1mg/mL concentration. In order to obtain a 3mg/mL concentration of Poly Dimethyl-Diallyl-Ammonium chloride (PDDA), 10.5mL of PDDA (20% by weight) were added to 100 mL of DI water. 1.42g of sodium phosphate were dissolved in 100mL of DI water to make 0.1M Phosphate Buffered Saline (PBS). To make 1mg/mL concentration of fibrinogen, 100mg of fibrinogen were dissolved in 100mL of TRIS buffer. 50mL of collagen (100% by weight) were added to an acetic acid solution comprised of 1.1mL of glacial acetic acid (99.5% by weight) added to 98.9 mL of DI water. Acridine Orange (AO), the fluorescent dye, was prepared by dissolving 100mg of AO in 100mL of DI water to attain a concentration of 1mg/mL. 1mM L-Arginine solution was prepared by dissolving 1.742mg of L-Arginine in 10mL of DI water. Layer-by-Layer (LbL) Self-assembly was the technique used to immobilize fibrinogen and collagen onto the microchannels. LbL is a process of layering by alternating oppositely charged polyion solutions onto a substrate. PDDA, a strong polycation, and PSS, a weak polyanion, were used to form a negatively charged layer, in which the positively charged collagen adsorption could occur. The polycation, PEI, and PSS were used to form a positively charged layer to adsorb the negatively charged fibrinogen. In order to coat the channels with fibrinogen, the channels were immersed for 10 minutes, a time optimized for the adsorption of a single layer (1nm in thickness), in PEI and PSS solutions, then rinsed in TRIS buffer and dried with nitrogen gas, alternating six times to allow adsorption of six foundation layers. The positively charged channels were then immersed in fibrinogen for 20 minutes, alternating four times with PEI. Channels were coated with collagen in the same manner by alternating PDDA and PSS to form six bilayers with four terminal bilayers composed of PSS and collagen. The resonator was cleaned in a solution comprised of 50% DI water, 49% alcohol, and 1% potassium hydroxide for two minutes. It was then dried with a steady stream of nitrogen and placed in the QCM to measure the initial frequency. The resonator was immersed in PDDA for 10 minutes, washed in TRIS buffer for 30 seconds, and dried with nitrogen. The resonator was placed on the QCM to measure frequency to ensure the deposit of layers. It was then immersed in PSS for 10 minutes, washed, dried, and measured. The previous steps were repeated to deposit six bilayers of PDDA and PSS. PDDA was replaced with collagen and submerged for 20 minutes, repeating steps to form four bilayers ending in collagen. Using the previous method of layering collagen, six primary bilayers of PEI and PSS were deposited. PSS was replaced with fibrinogen and immersed for 20 minutes, resulting in four bilayers of PEI ending with fibrinogen. Blood was collected from cow #818 at the Louisiana Tech Dairy Farm. Blood was obtained from the same cow to ensure consistent results. The cow was stuck with a 16-gauge needle in the milk vein. Blood was allowed to flow freely for three seconds before being collected in conical tubes. Sodium citrate was added to blood in a 1:9 ratio. The blood and sodium citrate mixture was immediately turned over four times to a homogeneous mixture of the anticoagulant. Blood was centrifuged at 1500 rcf for 15 minutes at 25 C using a Hermle Labnet Z323K. The blood separated and the top layer of platelet-rich plasma (PRP) was extracted. PBS was added to PRP to obtain the original concentration. L-arginine was added to 1mL of PRP in portions of 1 L, 5 L, 10 L, 15 L, and 25 L, leaving a sample of PRP unaltered to be used as a control. B. Testing PRP was pumped via a syringe pump at a shear rate of 1500 s> , corresponding to the shear rate found in arterioles as well as the optimal shear rate of platelet adhesion. The altered PRP was purged through 1/16" FEP Teflon tubing into six parallel microchannels, each of which contained a small area that served as the model blood vessel. This area consisted of a silicone elastomer sheet coated with the structural proteins, fibrinogen and collagen. After 30 seconds of blood flow through each microchannel, the channels were allowed to incubate for 10 minutes, the substrates were washed in PBS for 30 seconds to remove excess platelets and allowed to air dry. The microchannels were then dyed with fluorescent acridine orange (AO) for 20 minutes. Excess acridine orange was then washed off in PBS for 15 seconds and allowed to air dry. The microchannels were then analyzed with a Nikon TS100 Eclipse Epi fluorescence microscope with a FITC B-2A filter. Digital images were taken of platelet adhesion along the middle of the microchannel. An image processing MATLAB program was used to determine the percent adhesion of platelets on each microchannel. The image was sent through a two-dimensional median filter that removed noise present in the images. The program then performed background subtraction and thresholding to eliminate any non-uniform illuminated objects. The RGB image was then converted to grayscale and then to a binary image, where the platelet coverage was determined by the number of on pixels found. C. Statistical Analysis Numerical data were expressed as the mean standard deviation. The statistical analysis was performed using linear regression analysis correlating L-arginine levels with platelet adhesion. Probability values less than 5% were considered to indicate significance (p< 0.05). IV. Results QCM As previously stated, the LbL assembly of collagen and fibrinogen were tested using the QCM to ensure deposition of layers. The initial layers of PDDA and PSS of collagen had a steady decrease in frequency which proved the addition of layers because the change in frequency and the change in thickness are directly proportional. After collagen was added, the frequency increased which suggests that several layers were stripped off. The frequencies from collagen to collagen layer continued to decrease which proved that collagen was successfully assembled as shown in Figure 3. QCM analysis for fibrinogen was also performed to guarantee the deposition of layers. As with collagen, the frequency continued to decrease on the foundation layers of PEI and PSS. Layers were also stripped away once fibrinogen was added, but the frequencies decreased on the fibrinogen to fibrinogen layers. Therefore, the adsorption of layers was successful. The QCM results for fibrinogen are shown in Figure 4.  EMBED Excel.Sheet.8 Figure 3. QCM results for collagen assembly  EMBED Excel.Sheet.8  Figure 4. QCM results for fibrinogen assembly L-arginine Tests Varying concentrations of L-arginine were added to bovine PRP, and platelet adhesion over fibrinogen and collagen were compared at a shear rate of 1500/s. Results of these tests are shown in Figure 5.  Figure 5. Average percent adhesion of fibrinogen and collagen The L-arginine standard was a 1 (M solution (1.742 mg L-arginine in 10 mL H2O). V. DISCUSSION Myocardial infarctions are associated with high platelet reactivity and coagulation within blood vessels. NO production reduces the amount of platelet adhesion, and is produced within the platelets by L-arginine. (Freedman et al.) Therefore, the study of the effects of increased L-arginine levels on platelet adhesion to fibrinogen and collagen was performed to test whether the platelet analyzer was able to differentiate between the two substrates. Tests were performed using L-arginine concentrations varying from 1-25 mL. Pearson s correlation test (p<0.05) was used to determine the statistical significance between L-arginine levels and platelet coverage. The p-value shows a significant decrease in platelet coverage on fibrinogen with an increase in L-arginine concentration. The L-arginine concentrations had an initial effect on platelet coverage over collagen, but subsequent increases in L-arginine concentrations had little to no effect. The results of these experiments show that the percentage of platelet coverage to fibrinogen-coated and collagen-coated surfaces at a shear rate of 1500/s decreases with an increase in L-arginine concentration. VI. CONCLUSION The results show that platelets adhere to fibrinogen at a higher percentage than collagen. The adhesion pattern for fibrinogen shows that with increasing concentrations of L-arginine, less adhesion is seen. The increase of adherence at 1 mL and 25 mL are believed to be caused from the incubation of platelets within the channel, along with the staining of AO to fibrinogen. Adhesion of platelets to collagen initially decreased and leveled off with increasing amounts of L-arginine. These results show that platelet adhesion to collagen reaches a steady state with concentrations of L-arginine higher than 1 mL. VII. FUTURE WORK The main objective of these experiments is to devise an instrument that can measure the critical parameters of platelet function including platelet activation, aggregation, and adhesion. To continue this endeavor, further testing of platelet function over different substrates seems to be the most logical next phase of experimentation. The experiments will be repeated using the previously designed platelet analyzer over fibronectin and von Willebrand factor. Fibronectin and von Willebrand factor are other proteins found within the blood vessel wall that promote platelet activation and adhesion. Once these experiments are performed, the percent adhesion with increasing concentrations of L-arginine can be directly compared between all four substrates. VIII. ACKNOWLEDGEMENTS First and foremost, I would like to thank my parents for being supportive in every aspect of my life. I would also like to thank my siblings for being good role models and motivating me to succeed. I thank the NSF for realizing the funding for research is crucial to our future. I owe many thanks to Dr. Steven A. Jones for allowing me to participate in this prestigious program. This experience has allowed me to apply the knowledge that I have accumulated over the past three years and motivates me to learn more. I would like to thank Erich Stein for helping me use the MATLAB program and Javeed Shaikh Mohammed for showing me how to use all the different machines required to perform my experiments. I would also like to thank the IfM staff for tending to my every need. IX. REFERENCES h l w x bc4o ~JL{ | !jhV|UjŢhV|UjJIhV|UhW hV|OJQJ hB hV|h&hV|5 hBhV|j1(hBhV|UjhGFhV|U hvMhV| hKQhV|h(hV|OJQJh$_ hqL hV| hV|5hV|2     $a$gdV|gdV|q1q) h i j k l x c  dgdV| $da$gdV|$a$gdV|4zno ijw x } ! 7$8$H$^gdV| d`gdV|$d`a$gdV|dgdV| $da$gdV|!!!"'+j/448G;_;s<t<<<>j@k@@ d^gdV| $da$gdV|$d7$8$H$`a$gdV|dgdV| d`gdV|d7$8$H$`gdV| 7$8$H$^gdV|!!""J1K1444466>6H6n6y666666677s<t<<k@l@@@@@@@@@@@@ AAAAB8Bx h>h>j)hthV|UjhZBhV|UjF hZBhV|Uj$hZBhV|UjF hZBhV|U hZBhV|jhZBhV|U hV|5 h$_5 h{hV| h>=hV| h=hV|CJOJQJ^JaJhV| hthV|-@@@ AAABhBvBxDHHHLLLLLMPPPS $da$gdV|dgd> $da$gdV|dgdV|d7$8$H$]^gdV|8B9BcBdBgBhBwBE EHHHJJJJLLLLMPPPSSSSShhhhhiiKjTjbjcjjjjjjqkpֹֹ֧֮֠ڒ֍֙֍֍֙֍ֆxhV|CJOJQJ^JaJ hhV| hV|6U h$_5 h1hV| hHhV| hw6hV|h8hV|OJQJhd\hV|OJQJ hhV|hthV|OJQJhV| hV|5h>hV|5h>h>H* h>h> jmh>h>.SSSShhuivi j jcjdjjjjjqkkkk4lllmm0m dh7$8$H$gdV|gdV| $da$gdV|dgdV|Freedman J, Loscalzo J, Barnard M, Alpert, Keaney J, Michelson A. Nitric Oxide Released from Activated Platelets Inhibits Platelet Recruitment. J. Clin. Invest. 1997; 100:350-356. Jonnalagadda, K. Platelet Adhesion in Microchannels: Effects of Protein Coatings and Glucose Concentrations, 2004. Thesis, Department of Biomedical Engineering, Louisiana Tech University. Michelson, Alan D. Signal Transduction During the Initiation, Extenstion, and Perpetuation of Platelet Plug Formation. Platelets. 2002. p197-198. Michelson, Alan D. Platelet Thrombus Formation in Flowing Blood. Platelets. 2002. p216. Prentice, Colin R.M. Pathogenesis of Thrombosis. Haemostasis. 1990. 20:50-59. X. APPENDICES The following is the MATLAB program that was used to calculate the percent adhesion of platelets within the microchannels. The program was derived by Kanvasri Jonnalagadda. for x=02:1:99 X=num2str(x); //Converts a number to a string fileName=strcat(strcat('DSCN00',X),'.jpg'); //Concatenate strings BW1=imread(fileName); //Read image from graphics file background= imopen(BW1,strel('disk',30)); //Performs morphological operation S=imsubtract(BW1, background); //Subtracts the background of the image [l,m,n]=size(S) //Determines the size of the image W=zeros(l,m,n); r=S(1:l,1:m,1); g=S(1:l,1:m,2); b=S(1:l,1:m,3); //Performs thresholding and segmentation for i=1:l for j=1:m if r(i,j)<55 W(i,j,1)=0; else W(i,j,1)=256; end if g(i,j) < 80 W(i,j,2)=0; else W(i,j,2)=256; end if(b(i,j) < 72 ) W(i,j,3)=0; else W(i,j,3)=256; end end end %figure,imshow(uint8(W)) g=rgb2gray(uint8(W)); //Converts an RGB image to a grayscale image MF=medfilt2(g); //Performs 2-D median filtering by using 3x3 neighborhood %figure,imshow(MF) //Shows the image %pixval T = roicolor(g,76,255); //Select region of interest based on color and converts to a binary image %figure,imshow(T) u=bwarea(T); //Computes the area of objects in binary image z=l*m p=(u/z)*100 PercentArea(x-01)=p end PAGE  PAGE 14 0mDm_mmmmmmmn$n@n\nmnnnnnno%o1o9oVooop pp dh7$8$H$gdV|pppppqqqq q!q"q.q/q0q1q2qh]hgd &`#$gd gdV| dh7$8$H$gdV|pqqqqqq q"q#q)q*q,q-q.q0q1q2q̷³hTh>0JmHnHuh h 0Jjh 0JU hV|hlhV|CJOJQJ^JaJ(hhV|CJOJQJ^JaJmH sH ) 01h:p / =!"#$%1(Dd*e_t  C PA8PERFUSION SYSTEM(side view)bi']bG\E'DPn=']bG\PNG  IHDRK}b\sRGB&IDATx^ݻrF`yܤEГFɤͤj2bu'<Q$`xX$6KG^ @~F  A@ ] @ @"(A"P @@%Ht] @Js K @@ b @ uI(A @ $.  @%9@DPD@% 1 @J$@  A@ ] @ @"(A"P @@%Ht] @Js K @@ b @ uI(A @ $.  @%9@DPD@% 1 @J$@(An;~}-6yMI{!@yjtqۻ]O_\zGݰy#O58i. @&} 5ɍn?~7[op^dDRTU -o^Oۙ-ڬ-55-Wga3FgE @xK勯oׯy۟^]~p[htu__Aveߡ7דS1L_{\.X6*~J CdV%BdϗP?~T6.n^{rbiܵ  @gz.AGucwRU?g/._!.!@% $Vb6Z _Z/yΚիoƩrrt⧤ e, @@~pcq|=fzcywlHu1HxNTߜ9lsq1mjϝ- lޖa>&@`PN_)p=X)}d4χ71g,Çez]wHl!&MuތaX?vؓ  @JbSAe!EY+YǍ֪<$;/)>HgaQy9U=  @@_U!zxUxg"|jn 2"_h\OΖߊUpKi L"*P} Z7W/ӝ_:7 m*]R @_~;*uZF6riCqچ*5J  @;ͯ@{-eG *MHm @FNj?}t3#wU7zv %ȳDm\q^&@@_>^!}.o2}KOqFՖRi ֌*}S- @%_n]<0_._JemnfxE7Gi/7` L{|chcUw7Í;;`YLk3+0; @_UK0Ül@Qߨ,HWݹdK J'*C\M @`x}) W@Qߨ|B:'d(#i>AY (AzJ*'h @@&J ZO+p7?BxiL k>T!rfCsTSe;%H߹Q-?JSA])3oE9T!jkJJ, &*$ HX`わ#کJSO_r} (LKa }v8Jg@ҭ A@CڏQ Ҿ-B=e࣌<61];B #CPdr{[_ "MBN? 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Jonesi3f9&l=^`o(. ^`hH. pLp^p`LhH. @ @ ^@ `hH. ^`hH. L^`LhH. ^`hH. ^`hH. PLP^P`LhH.^`o(. ^`hH. pLp^p`LhH. @ @ ^@ `hH. ^`hH. L^`LhH. ^`hH. ^`hH. PLP^P`LhH.i3f9&l                  =<WGvW qL V iP .nQ/Zp:>=/<>:@FHvMKQdQ[e;&eQgq[rCuV|Y-}NpZB.i=QVlto:KJr1 8hT >0x>/7rSi/$_$4@>>,e>>eeW&W(W6W7[:[;[<BEK@$@@@2l@D@JL@@UnknownGz Times New Roman5Symbol3& z Arial?5 z Courier New"qh$8F 7 ?&7 ?&!24dKK 3QH)?QhThe effects of increased nitric oxide levels on platelet thrombus formation over fibrinogen and collagenKimberlySteven A. Jones  Oh+'0 ,8DX p|   iThe effects of increased nitric oxide levels on platelet thrombus formation over fibrinogen and collagenthe  Kimberlyts imbimb Normal.dot Steven A. Jones19vMicrosoft Word 10.0@Hmp%@H@F@,7 ?՜.+,0\ hp  =Kim Rocks, Inc.&KA iThe effects of increased nitric oxide levels on platelet thrombus formation over fibrinogen and collagen Title  !"#$%&'()*+,-./0123456789:;<>?@ABCDEFGHIJKLMNOPQRSTUVWXYZ[\]^_`abcdefghijklmnopqrstuvwxyz{|}~Root Entry F, Data ={51TableM4WordDocument+xSummaryInformation(DocumentSummaryInformation8CompObjj  FMicrosoft Word Document MSWordDocWord.Document.89q