<?xml version="1.0" encoding="UTF-8"?><xml><records><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Bassam A. Hazae</style></author><author><style face="normal" font="default" size="100%">Yetti Hernaningsih</style></author><author><style face="normal" font="default" size="100%">Puspa Wardhani</style></author><author><style face="normal" font="default" size="100%">Fatima Albadwi</style></author><author><style face="normal" font="default" size="100%">Nastasya Nunki</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Abnormalities in Hemostatic Parameters Related to Hemodialysis in End-stage Kidney Pathology: A Narrative Review</style></title><secondary-title><style face="normal" font="default" size="100%">Pharmacognosy Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Coagulation</style></keyword><keyword><style  face="normal" font="default" size="100%">End-stage Kidney Disease (ESKD)</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemodialysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemostasis</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2024</style></year><pub-dates><date><style  face="normal" font="default" size="100%">October 2024</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">16</style></volume><pages><style face="normal" font="default" size="100%">1223-1230</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;Chronic kidney disease (CKD) is a progressively prevalent global health issue. During the initial phases of the condition, CKD is commonly linked to a tendency for excessive blood clotting. While in the end-stage of disease, patients undergoing hemodialysis have a multitude of hemostatic abnormalities. These include prolonged bleeding time, altered platelet count, prolonged PT and aPTT, elevated FDPs and D-dimer, dysregulated vWF activity, and abnormal thrombin generation. These changes result from a combination of uremic toxicity, endothelial dysfunction, inflammatory states, and the effects of the hemodialysis procedure itself. Understanding these mechanisms is crucial for managing and mitigating the bleeding and thrombotic risks in this patient population. This review aims to systematically investigate the effects of hemodialysis on key hemostasis parameters in CKD patients.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">5</style></issue><work-type><style face="normal" font="default" size="100%">Review Article</style></work-type><section><style face="normal" font="default" size="100%">1223</style></section><auth-address><style face="normal" font="default" size="100%">&lt;p class=&quot;rtejustify&quot;&gt;&lt;strong&gt;Bassam A. Hazae&lt;sup&gt;1&lt;/sup&gt;, Yetti Hernaningsih&lt;sup&gt;2,3,4*&lt;/sup&gt;, Puspa Wardhani&lt;sup&gt;2,3,4,5&lt;/sup&gt;, Fatima Albadwi&lt;sup&gt;6&lt;/sup&gt;, Nastasya Nunki&lt;sup&gt;1,7&lt;/sup&gt;&lt;/strong&gt;&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;1&lt;/sup&gt;Laboratory Medicine Study Interest, Master Program of Basic Medical Science, Faculty of Medicine, Universitas Airlangga, Surabaya, East Java, INDONESIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;²Department of Clinical Pathology, Faculty of Medicine, Universitas Airlangga, Surabaya, East Java, INDONESIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;3&lt;/sup&gt;Dr. Soetomo General Academic Hospital, Surabaya, East Java, INDONESIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;⁴Postgraduate School of Universitas Airlangga, Surabaya, East Java, INDONESIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;5&lt;/sup&gt;Institute of Tropical Disease, Universitas Airlangga, Surabaya, East Java, INDONESIA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;6&lt;/sup&gt;Master student, Biotechnology and Bioengineering, East China University of Science and Technology, Shanghai, CHINA.&lt;/p&gt;

&lt;p class=&quot;rtejustify&quot;&gt;&lt;sup&gt;7&lt;/sup&gt;Department of Medical Laboratory Technology, Faculty of Health, Universitas Nahdlatul Ulama Surabaya, Surabaya, INDONESIA.&lt;/p&gt;
</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sowmyashree Gangaraju</style></author><author><style face="normal" font="default" size="100%">Bhagyalakshmi Manjappa</style></author><author><style face="normal" font="default" size="100%">Girish Kesturu Subbaiah</style></author><author><style face="normal" font="default" size="100%">Kemparaju Kempaiah</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Jackfruit (Artocarpus heterophyllus) seed extract exhibits fibrino(geno)lytic activity</style></title><secondary-title><style face="normal" font="default" size="100%">Pharmacognosy Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Fibrino(geno)lysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemostasis</style></keyword><keyword><style  face="normal" font="default" size="100%">Jackfruit</style></keyword><keyword><style  face="normal" font="default" size="100%">Moraceae</style></keyword><keyword><style  face="normal" font="default" size="100%">Non-hemorrhagic</style></keyword><keyword><style  face="normal" font="default" size="100%">Serine/cysteine protease.</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">09th Mar, 2015</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">171-177</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;strong&gt;Objective:&lt;/strong&gt; The current study assesses the fibrinogen and fibrin clot hydrolyzing activities of aqueous seed extract of Jackfruit (AqSEJ).&lt;strong&gt; Methods:&lt;/strong&gt; The protein banding pattern of AqSEJ (100 &amp;mu;g) was analyzed on SDS-PAGE. The proteolytic activity of AqSEJ was confirmed by spectrophotometer and zymography experiments. Fibrinogen, fibrin and plasma protein hydrolyzing activities of AqSEJ were analyzed on SDS-PAGE under reduced conditions. Plasminogen activation and indirect hemolytic activities was analyzed using spectrophotometer. The non-toxic property of AqSEJ was tested by edema, hemorrhage in experimental mice. &lt;strong&gt;Results: &lt;/strong&gt;AqSEJ exhibited proteolytic activity and the specific activity was found to be 1.04 units/mg/min. Furthermore, AqSEJ non-specifically hydrolyzed A&amp;alpha;, followed by B&amp;beta; and &amp;gamma; chains of human fibrinogen and specifically hydrolyzed &amp;alpha; polymer and &amp;alpha; chain of partially cross linked human fibrin clot without affecting &amp;beta; chain and &amp;gamma;-&amp;gamma; dimer even up to the tested dose of 30 &amp;micro;g for the incubation period of 8 hours. Importantly, AqSEJ did not hydrolyze other plasma proteins and devoid of plasminogen activation property. The proteolytic activity of AqSEJ was completely neutralized by PMSF and IAA, while EDTA, EGTA, 1,10-Phenanthroline did not, suggesting the presence of serine and cysteine family proteases. Moreover, AqSEJ did not cause edema and hemorrhage in experimental mice up to the tested dose of 200 &amp;micro;g and nontoxic to RBC cells. &lt;strong&gt;Conclusion: &lt;/strong&gt;AqSEJ hydrolyzes fibrinogen and fibrin clot and non-toxic in nature. Hence, this work showcases the potential applications of Jack fruit seed proteases in the treatment of thrombotic disorders.&lt;/p&gt;&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;strong&gt;Key words:&lt;/strong&gt; Fibrino(geno)lysis, Hemostasis, Jackfruit, Moraceae, Non-hemorrhagic, Serine/cysteine protease.&lt;/p&gt;</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><work-type><style face="normal" font="default" size="100%">Original Article</style></work-type><section><style face="normal" font="default" size="100%">171</style></section><auth-address><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;strong&gt;Sowmyashree Gangaraju&lt;sup&gt;1&lt;/sup&gt;, Bhagyalakshmi Manjappa&lt;sup&gt;1&lt;/sup&gt;, Girish Kesturu Subbaiah&lt;sup&gt;1&lt;/sup&gt;, Kemparaju Kempaiah&lt;sup&gt;2&lt;/sup&gt;, Rangaiah Shashidhara Murthy&lt;sup&gt;3&lt;/sup&gt;, Jane Hoover Plow&lt;sup&gt;4&lt;/sup&gt;, Sebastin Santhosh Martin&lt;sup&gt;5&lt;/sup&gt;, Manohar Shinde&lt;sup&gt;1&lt;/sup&gt;, and Devaraja Sannaningaiah&lt;sup&gt;1*&lt;/sup&gt;&lt;/strong&gt;&lt;/p&gt;&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;1,*&lt;/sup&gt;Department of Studies and Research in Biochemistry and Centre for Bioscience and Innovation, Tumkur University, Tumkur- 572103, India&lt;/p&gt;&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;2&lt;/sup&gt;Departments of Studies in Biochemistry, University of Mysore, Manasagangothry, Mysore-570 006, India&lt;/p&gt;&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;3&lt;/sup&gt;Department of Pharmaceutical Sciences, Philadelphia College of Osteopathic Medicine. Atlanta, Georgia, USA&lt;/p&gt;&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;4&lt;/sup&gt;Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Lerner Research Institute, Cleveland, OH&lt;/p&gt;&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;5&lt;/sup&gt;Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE 17177, Stockhlm, Sweden&lt;/p&gt;</style></auth-address></record><record><source-app name="Biblio" version="7.x">Drupal-Biblio</source-app><ref-type>17</ref-type><contributors><authors><author><style face="normal" font="default" size="100%">Sowmyashree Gangaraju</style></author><author><style face="normal" font="default" size="100%">Bhagyalakshmi Manjappa</style></author><author><style face="normal" font="default" size="100%">Girish Kesturu Subbaiah</style></author><author><style face="normal" font="default" size="100%">Kemparaju Kempaiah</style></author><author><style face="normal" font="default" size="100%">Rangaiah Shashidharamurthy</style></author><author><style face="normal" font="default" size="100%">Jane Hoover Plow</style></author><author><style face="normal" font="default" size="100%">Sebastin Santhosh Martin</style></author><author><style face="normal" font="default" size="100%">Manohar Shinde</style></author><author><style face="normal" font="default" size="100%">Devaraja Sannaningaiah</style></author></authors></contributors><titles><title><style face="normal" font="default" size="100%">Jackfruit (Artocarpus heterophyllus) seed extract exhibits fibrino(geno)lytic activity</style></title><secondary-title><style face="normal" font="default" size="100%">Pharmacognosy Journal</style></secondary-title></titles><keywords><keyword><style  face="normal" font="default" size="100%">Fibrino(geno)lysis</style></keyword><keyword><style  face="normal" font="default" size="100%">Hemostasis</style></keyword><keyword><style  face="normal" font="default" size="100%">Jackfruit</style></keyword><keyword><style  face="normal" font="default" size="100%">Moraceae</style></keyword><keyword><style  face="normal" font="default" size="100%">Non-hemorrhagic</style></keyword><keyword><style  face="normal" font="default" size="100%">Serine/cysteine protease.</style></keyword></keywords><dates><year><style  face="normal" font="default" size="100%">2015</style></year><pub-dates><date><style  face="normal" font="default" size="100%">01/2015</style></date></pub-dates></dates><volume><style face="normal" font="default" size="100%">7</style></volume><pages><style face="normal" font="default" size="100%">171-177</style></pages><language><style face="normal" font="default" size="100%">eng</style></language><abstract><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align:justify&quot;&gt;&lt;strong&gt;Objective: &lt;/strong&gt;The current study assesses the fibrinogen and fibrin clot hydrolyzing activities of aqueous seed extract of Jackfruit (AqSEJ). &lt;strong&gt;Methods:&lt;/strong&gt; The protein banding pattern of AqSEJ (100 &amp;mu;g) was analyzed on SDS-PAGE. The proteolytic activity of AqSEJ was confirmed by spectrophotometer and zymography experiments. Fibrinogen, fibrin and plasma protein hydrolyzing activities of AqSEJ were analyzed on SDS-PAGE under reduced conditions. Plasminogen activation and indirect hemolytic activities was analyzed using spectrophotometer. The non-toxic property of AqSEJ was tested by edema, hemorrhage in experimental mice. &lt;strong&gt;Results:&lt;/strong&gt; AqSEJ exhibited proteolytic activity and the specific activity was found to be 1.04 units/mg/min. Furthermore, AqSEJ non-specifically hydrolyzed A&amp;alpha;, followed by B&amp;beta; and &amp;gamma; chains of human fibrinogen and specifically hydrolyzed &amp;alpha; polymer and &amp;alpha; chain of partially cross linked human fibrin clot without affecting &amp;beta; chain and &amp;gamma;-&amp;gamma; dimer even up to the tested dose of 30 &amp;micro;g for the incubation period of 8 hours. Importantly, AqSEJ did not hydrolyze other plasma proteins and devoid of plasminogen activation property. The proteolytic activity of AqSEJ was completely neutralized by PMSF and IAA, while EDTA, EGTA, 1,10-Phenanthroline did not, suggesting the presence of serine and cysteine family proteases. Moreover, AqSEJ did not cause edema and hemorrhage in experimental mice up to the tested dose of 200 &amp;micro;g and non-toxic to RBC cells. &lt;strong&gt;Conclusion:&lt;/strong&gt; AqSEJ hydrolyzes fibrinogen and fibrin clot and non-toxic in nature. Hence, this work showcases the potential applications of Jack fruit seed proteases in the treatment of thrombotic disorders.&lt;/p&gt;
</style></abstract><issue><style face="normal" font="default" size="100%">3</style></issue><work-type><style face="normal" font="default" size="100%">Original Article</style></work-type><section><style face="normal" font="default" size="100%">171</style></section><auth-address><style face="normal" font="default" size="100%">&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;strong&gt;Sowmyashree Gangaraju&lt;sup&gt;1&lt;/sup&gt;, Bhagyalakshmi Manjappa&lt;sup&gt;1&lt;/sup&gt;, Girish Kesturu Subbaiah&lt;sup&gt;1&lt;/sup&gt;, Kemparaju Kempaiah&lt;sup&gt;2&lt;/sup&gt;, Rangaiah Shashidharamurthy&lt;sup&gt;3&lt;/sup&gt;, Jane Hoover Plow&lt;sup&gt;4&lt;/sup&gt;, Sebastin Santhosh Martin&lt;sup&gt;5&lt;/sup&gt;, Manohar Shinde&lt;sup&gt;1&lt;/sup&gt;, and Devaraja Sannaningaiah&lt;sup&gt;1*&lt;/sup&gt; &lt;/strong&gt;&lt;/p&gt;

&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;1,*&lt;/sup&gt;Department of Studies and Research in Biochemistry and Centre for Bioscience and Innovation, Tumkur University, Tumkur- 572103, India.&lt;/p&gt;

&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;2&lt;/sup&gt;Department of Studies in Biochemistry, University of Mysore, Manasagangothry, Mysore-570 006, India.&lt;/p&gt;

&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;3&lt;/sup&gt;Department of Pharmaceutical Sciences, Philadelphia College of Osteopathic Medicine. Atlanta, Georgia, USA .&lt;/p&gt;

&lt;p style=&quot;text-align: justify;&quot;&gt;&lt;sup&gt;4&lt;/sup&gt;Joseph J. Jacobs Center for Thrombosis and Vascular Biology, Department of Molecular Cardiology, Cleveland Clinic Lerner Research Institute, Cleveland, OH 5Department of Medical Biochemistry and Biophysics, Karolinska Institute, SE 17177, Stockhlm, Sweden.&lt;/p&gt;
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