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Articoli di riviste sul tema "Heparin"

Autore: Grafiati

Pubblicato: 4 giugno 2021

Ultima modifica: 25 luglio 2025

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1

Zvibel, I., E. Halay, and L. M. Reid. "Heparin and hormonal regulation of mRNA synthesis and abundance of autocrine growth factors: relevance to clonal growth of tumors." Molecular and Cellular Biology 11, no. 1 (1991): 108–16. http://dx.doi.org/10.1128/mcb.11.1.108-116.1991.

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Highly sulfated, heparinlike species of heparan sulfate proteoglycans, with heparinlike glycosaminoglycan chains, are extracellular matrix components that are plasma membrane bound in growth-arrested liver cells. Heparins were found to inhibit the growth and lower the clonal growth efficiency of HepG2, a minimally deviant, human hepatoma cell line. Heparan sulfates, closely related glycosaminoglycans present in the extracellular matrix around growing liver cells, had no effect on the growth rate or clonal growth efficiency of HepG2 cells. Neither heparins nor heparan sulfates had any effect on

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2

Zvibel, I., E. Halay, and L. M. Reid. "Heparin and hormonal regulation of mRNA synthesis and abundance of autocrine growth factors: relevance to clonal growth of tumors." Molecular and Cellular Biology 11, no. 1 (1991): 108–16. http://dx.doi.org/10.1128/mcb.11.1.108.

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Highly sulfated, heparinlike species of heparan sulfate proteoglycans, with heparinlike glycosaminoglycan chains, are extracellular matrix components that are plasma membrane bound in growth-arrested liver cells. Heparins were found to inhibit the growth and lower the clonal growth efficiency of HepG2, a minimally deviant, human hepatoma cell line. Heparan sulfates, closely related glycosaminoglycans present in the extracellular matrix around growing liver cells, had no effect on the growth rate or clonal growth efficiency of HepG2 cells. Neither heparins nor heparan sulfates had any effect on

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3

Bar-Ner, M., A. Eldor, L. Wasserman, et al. "Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin species." Blood 70, no. 2 (1987): 551–57. http://dx.doi.org/10.1182/blood.v70.2.551.551.

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Abstract Incubation of human platelets, human neutrophils, or highly metastatic mouse lymphoma cells with sulfate-labeled extracellular matrix (ECM) results in heparanase-mediated release of labeled heparan sulfate cleavage fragments (0.5 less than Kav less than 0.85 on Sepharose 6B). This degradation was inhibited by native heparin both when brought about by intact cells or their released heparanase activity. Degradation of heparan sulfate in ECM may facilitate invasion of normal and malignant cells through basement membranes. The present study tested the heparanase inhibitory effect of nonan

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4

Bar-Ner, M., A. Eldor, L. Wasserman, et al. "Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin species." Blood 70, no. 2 (1987): 551–57. http://dx.doi.org/10.1182/blood.v70.2.551.bloodjournal702551.

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Incubation of human platelets, human neutrophils, or highly metastatic mouse lymphoma cells with sulfate-labeled extracellular matrix (ECM) results in heparanase-mediated release of labeled heparan sulfate cleavage fragments (0.5 less than Kav less than 0.85 on Sepharose 6B). This degradation was inhibited by native heparin both when brought about by intact cells or their released heparanase activity. Degradation of heparan sulfate in ECM may facilitate invasion of normal and malignant cells through basement membranes. The present study tested the heparanase inhibitory effect of nonanticoagula

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5

Fareed, Jawed, Adrian Sonevytsky, Omer Iqbal, Walter P. Jeske, Massimo Iacobelli, and Debra Hoppensteadt. "Inhibition of Heparinase I by Defibrotide with Potential Clinical Implications." Blood 108, no. 11 (2006): 1626. http://dx.doi.org/10.1182/blood.v108.11.1626.1626.

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Abstract Defibrotide represents a poly-deoxyribonucleotide derived antischemic and antithrombotic agent. Currently this agent is used for the management of transplantation associated with vascular complications. Defibrotide is a polyanionic electrolyte capable of releasing endogenous antithrombotic mediators such as (tissue factor pathway inhibitor (TFPI) and heparans. Co-administration of defibrotide with heparin has been shown to produce an augmentation of the effect of heparin and an increase in the biologic half-life. This may be due to the drug interactions or inhibition of endogenous hep

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6

Pinhal, Maria A. S., Isabel A. N. Santos, Irani F. Silva, Carl P. Dietrich, and Helena B. Nader. "Minimum Fragments of the Heparin Molecule Able to Produce the Accumulation and Change of the Sulfation Pattern of an Antithrombotic Heparan Sulfate from Endothelial Cells." Thrombosis and Haemostasis 74, no. 04 (1995): 1169–74. http://dx.doi.org/10.1055/s-0038-1649898.

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SummaryHeparin and low molecular weight heparins stimulate two to three fold the accumulation of an antithrombotic heparan sulfate secreted by endothelial cells in culture. This led us to search for the minimum structural requirements of the heparin molecule able to elicit the enhancement of the heparan sulfate. Fragments were prepared from heparin by degradation with bacterial heparinase and heparitinases. A heparin pentasulfated tetrasaccharide was shown to be the minimum structural sequence able to enhance two to three fold the secretion of heparan sulfate by endothelial cells. The stimulat

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7

Hovingh, P., M. Piepkorn, and A. Linker. "Biological implications of the structural, antithrombin affinity and anticoagulant activity relationships among vertebrate heparins and heparan sulphates." Biochemical Journal 237, no. 2 (1986): 573–81. http://dx.doi.org/10.1042/bj2370573.

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We analysed the distribution, structural characteristics, antithrombin-III-binding properties and anticoagulant activities of heparins and heparan sulphates isolated from the tissues of a wide range of vertebrates. Heparin has a curiously limited distribution, since it was absent from lower aquatic vertebrate species, present in only certain organs such as intestine in many higher vertebrates, and completely absent from the rabbit among mammals examined. The heparins were structurally diverse, and they exhibited a broad range of anticoagulant activities, from approx. 50% to 150% of average com

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8

Sieme, Daniel, Christian Griesinger, and Nasrollah Rezaei-Ghaleh. "Metal Binding to Sodium Heparin Monitored by Quadrupolar NMR." International Journal of Molecular Sciences 23, no. 21 (2022): 13185. http://dx.doi.org/10.3390/ijms232113185.

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Heparins and heparan sulfate polysaccharides are negatively charged glycosaminoglycans and play important roles in cell-to-matrix and cell-to-cell signaling processes. Metal ion binding to heparins alters the conformation of heparins and influences their function. Various experimental techniques have been used to investigate metal ion-heparin interactions, frequently with inconsistent results. Exploiting the quadrupolar 23Na nucleus, we herein develop a 23Na NMR-based competition assay and monitor the binding of divalent Ca2+ and Mg2+ and trivalent Al3+ metal ions to sodium heparin and the con

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9

Diamond, M. S., R. Alon, C. A. Parkos, M. T. Quinn, and T. A. Springer. "Heparin is an adhesive ligand for the leukocyte integrin Mac-1 (CD11b/CD1)." Journal of Cell Biology 130, no. 6 (1995): 1473–82. http://dx.doi.org/10.1083/jcb.130.6.1473.

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Previous studies have demonstrated that the leukocyte integrin Mac-1 adheres to several cell surface and soluble ligands including intercellular adhesion molecule-1, fibrinogen, iC3b, and factor X. However, experiments with Mac-1-expressing transfectants, purified Mac-1, and mAbs to Mac-1 indicate the existence of additional ligands. In this paper, we demonstrate a direct interaction between Mac-1 and heparan sulfate glycans. Heparin affinity resins immunoprecipitate Mac-1, and neutrophils and transfectant cells that express Mac-1 bind to heparin and heparan sulfate, but not to other sulfated

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10

Zhang, Fuming, Lanhong Zheng, Shuihong Cheng, et al. "Comparison of the Interactions of Different Growth Factors and Glycosaminoglycans." Molecules 24, no. 18 (2019): 3360. http://dx.doi.org/10.3390/molecules24183360.

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Most growth factors are naturally occurring proteins, which are signaling molecules implicated in cellular multiple functions such as proliferation, migration and differentiation under patho/physiological conditions by interacting with cell surface receptors and other ligands in the extracellular microenvironment. Many of the growth factors are heparin-binding proteins (HBPs) that have a high affinity for cell surface heparan sulfate proteoglycans (HSPG). In the present study, we report the binding kinetics and affinity of heparin interacting with different growth factors, including fibroblast

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11

Adler, S. "Inhibition of rat glomerular visceral epithelial cell growth by heparin." American Journal of Physiology-Renal Physiology 255, no. 4 (1988): F781—F786. http://dx.doi.org/10.1152/ajprenal.1988.255.4.f781.

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The effect of several glycosaminoglycans and sulfated polysaccharides on the growth of cultured rat glomerular visceral epithelial cells (GEC) was studied in vitro. Heparin, one preparation of heparan sulfate proteoglycan, dextran sulfate, and pentosan polysulfate significantly inhibited the growth of several GEC clones studied (36.0-77.1% inhibition at 100 micrograms/ml). Other glycosaminoglycans studied did not affect GEC growth. Growth inhibition by heparin was dose related and did not appear to reflect cytotoxicity. Heparins with high or low affinity for antithrombin inhibited growth to si

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12

von Hugo, R. "Ist niedermolekulares Heparin plazentagängig?" Hämostaseologie 09, no. 05 (1989): 244–47. http://dx.doi.org/10.1055/s-0038-1655277.

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ZusammenfassungThromboembolische Komplikationen in der Schwangerschaft sind seltene, wegen des Risikos einer Lungenembolie jedoch lebensbedrohliche Krankheitszustände. Auch Langzeitschäden an den Venenklappen, die zu einem postthrombotischen Syndrom führen können, sind zu bedenken. Da in jedem Fall die Antikoagulation als erste therapeutische Maßnahme angezeigt ist, war es naheliegend, Heparin nicht nur wegen seiner akut einsetzenden Wirkung, sondern auch wegen fehlender Plazentagängigkeit einzusetzen. Hier liegt der Unterschied zu den Kumarinderivaten, die beim Fetus neben einer Kumarinembryo

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13

Beurskens, Danielle M. H., Joram P. Huckriede, Roy Schrijver, H. Coenraad Hemker, Chris P. Reutelingsperger, and Gerry A. F. Nicolaes. "The Anticoagulant and Nonanticoagulant Properties of Heparin." Thrombosis and Haemostasis 120, no. 10 (2020): 1371–83. http://dx.doi.org/10.1055/s-0040-1715460.

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AbstractHeparins represent one of the most frequently used pharmacotherapeutics. Discovered around 1926, routine clinical anticoagulant use of heparin was initiated only after the publication of several seminal papers in the early 1970s by the group of Kakkar. It was shown that heparin prevents venous thromboembolism and mortality from pulmonary embolism in patients after surgery. With the subsequent development of low-molecular-weight heparins and synthetic heparin derivatives, a family of related drugs was created that continues to prove its clinical value in thromboprophylaxis and in preven

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14

Banik, Nipa, Seong-Bin Yang, Tae-Bong Kang, Ji-Hong Lim, and Jooho Park. "Heparin and Its Derivatives: Challenges and Advances in Therapeutic Biomolecules." International Journal of Molecular Sciences 22, no. 19 (2021): 10524. http://dx.doi.org/10.3390/ijms221910524.

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Heparin has been extensively studied as a safe medicine and biomolecule over the past few decades. Heparin derivatives, including low-molecular-weight heparins (LMWH) and heparin pentasaccharide, are effective anticoagulants currently used in clinical settings. They have also been studied as functional biomolecules or biomaterials for various therapeutic uses to treat diseases. Heparin, which has a similar molecular structure to heparan sulfate, can be used as a remarkable biomedicine due to its uniquely high safety and biocompatibility. In particular, it has recently drawn attention for use i

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15

Shaughnessy, SG, E. Young, P. Deschamps, and J. Hirsh. "The effects of low molecular weight and standard heparin on calcium loss from fetal rat calvaria." Blood 86, no. 4 (1995): 1368–73. http://dx.doi.org/10.1182/blood.v86.4.1368.bloodjournal8641368.

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Osteoporosis is a well-recognized complication of long-term heparin use. However, the mechanisms by which heparin can influence bone metabolism are unclear. We report here that unfractionated heparin stimulates the process of bone resorption and that the low molecular weight heparins (LMWHs), enoxaparin, fragmin, logiparin, and ardeparin produce significantly less calcium loss than unfractionated heparin. To assess calcium loss from bone, we quantified the release of 45Ca into the culture medium of fetal rat calvaria. 45Ca release was increased in a dose-dependent manner by the addition of eit

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16

Coltrini, D., M. Rusnati, G. Zoppetti, et al. "Different effects of mucosal, bovine lung and chemically modified heparin on selected biological properties of basic fibroblast growth factor." Biochemical Journal 303, no. 2 (1994): 583–90. http://dx.doi.org/10.1042/bj3030583.

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Heparins from bovine mucosa and lung, and chemically modified heparins were assayed for their capacity to: (i) protect human recombinant basic fibroblast growth factor (bFGF) from tryptic cleavage; (ii) prevent 125I-bFGF binding to heparan sulphate proteoglycans present in the extracellular matrix and on the cell surface of fetal bovine aortic endothelial GM 7373 cell cultures; (iii) affect 125I-bFGF binding to high-affinity tyrosine kinase FGF receptors present on the cell membrane of GM 7373 cells; (iv) inhibit the mitogenic activity exerted by bFGF in the same cells. The results demonstrate

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17

Pahl, M. V., N. D. Vaziri, F. Oveisi, J. Wang, and Y. Ding. "Antithrombin III inhibits mesangial cell proliferation." Journal of the American Society of Nephrology 7, no. 10 (1996): 2249–53. http://dx.doi.org/10.1681/asn.v7102249.

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Thrombin stimulates and heparin and heparan sulfate inhibit mesangial cell proliferation. In addition, heparin has been shown to inhibit thrombin-stimulated smooth muscle cell proliferation. The anticoagulant action of heparin is mediated by antithrombin III. This study investigated whether heparin's antiproliferative action is also mediated by antithrombin III. To this end, the effect of antithrombin III on thrombin-stimulated mesangial cell growth was examined. As expected, thrombin stimulated DNA synthesis and cell growth in cultured human mesangial cells. The effect of thrombin on DNA synt

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18

Mycroft-West, Courtney J., Lynsay C. Cooper, Anthony J. Devlin та ін. "A Glycosaminoglycan Extract from Portunus pelagicus Inhibits BACE1, the β Secretase Implicated in Alzheimer’s Disease". Marine Drugs 17, № 5 (2019): 293. http://dx.doi.org/10.3390/md17050293.

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Therapeutic options for Alzheimer’s disease, the most common form of dementia, are currently restricted to palliative treatments. The glycosaminoglycan heparin, widely used as a clinical anticoagulant, has previously been shown to inhibit the Alzheimer’s disease-relevant β-secretase 1 (BACE1). Despite this, the deployment of pharmaceutical heparin for the treatment of Alzheimer’s disease is largely precluded by its potent anticoagulant activity. Furthermore, ongoing concerns regarding the use of mammalian-sourced heparins, primarily due to prion diseases and religious beliefs hinder the deploy

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19

Buddecke, E. "Non-anticoagulant functions of heparin and heparan sulfate." Hämostaseologie 16, no. 01 (1996): 6–14. http://dx.doi.org/10.1055/s-0038-1656632.

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SummaryHeparin is known to bind a large number of proteins not involved in anticoagula-tion, such as growth factors, adhesive proteins of the extracellular matrix, viral coat proteins and other enzymes and proteins. In vivo predominantly heparan sulfate – the most ubiquitous cell surface glycosaminoglycan – takes the functional role of heparin. Structural features, sources and non-anticoagulant func-tions of heparin and heparan sulfate proteoglycan are described. The functional diversity of heparin and heparan sulfate is reviewed in the following sections: (I) heparin and heparan sulfate as pa

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20

Fareed, Jawed, Rakesh Wahi, Indermohan Thethi, et al. "Molecular Mimicry in the Adulteration of Heparins. Chemical Basis for the Development of Oversulfated Chondroitin Sulfate and Related Contaminants." Blood 118, no. 21 (2011): 4322. http://dx.doi.org/10.1182/blood.v118.21.4322.4322.

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Abstract Abstract 4322 The main contaminant in heparin and low molecular weight heparins reported during the heparin crisis (2007–8) was characterized to be oversulfated chondroitin sulfate (OSCS). However, several other sulfated glycosaminoglycans have also been reported to be present. Dermatan sulfate, heparan sulfate and chondroitin sulfate represent heparin byproducts and are invariably present in different proportions in heparin preparations. Hypersulfated derivatives of these are also found as contaminants. The chondroitin sulfate obtained from mammalian tissues and cartilage can be hype

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21

Chao, Yapeng, Shaoxiang Xiong, Xiulan Cheng, and Shijun Qian. "Mass Spectrometric Evidence of Heparin Disaccharides for the Catalytic Characterization of a Novel Endolytic Heparinase." Acta Biochimica et Biophysica Sinica 36, no. 12 (2004): 840–44. http://dx.doi.org/10.1093/abbs/36.12.840.

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Abstract Heparinase from different sources can eliminate heparin or/and heparan sulfate into various low-molecular weight heparins with different characteristics. Porcine intestinal mucosa heparin was degraded into a series of oligosaccharides by a novel heparinase from the species Sphingobacterium. Disaccharide components from the digests were separated and purified by ultrafiltration and HPLC. Five major peaks appeared as three types according to their retention time. The mass spectrometry of peak I mainly gave the non-sulfated disaccharide with the mass of 379 Da. Peak II and III were indic

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22

Yanaka, Kiyoyuki, Stephen R. Spellman, James B. McCarthy, Theodore R. Oegema, Walter C. Low, and Paul J. Camarata. "Reduction of brain injury using heparin to inhibit leukocyte accumulation in a rat model of transient focal cerebral ischemia. I. Protective mechanism." Journal of Neurosurgery 85, no. 6 (1996): 1102–7. http://dx.doi.org/10.3171/jns.1996.85.6.1102.

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✓ Heparin has long been established as an anticoagulant. Although heparin has been demonstrated to reduce brain injury after ischemia and reperfusion, its mechanism of action remains unknown. Recent investigations reveal that it can modulate biological processes such as binding to adhesion receptors on endothelial cells and leukocytes. The authors hypothesized that heparin's protective effect is closely related to its antileukocyte adherence property. They evaluated the efficacy of sulfated polysaccharides (unfractionated heparin, low-molecular-weight heparin, heparan sulfate, chondroitin sulf

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23

Badillo-Samapayo, Jessica, and Jesús Aguilar-Castro. "Trombocitopenia como efecto secundario por la administración de heparinas en los pacientes de COVID-19. Una revisión sistemática." Casos y Revisiones de Salud 4, no. 1 (2022): 72–88. http://dx.doi.org/10.22201/fesz.26831422e.2022.4.1.7.

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Introducción. En la actualidad existen algunas publicaciones que describen alteraciones de la coagulación y complicaciones trombóticas arteriales y venosas principalmente en pacientes ingresados en unidades de cuidados intensivos por COVID-19. Sin embargo, no se ha publicado una revisión sistemática sobre dicha alteración. Objetivo. Presentar una síntesis del conocimiento sobre la frecuencia de la trombocitopenia como efecto secundario por la administración de heparinas en pacientes por COVID-19. Métodos. Se llevó a cabo una búsqueda en las plataformas de PubMed, SCOPUS, Biblioteca Cochrane, L

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Jaques, L. B. "Heparin." Hämostaseologie 05, no. 04 (1985): 154–59. http://dx.doi.org/10.1055/s-0038-1655119.

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ZusammenfassungDie Verteilung des Heparins ist von der Zahl der betroffenen RES-Zellen abhängig, die nach der Art der Heparinanwendung variiert. Intravenöses Heparin (besonders dauerinfundiertes und »Ultra-low dose«-Heparin) ist hauptsächlich auf das kardiovaskuläre Endothel beschränkt. Bei intramuskulärer, subkutaner und intrapulmonaler Applikation wird es auf dem Lymphweg ab transportiert, ist im lokalen Kreislauf mit einer zunehmenden Zahl von RES-Zellen konfrontiert und tritt daher im Venensystem verzögert auf.Inhalation oder Instillation in die Lunge ist eine neue Form der Heparinanwendun

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Kouta, Ahmed, Walter Jeske, Debra Hoppensteadt, Omer Iqbal, Yiming Yao, and Jawed Fareed. "Comparative Pharmacological Profiles of Various Bovine, Ovine, and Porcine Heparins." Clinical and Applied Thrombosis/Hemostasis 25 (January 1, 2019): 107602961988940. http://dx.doi.org/10.1177/1076029619889406.

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Unfractionated heparin is the first anticoagulant drug and has been successfully used clinically for over 80 years. Heparin and its analogues are used during surgery and dialysis and are often used to coat indwelling catheters and other devices where the vascular system is exposed. Most of the heparins used clinically are derived from porcine intestinal mucosa. However, heparins have also been manufactured from tissues of other mammalian species such as cows and sheep. Recently there have been attempts to generate bioengineered heparin in order to overcome contamination and antigenicity proble

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Shi, Deling, Changkai Bu, Peng He, et al. "Structural Characteristics of Heparin Binding to SARS-CoV-2 Spike Protein RBD of Omicron Sub-Lineages BA.2.12.1, BA.4 and BA.5." Viruses 14, no. 12 (2022): 2696. http://dx.doi.org/10.3390/v14122696.

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The now prevalent Omicron variant and its subvariants/sub-lineages have led to a significant increase in COVID-19 cases and raised serious concerns about increased risk of infectivity, immune evasion, and reinfection. Heparan sulfate (HS), located on the surface of host cells, plays an important role as a co-receptor for virus–host cell interaction. The ability of heparin and HS to compete for binding of the SARS-CoV-2 spike (S) protein to cell surface HS illustrates the therapeutic potential of agents targeting protein–glycan interactions. In the current study, phylogenetic tree of variants a

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Scully, M. F., V. Ellis, N. Shah, and V. Kakkar. "Effect of a heparan sulphate with high affinity for antithrombin III upon inactivation of thrombin and coagulation factor Xa." Biochemical Journal 262, no. 2 (1989): 651–58. http://dx.doi.org/10.1042/bj2620651.

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The kinetics of inhibition of human alpha-thrombin and coagulation Factor Xa by antithrombin III were examined under pseudo-first-order reaction conditions as a function of the concentration of heparan sulphate with high affinity for antithrombin III. The maximum observed second-order rate constant was, for the antithrombin III-thrombin reaction, 1.2 x 10(9) M-1.min-1 compared with 2.4 x 10(9) M-1.min-1 in the presence of high-affinity heparin. However, the maximum rate was catalysed by much higher concentrations of heparan sulphate (1.3 microM) than of heparin (0.025 microM). Differences were

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Baig, Nausheen, Ahmed Kouta, Walter Jeske, et al. "Validation of the Bioequivalence of USP Potency Adjusted Porcine, Ovine, and Bovine Heparins." Blood 136, Supplement 1 (2020): 6. http://dx.doi.org/10.1182/blood-2020-142861.

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Introduction: Currently, there is a shortage of porcine heparin due to several factors such as limited availability of porcine mucosa, supply chain issues, and increased usage due to COVID-19. This has warranted the development of heparin from alternate sources such as bovine and ovine mucosa which is abundantly available for this purpose. On a mass basis, commercially available porcine heparins exhibit a similar potency (200 units/mg) to their ovine counterpart (190 units/mg) and a higher potency in contrast to their bovine counterpart (130-150 units/mg). Therefore, at gravimetric levels, the

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Su, Dunhao, Yong Li, Edwin A. Yates, Mark A. Skidmore, Marcelo A. Lima, and David G. Fernig. "Analysis of protein-heparin interactions using a portable SPR instrument." PeerJ Analytical Chemistry 4 (April 8, 2022): e15. http://dx.doi.org/10.7717/peerj-achem.15.

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Optical biosensors such as those based on surface plasmon resonance (SPR) are a key analytical tool for understanding biomolecular interactions and function as well as the quantitative analysis of analytes in a wide variety of settings. The advent of portable SPR instruments enables analyses in the field. A critical step in method development is the passivation and functionalisation of the sensor surface. We describe the assembly of a surface of thiolated oleyl ethylene glycol/biotin oleyl ethylene glycol and its functionalisation with streptavidin and reducing end biotinylated heparin for a p

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Lindsay, Susan L., Rebecca Sherrard Smith, Edwin A. Yates, et al. "Validation of Recombinant Heparan Sulphate Reagents for CNS Repair." Biology 12, no. 3 (2023): 407. http://dx.doi.org/10.3390/biology12030407.

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Therapies that target the multicellular pathology of central nervous system (CNS) disease/injury are urgently required. Modified non-anticoagulant heparins mimic the heparan sulphate (HS) glycan family and have been proposed as therapeutics for CNS repair since they are effective regulators of numerous cellular processes. Our in vitro studies have demonstrated that low-sulphated modified heparan sulphate mimetics (LS-mHeps) drive CNS repair. However, LS-mHeps are derived from pharmaceutical heparin purified from pig intestines, in a supply chain at risk of shortages and contamination. Alternat

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Olson, Guy, Walter Jeske, Omer Iqbal, et al. "Potency Adjusted Blended Heparin of Bovine, Ovine, and Porcine Heparin Exhibit Comparable Biologic Effects to Referenced Single-Sourced Porcine Heparin." Clinical and Applied Thrombosis/Hemostasis 29 (January 2023): 107602962311632. http://dx.doi.org/10.1177/10760296231163251.

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Introduction: Bovine and ovine mucosa represent alternate anticoagulants to porcine mucosa for production of unfractionated heparin (UFH). Standardized heparins from various sources can be blended and potency adjusted, blended heparins exhibit comparable effects as single-sourced porcine UFH. This study evaluated the pharmacologic profile of blended heparin and compared their activities to that of single sourced porcine, ovine, and bovine heparins. Methods: The anticoagulant effects of gravimetric and potency-adjusted heparins were evaluated with aPTT, TT, anti-Xa, anti-IIa, ACT, and TGA studi

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Vairo, Bruno, Leonardo Cinelli, Gustavo Santos, et al. "Heparins from porcine and bovine intestinal mucosa: Are they similar drugs?" Thrombosis and Haemostasis 103, no. 05 (2010): 1005–15. http://dx.doi.org/10.1160/th09-11-0761.

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Abstract (sommario):

SummaryIncreasing reports of bleeding and peri- or post-operative blood dyscrasias in Brazil were possibly associated with the use of heparin from bovine instead of porcine intestine. These two pharmaceutical grade heparins were analysed for potential differences. NMR analyses confirmed that porcine heparin is composed of mainly trisulfated disaccharides →4-α-IdoA2S-1→4-α-GlcNS6S-1→. Heparin from bovine intestine is also composed of highly 2-sulfated α-iduronic acid residues, but the sulfation of the α-glucosamine units vary significantly: ~50% are 6-and N-disulfated, as in porcine heparin, wh

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Greinacher, A., I. Michels, and C. Mueller-Eckhardt. "Heparin-Associated Thrombocytopenia: The Antibody Is Not Heparin Specific." Thrombosis and Haemostasis 67, no. 05 (1992): 545–49. http://dx.doi.org/10.1055/s-0038-1648491.

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Abstract (sommario):

SummaryIn this study the hypothesis was assessed whether heparin-associated thrombocytopenia (HAT) may be caused by an antibody dependent on polysulfated oligosaccharide epitopes, present not only on heparin but also on different polysulfated substances such as dextran sulfate and pentosan polysulfate. We found that the major factor for eliciting platelet activation with sera of HAT type II patients is neither the structure nor the AT III binding capacity of an oligosaccharide, but rather its grade of sulfation. This was shown by in vitro crossreactivity studies with 40 sera of HAT type II pat

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Patton, W. A., C. A. Granzow, L. A. Getts, et al. "Identification of a heparin-binding protein using monoclonal antibodies that block heparin binding to porcine aortic endothelial cells." Biochemical Journal 311, no. 2 (1995): 461–69. http://dx.doi.org/10.1042/bj3110461.

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Abstract (sommario):

The binding of heparin or heparan sulphate to a variety of cell types results in specific changes in cell function. Endothelial cells treated with heparin alter their synthesis of heparan sulphate proteoglycans and extracellular matrix proteins. In order to identify a putative endothelial cell heparin receptor that could be involved in heparin signalling, anti-(endothelial cell) monoclonal antibodies that significantly inhibit heparin binding to endothelial cells were prepared. Four of these antibodies were employed in affinity-chromatographic isolation of a heparin-binding protein from deterg

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35

Hoppensteadt, Debra, Jeanine M. Walenga, Jawed Fareed, and Rodger L. Bick. "Heparin, low–molecular-weight heparins, and heparin pentasaccharide." Hematology/Oncology Clinics of North America 17, no. 1 (2003): 313–41. http://dx.doi.org/10.1016/s0889-8588(02)00091-6.

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36

Weiss, Ryan J., Philipp N. Spahn, Alejandro Gómez Toledo, et al. "ZNF263 is a transcriptional regulator of heparin and heparan sulfate biosynthesis." Proceedings of the National Academy of Sciences 117, no. 17 (2020): 9311–17. http://dx.doi.org/10.1073/pnas.1920880117.

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Abstract (sommario):

Heparin is the most widely prescribed biopharmaceutical in production globally. Its potent anticoagulant activity and safety makes it the drug of choice for preventing deep vein thrombosis and pulmonary embolism. In 2008, adulterated material was introduced into the heparin supply chain, resulting in several hundred deaths and demonstrating the need for alternate sources of heparin. Heparin is a fractionated form of heparan sulfate derived from animal sources, predominantly from connective tissue mast cells in pig mucosa. While the enzymes involved in heparin biosynthesis are identical to thos

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37

Visentin, Gian Paolo. "Heparin-Induced Thrombocytopenia: Molecular Pathogenesis." Thrombosis and Haemostasis 82, no. 08 (1999): 448–56. http://dx.doi.org/10.1055/s-0037-1615865.

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Abstract (sommario):

IntroductionHeparin-induced thrombocytopenia (HIT), a relatively common complication of heparin therapy, is characterized by an unexpected fall in platelet count occurring 5 days or more after the initiation of treatment.1,2 Patients who manifest only the thrombocytopenia rarely experience severe bleeding or other major adverse effects.3 Often, however, the thrombocytopenia is accompanied by arterial and/or venous thrombosis and thromboembolism, a complication which can be devastating.4 HIT, with or without thrombosis, is probably the most common cause of immunologically-mediated, drug-induced

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Sung, Michelle, Jeanine Walenga, Walter Jeske, Omer Iqbal, and Mamdouh Bakhos. "Comparing a New Bovine Source Heparin to the Clinically Used Porcine Heparin for Platelet Function Effects and Heparin-Induced Thrombocytopenia Potential." Blood 132, Supplement 1 (2018): 2540. http://dx.doi.org/10.1182/blood-2018-99-118781.

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Abstract (sommario):

Abstract Background Heparin is a sulfated polysaccharide obtained from intestinal mucosa with anticoagulant properties that is widely used as a standard clinical therapeutic agent to treat and prevent thrombosis. Heparin is known to affect platelet function, and among its side effects is heparin-induced thrombocytopenia (HIT) that can occur in about 1% of patients exposed to heparin. Presently, only porcine source heparin is approved for use in the United States. The aims of this study were to determine if platelet activation by physiological agonists and platelet aggregation induced by HIT an

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39

Walsh, R. L., T. J. Dillon, R. Scicchitano, and G. McLennan. "Heparin and heparan sulphate are inhibitors of human leucocyte elastase." Clinical Science 81, no. 3 (1991): 341–46. http://dx.doi.org/10.1042/cs0810341.

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Abstract (sommario):

1. Heparin and heparan sulphate strongly inhibited human leucocyte elastase activity in an automated assay using the soluble substrate, n-succinyl-(l-alanine)3-p-nitroanilide (50% inhibition of 250 μl of 10 μg of human leucocyte elastase/ml was obtained with 80 μl of 2.8 μg of heparin/ml and 8 μg of heparan sulphate/ml). Less significant inhibition at the same concentrations was seen with the other glycosaminoglycans tested: hyaluronic acid and chondroitin sulphates A–C. 2. Heparin and heparan sulphate also strongly inhibited human leucocyte elastase activity towards insoluble human lung elast

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40

Khiella, Marco, Walter Jeske, Jeanine Walenga, et al. "Bovine Heparin Compared to Porcine Heparin to Demonstrate Bioequivalence." Blood 132, Supplement 1 (2018): 1253. http://dx.doi.org/10.1182/blood-2018-99-118809.

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Abstract (sommario):

Abstract Introduction: Heparin prevents blood clots from forming in patients undergoing heart surgeries, dialysis, multiple other procedures, and for medical treatment of thrombosis such as associated with cancer. Currently, all heparin products in the U.S. are derived from the intestinal mucosa of pigs. Seventy-five percent of the crude porcine heparin used to make the active pharmaceutical ingredient (API) comes from outside the U.S., with a majority originating from China. Reintroduction of bovine heparin into the U.S. market would expand sources for this critical drug, thus addressing conc

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41

Ljungberg, B., and H. Johnsson. "In Vivo Effects of a Low Molecular Weight Heparin Fragment on Platelet Aggregation and Platelet Dependent Hemostasis in Dogs." Thrombosis and Haemostasis 60, no. 02 (1988): 232–35. http://dx.doi.org/10.1055/s-0038-1647036.

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Abstract (sommario):

SummaryPlasma defibrinogenated dogs were used to study the influence of conventional heparin and a low molecular weight heparin fragment (Fragmin®, mean MW 5,000 d) on platelet dependent hemostasis. The heparins were given intravenously in gravimetri- cafly equal doses. The bleeding from standardized skin flap wounds and platelet aggregation (ADP and thrombin) was studied. In comparison, higher doses of the fragment than of heparin were required to increase the bleeding. ADP-induced aggregation in defibrinogenated platelet rich plasma (after addition of normal dog plasma) was potentiated by bo

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42

Walenga, Jeanine, Walter Jeske, Sabrina Bertini, et al. "Bovine Heparin Demonstrates the Same Interaction with HIT Antibodies As Porcine Heparin." Blood 134, Supplement_1 (2019): 2351. http://dx.doi.org/10.1182/blood-2019-127304.

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Abstract (sommario):

Heparin, an anticoagulant widely used in numerous medical applications, is considered an essential medicine by the WHO. Due to its high volume use and that it is the parent material for low molecular weight heparins, there is potential for the raw material to be in short supply. The African swine fever epidemic in China, ongoing since August 2018, has added further restraints on heparin source material supply. At present medical grade heparin in the US is only derived from porcine intestinal mucosa; however, there are explorations into using bovine, ovine, and other sources. Bovine heparin, on

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43

Carlsson, Pernilla, Jenny Presto, Dorothe Spillmann, Ulf Lindahl, and Lena Kjellén. "Heparin/Heparan Sulfate Biosynthesis." Journal of Biological Chemistry 283, no. 29 (2008): 20008–14. http://dx.doi.org/10.1074/jbc.m801652200.

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44

Sandoval, Daniel R., Alejandro Gomez Toledo, Chelsea D. Painter, et al. "Proteomics-based screening of the endothelial heparan sulfate interactome reveals that C-type lectin 14a (CLEC14A) is a heparin-binding protein." Journal of Biological Chemistry 295, no. 9 (2020): 2804–21. http://dx.doi.org/10.1074/jbc.ra119.011639.

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Abstract (sommario):

Animal cells express heparan sulfate proteoglycans that perform many important cellular functions by way of heparan sulfate–protein interactions. The identification of membrane heparan sulfate–binding proteins is challenging because of their low abundance and the need for extensive enrichment. Here, we report a proteomics workflow for the identification and characterization of membrane-anchored and extracellular proteins that bind heparan sulfate. The technique is based on limited proteolysis of live cells in the absence of denaturation and fixation, heparin-affinity chromatography, and high-r

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45

VILAR, Rolando E., Dineshchandra GHAEL, Min LI, et al. "Nitric oxide degradation of heparin and heparan sulphate." Biochemical Journal 324, no. 2 (1997): 473–79. http://dx.doi.org/10.1042/bj3240473.

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Abstract (sommario):

NO is a bioactive free radical produced by NO synthase in various tissues including vascular endothelium. One of the degradation products of NO is HNO2, an agent known to degrade heparin and heparan sulphate. This report documents degradation of heparin by cultured endothelial-cell-derived as well as exogenous NO. An exogenous narrow molecular-mass preparation of heparin was recovered from the medium of cultured endothelial cells using strong-anion exchange. In addition, another narrow molecular-mass preparation of heparin was gassed with exogenous NO under argon. Degradation was evaluated by

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46

Ahmed, Tahir, Jaime Ungo, Min Zhou, and Carlos Campo. "Inhibition of allergic late airway responses by inhaled heparin-derived oligosaccharides." Journal of Applied Physiology 88, no. 5 (2000): 1721–29. http://dx.doi.org/10.1152/jappl.2000.88.5.1721.

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Abstract (sommario):

Inhaled heparin has been shown to inhibit allergic bronchoconstriction in sheep that develop only acute responses to antigen (acute responders) but was ineffective in sheep that develop both acute and late airway responses (LAR) (dual responders). Because the antiallergic activity of heparin is molecular-weight dependent, we hypothesized that heparin-derived oligosaccharides (<2,500) with potential anti-inflammatory activity may attenuate the LAR in the dual-responder sheep. Specific lung resistance was measured in 24 dual-responder sheep before and serially for 8 h after challenge with Asc

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47

Leong, John M., Douglas Robbins, Louis Rosenfeld, Biswajit Lahiri, and Nikhat Parveen. "Structural Requirements for Glycosaminoglycan Recognition by the Lyme Disease Spirochete, Borrelia burgdorferi." Infection and Immunity 66, no. 12 (1998): 6045–48. http://dx.doi.org/10.1128/iai.66.12.6045-6048.1998.

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Abstract (sommario):

ABSTRACT Borrelia burgdorferi, the Lyme disease agent, binds glycosaminoglycans (GAGs) such as heparin, heparan sulfate, and dermatan sulfate. Heparin or heparan sulfate fractions separated by size or charge were tested for their ability to inhibit attachment ofB. burgdorferi to Vero cells. GAG chains of increasing length and/or charge showed increasing inhibitory potency, and detectable heparin inhibition of bacterial binding required a minimum of 16 residues. The ability of a given heparin fraction to inhibit binding to Vero cells was strongly predictive of its ability to inhibit hemagglutin

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48

Sekiguchi, Asuka, Miwako Narita, Toshio Yano, et al. "Enhancing Effects of Heparin/Low Molecular Weight Heparin/Heparan Sulfate on Antigen Presentation and Antigen-Specific Cytotoxic T Lymphocyte (CTL) Induction by Monocyte-Derived Dendritic Cells." Blood 104, no. 11 (2004): 3816. http://dx.doi.org/10.1182/blood.v104.11.3816.3816.

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Abstract (sommario):

Abstract Heparin is bound with heparin-binding sites on certain cells, which induces proliferation and differentiation signals. In addition, heparin is bound with heparin-binding domains of various cytokines, which enhances the interaction between cytokines and target cells. Monocytes have been demonstrated to posses heparin-binding sites on cell surfaces. In the present study, we investigated the effects of heparin (including low molecular weight heparin) and heparan sulfate on antigen presentation and antigen-specific CTL induction of monocyte-derived DCs. Peripheral blood CD14+ cells were c

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49

Kung, Chun, Jagadeesh Gabbeta, Valeri Krougliak, Emmanuel Quiazon, and Mark Triscott. "Liquid Heparin Assay: A Straightforward Approach for Monitoring the Clinical Use of Heparins." Blood 108, no. 11 (2006): 890. http://dx.doi.org/10.1182/blood.v108.11.890.890.

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Abstract (sommario):

Abstract There are number of commercial heparins available in the market. The choice of heparin may depend on the clinical condition of the patient. For example, patients with deep-vein thrombosis (DVT), low molecular weight heparins (LMWH) (such as enoxaparin) may be used; whereas for pulmonary embolism (PE) cases, unfractionated heparins (UFH) may be the heparin of choice. In clinical studies, the synthetic heparin pentasaccharide, Fondaparinux (commercially known as Arixtra) has been shown to be efficacious in the treatment of both types of patients. Monitoring heparin activity in patients

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50

Skaanning, Line K., Angelo Santoro, Thomas Skamris та ін. "The Non-Fibrillating N-Terminal of α-Synuclein Binds and Co-Fibrillates with Heparin". Biomolecules 10, № 8 (2020): 1192. http://dx.doi.org/10.3390/biom10081192.

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Abstract (sommario):

The intrinsically disordered protein α-synuclein (aSN) is, in its fibrillated state, the main component of Lewy bodies—hallmarks of Parkinson’s disease. Additional Lewy body components include glycosaminoglycans, including heparan sulfate proteoglycans. In humans, heparan sulfate has, in an age-dependent manner, shown increased levels of sulfation. Heparin, a highly sulfated glycosaminoglycan, is a relevant mimic for mature heparan sulfate and has been shown to influence aSN fibrillation. Here, we decompose the underlying properties of the interaction between heparin and aSN and the effect of

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