PADGEM

SELP
Available structures
PDB	Ortholog search: PDBe RCSB
List of PDB id codes
	1FSB, 1G1Q, 1G1R, 1G1S, 1HES
Identifiers
Aliases	SELP, CD62, CD62P, GMP140, GRMP, LECAM3, PADGEM, PSEL, selectin P
External IDs	OMIM: 173610 MGI: 98280 HomoloGene: 2260 GeneCards: 6403
Gene ontology
Molecular function	• heparin binding; • oligosaccharide binding; • lipopolysaccharide binding; • glycoprotein binding; • calcium-dependent protein binding; • protein binding; • glycosphingolipid binding; • fucose binding; • carbohydrate binding; • sialic acid binding;
Cellular component	• cytoplasm; • integral component of membrane; • membrane; • plasma membrane; • integral component of plasma membrane; • nucleoplasm; • extracellular space; • platelet alpha granule membrane; • platelet dense granule membrane; • external side of plasma membrane;
Biological process	• leukocyte cell-cell adhesion; • single organismal cell-cell adhesion; • heterophilic cell-cell adhesion via plasma membrane cell adhesion molecules; • response to organic cyclic compound; • positive regulation of leukocyte migration; • platelet degranulation; • blood coagulation; • platelet activation; • regulation of integrin activation; • response to lipopolysaccharide; • regulation of cellular extravasation; • cell adhesion; • defense response to Gram-negative bacterium; • leukocyte tethering or rolling; • positive regulation of phosphatidylinositol 3-kinase signaling; • inflammatory response; • calcium-mediated signaling using intracellular calcium source; • positive regulation of platelet activation; • leukocyte migration; • positive regulation of cell adhesion;
	Sources:Amigo / QuickGO
RNA expression pattern
	More reference expression data
Orthologs
	6403
	20344
	ENSG00000174175
	ENSMUSG00000026580
	P16109
	Q01102
	NM_003005
	NM_011347
	NP_002996.2; NP_002996.2
	NP_035477.1
	Wikidata
View/Edit Human	View/Edit Mouse

関: P-Selectin, CD62P

関: P-Selectin, CD62P

Wikipedia preview

出典(authority):フリー百科事典『ウィキペディア（Wikipedia）』「2016/06/29 01:39:28」(JST)

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[Wiki en表示]

P-selectin is a protein that in humans is encoded by the SELP gene.^[1]

P-selectin functions as a cell adhesion molecule (CAM) on the surfaces of activated endothelial cells, which line the inner surface of blood vessels, and activated platelets. In unactivated endothelial cells, it is stored in granules called Weibel-Palade bodies. In unactivated platelets P-selectin is stored in α-granules.

Other names for P-selectin include CD62P, Granule Membrane Protein 140 (GMP-140), and Platelet Activation-Dependent Granule to External Membrane Protein (PADGEM). It was first identified in endothelial cells in 1989.^[2]

Gene and regulation

P-selectin is located on chromosome 1q21-q24, spans > 50 kb and contains 17 exons in humans.^[3] P-selectin is constitutively expressed in megakaryocytes (the precursor of platelets) and endothelial cells.^[4] P-selectin expression is induced by two distinct mechanisms. First, P-selectin is synthesized by megakaryocytes and endothelial cells, where it is sorted into the membranes of secretory granules.^[5] When megakaryocytes and endothelial cells are activated by agonists such as thrombin, P-selectin is rapidly translocated to the plasma membrane from granules.^[6] Secondly, increased levels of P-selectin mRNA and protein are induced by inflammatory mediators such as tumor necrosis factor-a (TNF-a), LPS, and interleukin-4 (IL-4). Although TNF-a and LPS increase levels of both mRNA and protein in murine models, they do not appear to affect mRNA in human endothelial cells, while IL-4 increases P-selectin transcription in both species.^[7]^[8]^[9] The elevated synthesis of P-selectin may play an important role in the delivery of protein to the cell surface. In ischemic stroke patients, plasma P-selectin concentration was reported to be highly correlated to plasminogen activator inhibitor-1 activity and tissue plasminogen activator activity.^[10]

Structure

P-selectin is found in endothelial cells and platelets where it is stored in Weibel-Palade bodies and α-granules, respectively. In response to inflammatory cytokines such as IL-4 and IL-13, P-selectin is translocated to the plasma membrane in endothelial cells.^[11] The extracellular region of P-selectin is composed of three different domains like other selectin types; a C-type lectin-like domain in the N-terminus, an EGF-like domain and a complement-binding protein-like domains (same as complement regulatory proteins: CRP) having short consensus repeats (~60 amino acids). The number of CRP repeats is the major feature differentiating the type of selectin in extracellular region. In human, P-selectin has nine repeats while E-selectin contains six and L-selectin has only two. P-selectin is anchored in transmembrane region that is followed by a short cytoplasmic tail region.^[12]

Ligand

The primary ligand for P-selectin is P-selectin glycoprotein ligand-1 (PSGL-1) which is expressed on almost all leukocytes, although P-selectin also binds to heparan sulfate and fucoidan. PSGL-1 is situated on various hematopoietic cells such as neutrophils, eosinophils, lymphocytes, and monocytes, in which it mediates tethering and adhesion of these cells. However, PSGL-1 is not specific for P-selectin, as it can also function as a ligand for both E- and L-selectin.^[13]

Function

P-selectin plays an essential role in the initial recruitment of leukocytes (white blood cells) to the site of injury during inflammation. When endothelial cells are activated by molecules such as histamine or thrombin during inflammation, P-selectin moves from an internal cell location to the endothelial cell surface.

Thrombin is one trigger which can stimulate endothelial-cell release of P-selectin and recent studies suggest an additional Ca²⁺-independent pathway involved in release of P-selectin.^[14]

Ligands for P-selectin on eosinophils and neutrophils are similar sialylated, protease-sensitive, endo-beta-galactosidase-resistant structures, clearly different than those reported for E-selectin, and suggest disparate roles for P-selectin and E-selectin during recruitment during inflammatory responses.^[15]

P-selectin is also very important in the recruitment and aggregation of platelets at areas of vascular injury. In quiescent platelet, P-selectin is located on the inner wall of α-granules. Platelet activation (through agonists such as thrombin, Type II collagen and ADP) results in "membrane flipping" where the platelet releases α- and dense granules and the inner walls of the granules are exposed on the outside of the cell. The P-selectin then promotes platelet aggregation through platelet-fibrin and platelet-platelet binding.

P-selectin attaches to the actin cytoskeleton through anchor proteins that are still poorly characterized.

Role in cancer

P-selectin has a functional role in metastasis of tumor similar to E-selectin.^[16] P-selectin is expressed on the surface of both stimulated endothelial cell and activated platelet and helps cancer cells invade into bloodstream for metastasis and provided locally with multiple growth factors respectively.^[17] Moreover, it has been known that platelet facilitates tumor metastasis by forming complexes with tumor cells and leukocytes in the vasculature thus preventing recognition by macrophage, this is thought to contribute to the seeding of tumor microemboli to distant organs.^[18] In vivo mice experiment showed that reduction in circulating platelets could reduce cancer metastasis.^[19]

The oligosaccharide sialylated Lewis x (sLe(x)) is expressed on the surface of tumor cells and can be recognized by E-selectin and P-selectin, playing on a key role in metastasis of the tumor. However, in the 4T1 breast cancer cell line, E-selectin reactivity is sLe(x) dependent while P-selectin reactivity is sLe(x)-independent, suggesting P-selectin binding is Ca²⁺-independent and sulfation-dependent.^[20] One of the sulfated ligands is chondroitin sulfate, a type of glycosaminoglycan (GAG). Its activity in tumor metastasis has been probed by the addition of heparin that functions to blocks tumor metastasis. In addition to GAGs, mucin is of interest in P-selectin mediated tumor metastasis.^[21] Selective removal of mucin results in reduced interaction between P-selectin and platelets in vivo and in vitro.^[18]

Heparin has long been known to represent antiheparanase activity that is to keep an endoglycosidase from degrading heparin sulfate, one of the glycosaminoglycans, and to effectively inhibit P-selectin.^[22] Despite a striking effect of heparin on tumor progression shown in a number of clinical trials,^[23] the use of heparin as anti-cancer agent is limited because of its risk, which might induce adverse bleeding complications. Given those reasons, development of new compounds that target P-selectin is now emerging for cancer therapy. Among them, the inhibitory activity of semisynthetic sulfated tri mannose C-C-linked dimers (STMCs) to P-selectin was shown by the attenuation of tumor metastasis in vivo animal model, indicating the inhibition of interaction between tumor cell and endothelial cell is significant for blocking tumor dissemination.^[24]

References

^ Ryan US, Worthington RE (February 1992). "Cell-cell contact mechanisms". Curr. Opin. Immunol. 4 (1): 33–7. doi:10.1016/0952-7915(92)90120-4. PMID 1375831.
^ McEver RP, Beckstead JH, Moore KL, Marshall-Carlson L, Bainton DF (July 1989). "GMP-140, a platelet alpha-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies". J. Clin. Invest. 84 (1): 92–9. doi:10.1172/JCI114175. PMC 303957. PMID 2472431.
^ Herrmann SM, Ricard S, Nicaud V, Mallet C, Evans A, Ruidavets JB, Arveiler D, Luc G, Cambien F (August 1998). "The P-selectin gene is highly polymorphic: reduced frequency of the Pro715 allele carriers in patients with myocardial infarction". Hum. Mol. Genet. 7 (8): 1277–84. doi:10.1093/hmg/7.8.1277. PMID 9668170.
^ Pan J, Xia L, McEver RP (April 1998). "Comparison of promoters for the murine and human P-selectin genes suggests species-specific and conserved mechanisms for transcriptional regulation in endothelial cells". J. Biol. Chem. 273 (16): 10058–67. doi:10.1074/jbc.273.16.10058. PMID 9545353.
^ Disdier M, Morrissey JH, Fugate RD, Bainton DF, McEver RP (March 1992). "Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway". Mol. Biol. Cell 3 (3): 309–21. doi:10.1091/mbc.3.3.309. PMC 275532. PMID 1378326.
^ Hattori R, Hamilton KK, Fugate RD, McEver RP, Sims PJ (May 1989). "Stimulated secretion of endothelial von Willebrand factor is accompanied by rapid redistribution to the cell surface of the intracellular granule membrane protein GMP-140". J. Biol. Chem. 264 (14): 7768–71. PMID 2470733.
^ Hahne M, Jäger U, Isenmann S, Hallmann R, Vestweber D (May 1993). "Five tumor necrosis factor-inducible cell adhesion mechanisms on the surface of mouse endothelioma cells mediate the binding of leukocytes". J. Cell Biol. 121 (3): 655–64. doi:10.1083/jcb.121.3.655. PMC 2119562. PMID 7683689.
^ Liu et al., J. Exp. Med. Vol. 207 No. 13 2975-2987 www.jem.org/cgi/doi/10.1084/jem.20101545
^ Panes et al., Br J Pharmacol. 1999 February; 126(3): 537–550. at page 538 doi:10.1038/sj.bjp.0702328
^ Wang J, Li J, Liu Q (August 2005). "Association between platelet activation and fibrinolysis in acute stroke patients". Neurosci Lett. 384 (3): 305–9. doi:10.1016/j.neulet.2005.04.090. PMID 15916851.
^ Woltmann G, McNulty CA, Dewson G, Symon FA, Wardlaw AJ (May 2000). "Interleukin-13 induces PSGL-1/P-selectin-dependent adhesion of eosinophils, but not neutrophils, to human umbilical vein endothelial cells under flow". Blood 95 (10): 3146–52. PMID 10807781.
^ Vestweber D, Blanks JE (January 1999). "Mechanisms that regulate the function of the selectins and their ligands". Physiol. Rev. 79 (1): 181–213. PMID 9922371.
^ Lorenzon P, Vecile E, Nardon E, Ferrero E, Harlan JM, Tedesco F, Dobrina A (September 1998). "Endothelial cell E- and P-selectin and vascular cell adhesion molecule-1 function as signaling receptors". J. Cell Biol. 142 (5): 1381–91. doi:10.1083/jcb.142.5.1381. PMC 2149355. PMID 9732297.
^ Cleator JH, Zhu WQ, Vaughan DE, Hamm HE (April 2006). "Differential regulation of endothelial exocytosis of P-selectin and von Willebrand factor by protease-activated receptors and cAMP". Blood 107 (7): 2736–44. doi:10.1182/blood-2004-07-2698. PMC 1895372. PMID 16332977.
^ Wein M, Sterbinsky SA, Bickel CA, Schleimer RP, Bochner BS (March 1995). "Comparison of human eosinophil and neutrophil ligands for P-selectin: ligands for P-selectin differ from those for E-selectin". Am. J. Respir. Cell Mol. Biol. 12 (3): 315–9. doi:10.1165/ajrcmb.12.3.7532979. PMID 7532979.
^ Köhler S, Ullrich S, Richter U, Schumacher U (February 2010). "E-/P-selectins and colon carcinoma metastasis: first in vivo evidence for their crucial role in a clinically relevant model of spontaneous metastasis formation in the lung". Br. J. Cancer 102 (3): 602–9. doi:10.1038/sj.bjc.6605492. PMC 2822933. PMID 20010946.
^ Chen M, Geng JG (2006). "P-selectin mediates adhesion of leukocytes, platelets, and cancer cells in inflammation, thrombosis, and cancer growth and metastasis". Arch. Immunol. Ther. Exp. (Warsz.) 54 (2): 75–84. doi:10.1007/s00005-006-0010-6. PMID 16648968.
^ ^a ^b Borsig L, Wong R, Feramisco J, Nadeau DR, Varki NM, Varki A (March 2001). "Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3352–7. doi:10.1073/pnas.061615598. PMC 30657. PMID 11248082.
^ Gasic GJ (1984). "Role of plasma, platelets, and endothelial cells in tumor metastasis". Cancer Metastasis Rev. 3 (2): 99–114. doi:10.1007/BF00047657. PMID 6386144.
^ Monzavi-Karbassi B, Stanley JS, Hennings L, Jousheghany F, Artaud C, Shaaf S, Kieber-Emmons T (March 2007). "Chondroitin sulfate glycosaminoglycans as major P-selectin ligands on metastatic breast cancer cell lines". Int. J. Cancer 120 (6): 1179–91. doi:10.1002/ijc.22424. PMID 17154173.
^ Garcia J, Callewaert N, Borsig L (February 2007). "P-selectin mediates metastatic progression through binding to sulfatides on tumor cells". Glycobiology 17 (2): 185–96. doi:10.1093/glycob/cwl059. PMID 17043066.
^ Bar-Ner M, Eldor A, Wasserman L, Matzner Y, Cohen IR, Fuks Z, Vlodavsky I (August 1987). "Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin species". Blood 70 (2): 551–7. PMID 2955820.
^ Lazo-Langner A, Goss GD, Spaans JN, Rodger MA (April 2007). "The effect of low-molecular-weight heparin on cancer survival. A systematic review and meta-analysis of randomized trials". J. Thromb. Haemost. 5 (4): 729–37. doi:10.1111/j.1538-7836.2007.02427.x. PMID 17408406.
^ Borsig L, Vlodavsky I, Ishai-Michaeli R, Torri G, Vismara E (May 2011). "Sulfated hexasaccharides attenuate metastasis by inhibition of P-selectin and heparanase". Neoplasia 13 (5): 445–52. PMC 3084621. PMID 21532885.

External links

P-Selectin at the US National Library of Medicine Medical Subject Headings (MeSH)

English Journal

Laboratory assessment of anti-thrombotic therapy in heart failure, atrial fibrillation and coronary artery disease: insights using thrombelastography and a micro-titre plate assay of thrombogenesis and fibrinolysis.

Lau YC1, Xiong Q1,2, Ranjit P1, Lip GY1, Blann AD3.
Journal of thrombosis and thrombolysis.J Thromb Thrombolysis.2016 Aug;42(2):233-44. doi: 10.1007/s11239-016-1344-5.
As heart failure, coronary artery disease and atrial fibrillation all bring a risk of thrombosis, anti-thrombotic therapy is recommended. Despite such treatment, major cardiovascular events such as myocardial infarction and stroke still occur, implying inadequate suppression of thrombus formation. A
PMID 26942726

Simvastatin ameliorates deep vein thrombosis in rabbits by regulating the fibrinolytic system.

Feng Y1, Zhang F, Niu L, Zhang M.
Blood coagulation & fibrinolysis : an international journal in haemostasis and thrombosis.Blood Coagul Fibrinolysis.2016 Jul;27(5):531-541.
The study aimed to observe the therapeutic effect of simvastatin in a deep vein thrombosis (DVT) animal model and conduct a preliminary study into its mechanism. A total of 72 New Zealand white rabbits were randomly divided into control group (n = 18), low molecular weight heparin (LMWH) group (
PMID 27273142

D-allose protects the blood brain barrier through PPARγ-mediated anti-inflammatory pathway in the mice model of ischemia reperfusion injury.

Huang T1, Gao D1, Hei Y1, Zhang X1, Chen X1, Fei Z2.
Brain research.Brain Res.2016 Jul 1;1642:478-86. doi: 10.1016/j.brainres.2016.04.038. Epub 2016 Apr 19.
Our early experiments confirmed that D-allose was closely involved in the blood brain barrier (BBB) protection from ischemia reperfusion (IR) injury, but the regulatory mechanism is not fully defined. In this study, we aimed to investigate the role of D-allose in the protection of BBB integrity and
PMID 27103568

Japanese Journal

気菅支ぜん息患者の気管支粘膜における細胞浸潤と接着分子発現について

日本胸部疾患学会雑誌 34(12), 1317-1325, 1996
NAID 130003450427

Elevated Plasma Levels of P-Selectin (GMP-140/CD62P) in Patients with <i>Plasmodium falciparum</i> Malaria

MICROBIOLOGY and IMMUNOLOGY 38(9), 727-731, 1994
NAID 130003484150

Ｌ‐セレクチン：レクチン様白血球接着因子:レクチン様白血球接着因子

Trends in Glycoscience and Glycotechnology 4(15), 1-13, 1992
NAID 130003699073

Related Pictures

[pmid1375831-1] Ryan US, Worthington RE (February 1992). "Cell-cell contact mechanisms". Curr. Opin. Immunol. 4 (1): 33–7. doi:10.1016/0952-7915(92)90120-4. PMID 1375831.

[pmid2472431-2] McEver RP, Beckstead JH, Moore KL, Marshall-Carlson L, Bainton DF (July 1989). "GMP-140, a platelet alpha-granule membrane protein, is also synthesized by vascular endothelial cells and is localized in Weibel-Palade bodies". J. Clin. Invest. 84 (1): 92–9. doi:10.1172/JCI114175. PMC 303957. PMID 2472431.

[pmid9668170-3] Herrmann SM, Ricard S, Nicaud V, Mallet C, Evans A, Ruidavets JB, Arveiler D, Luc G, Cambien F (August 1998). "The P-selectin gene is highly polymorphic: reduced frequency of the Pro715 allele carriers in patients with myocardial infarction". Hum. Mol. Genet. 7 (8): 1277–84. doi:10.1093/hmg/7.8.1277. PMID 9668170.

[pmid9545353-4] Pan J, Xia L, McEver RP (April 1998). "Comparison of promoters for the murine and human P-selectin genes suggests species-specific and conserved mechanisms for transcriptional regulation in endothelial cells". J. Biol. Chem. 273 (16): 10058–67. doi:10.1074/jbc.273.16.10058. PMID 9545353.

[pmid1378326-5] Disdier M, Morrissey JH, Fugate RD, Bainton DF, McEver RP (March 1992). "Cytoplasmic domain of P-selectin (CD62) contains the signal for sorting into the regulated secretory pathway". Mol. Biol. Cell 3 (3): 309–21. doi:10.1091/mbc.3.3.309. PMC 275532. PMID 1378326.

[pmid2470733-6] Hattori R, Hamilton KK, Fugate RD, McEver RP, Sims PJ (May 1989). "Stimulated secretion of endothelial von Willebrand factor is accompanied by rapid redistribution to the cell surface of the intracellular granule membrane protein GMP-140". J. Biol. Chem. 264 (14): 7768–71. PMID 2470733.

[pmid7683689-7] Hahne M, Jäger U, Isenmann S, Hallmann R, Vestweber D (May 1993). "Five tumor necrosis factor-inducible cell adhesion mechanisms on the surface of mouse endothelioma cells mediate the binding of leukocytes". J. Cell Biol. 121 (3): 655–64. doi:10.1083/jcb.121.3.655. PMC 2119562. PMID 7683689.

[8] Liu et al., J. Exp. Med. Vol. 207 No. 13 2975-2987 www.jem.org/cgi/doi/10.1084/jem.20101545

[9] Panes et al., Br J Pharmacol. 1999 February; 126(3): 537–550. at page 538 doi:10.1038/sj.bjp.0702328

[pmid15916851-10] Wang J, Li J, Liu Q (August 2005). "Association between platelet activation and fibrinolysis in acute stroke patients". Neurosci Lett. 384 (3): 305–9. doi:10.1016/j.neulet.2005.04.090. PMID 15916851.

[pmid10807781-11] Woltmann G, McNulty CA, Dewson G, Symon FA, Wardlaw AJ (May 2000). "Interleukin-13 induces PSGL-1/P-selectin-dependent adhesion of eosinophils, but not neutrophils, to human umbilical vein endothelial cells under flow". Blood 95 (10): 3146–52. PMID 10807781.

[pmid9922371-12] Vestweber D, Blanks JE (January 1999). "Mechanisms that regulate the function of the selectins and their ligands". Physiol. Rev. 79 (1): 181–213. PMID 9922371.

[pmid9732297-13] Lorenzon P, Vecile E, Nardon E, Ferrero E, Harlan JM, Tedesco F, Dobrina A (September 1998). "Endothelial cell E- and P-selectin and vascular cell adhesion molecule-1 function as signaling receptors". J. Cell Biol. 142 (5): 1381–91. doi:10.1083/jcb.142.5.1381. PMC 2149355. PMID 9732297.

[pmid16332977-14] Cleator JH, Zhu WQ, Vaughan DE, Hamm HE (April 2006). "Differential regulation of endothelial exocytosis of P-selectin and von Willebrand factor by protease-activated receptors and cAMP". Blood 107 (7): 2736–44. doi:10.1182/blood-2004-07-2698. PMC 1895372. PMID 16332977.

[pmid7532979-15] Wein M, Sterbinsky SA, Bickel CA, Schleimer RP, Bochner BS (March 1995). "Comparison of human eosinophil and neutrophil ligands for P-selectin: ligands for P-selectin differ from those for E-selectin". Am. J. Respir. Cell Mol. Biol. 12 (3): 315–9. doi:10.1165/ajrcmb.12.3.7532979. PMID 7532979.

[pmid20010946-16] Köhler S, Ullrich S, Richter U, Schumacher U (February 2010). "E-/P-selectins and colon carcinoma metastasis: first in vivo evidence for their crucial role in a clinically relevant model of spontaneous metastasis formation in the lung". Br. J. Cancer 102 (3): 602–9. doi:10.1038/sj.bjc.6605492. PMC 2822933. PMID 20010946.

[pmid16648968-17] Chen M, Geng JG (2006). "P-selectin mediates adhesion of leukocytes, platelets, and cancer cells in inflammation, thrombosis, and cancer growth and metastasis". Arch. Immunol. Ther. Exp. (Warsz.) 54 (2): 75–84. doi:10.1007/s00005-006-0010-6. PMID 16648968.

[pmid11248082-18] Borsig L, Wong R, Feramisco J, Nadeau DR, Varki NM, Varki A (March 2001). "Heparin and cancer revisited: mechanistic connections involving platelets, P-selectin, carcinoma mucins, and tumor metastasis". Proc. Natl. Acad. Sci. U.S.A. 98 (6): 3352–7. doi:10.1073/pnas.061615598. PMC 30657. PMID 11248082.

[pmid6386144-19] Gasic GJ (1984). "Role of plasma, platelets, and endothelial cells in tumor metastasis". Cancer Metastasis Rev. 3 (2): 99–114. doi:10.1007/BF00047657. PMID 6386144.

[pmid17154173-20] Monzavi-Karbassi B, Stanley JS, Hennings L, Jousheghany F, Artaud C, Shaaf S, Kieber-Emmons T (March 2007). "Chondroitin sulfate glycosaminoglycans as major P-selectin ligands on metastatic breast cancer cell lines". Int. J. Cancer 120 (6): 1179–91. doi:10.1002/ijc.22424. PMID 17154173.

[pmid17043066-21] Garcia J, Callewaert N, Borsig L (February 2007). "P-selectin mediates metastatic progression through binding to sulfatides on tumor cells". Glycobiology 17 (2): 185–96. doi:10.1093/glycob/cwl059. PMID 17043066.

[pmid2955820-22] Bar-Ner M, Eldor A, Wasserman L, Matzner Y, Cohen IR, Fuks Z, Vlodavsky I (August 1987). "Inhibition of heparanase-mediated degradation of extracellular matrix heparan sulfate by non-anticoagulant heparin species". Blood 70 (2): 551–7. PMID 2955820.

[pmid17408406-23] Lazo-Langner A, Goss GD, Spaans JN, Rodger MA (April 2007). "The effect of low-molecular-weight heparin on cancer survival. A systematic review and meta-analysis of randomized trials". J. Thromb. Haemost. 5 (4): 729–37. doi:10.1111/j.1538-7836.2007.02427.x. PMID 17408406.

[pmid21532885-24] Borsig L, Vlodavsky I, Ishai-Michaeli R, Torri G, Vismara E (May 2011). "Sulfated hexasaccharides attenuate metastasis by inhibition of P-selectin and heparanase". Neoplasia 13 (5): 445–52. PMC 3084621. PMID 21532885.

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