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Home / Equine Research Bank / Sci Rep / Unique insertion/deletion polymorphisms within histidine-ric...
Scientific reports2023; 13(1); 300; doi: 10.1038/s41598-023-27374-0

Unique insertion/deletion polymorphisms within histidine-rich region of histidine-rich glycoprotein in Thoroughbred horses.

Abstract: Histidine-rich glycoprotein (HRG) is abundant plasma protein with various effects on angiogenesis, coagulation, and immune responses. Previously, we identified the base and amino acid sequences of equine HRG (eHRG) and revealed that eHRG regulates neutrophil functions. In this study, we first conducted a large-scale gene analysis with DNA samples extracted from 1700 Thoroughbred horses and identified unique insertion/deletion polymorphisms in the histidine-rich region (HRR) of eHRG. Here we report two types of polymorphisms (deletion type 1 [D1] and deletion type 2 [D2]) containing either a 45 bp or 90 bp deletion in the HRR of eHRG, and five genotypes of eHRG (insertion/insertion [II], ID1, ID2, D1D1, and D1D2) in Thoroughbred horses. Allele frequency of I, D1, and D2, was 0.483, 0.480, and 0.037 and the incidence of each genotype was II: 23.4%, ID1: 46.2%, ID2: 3.6%, D1D1: 23.1%, and D1D2: 3.7%, respectively. The molecular weights of each plasma eHRG protein collected from horses with each genotype was detected as bands of different molecular size, which corresponded to the estimated amino acid sequence. The nickel-binding affinity of the D1 or D2 deletion eHRG was reduced, indicating a loss of function at the site. eHRG proteins show a variety of biological and immunological activities in vivo, and HRR is its active center, suggesting that genetic polymorphisms in eHRG may be involved in the performance in athletic ability, productivity, and susceptibility to infectious diseases in Thoroughbred horses.
© 2023. The Author(s).
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Publication Date: 2023-01-06 PubMed ID: 36609619PubMed Central: PMC9822902DOI: 10.1038/s41598-023-27374-0Google Scholar: Lookup
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Summary

This research summary has been generated with artificial intelligence and may contain errors and omissions. Refer to the original study to confirm details provided. Submit correction.

This research article explores the unique insertion or deletion polymorphisms found in the histidine-rich region of histidine-rich glycoprotein (HRG) in Thoroughbred horses. It suggests that these variations could possibly influence the horses’ athletic performance, productivity, and susceptibility to diseases.

Background of the Research

  • The research is centered around Histidine-rich glycoprotein (HRG), a prevalent plasma protein noted for its diverse effects on angiogenesis (formation of new blood vessels), coagulation (ability to form blood clots), and immune responses.
  • The researchers have previously determined the base and amino acid sequences of equine HRG (eHRG), which is the horse equivalent of the HRG, and discovered that eHRG helps regulate neutrophil functions. Neutrophils are the key components of a body’s first line of defense in its immune system.

Identification of Unique Polymorphisms

  • Building on their previous work, the researchers conducted a broad gene analysis using DNA samples extracted from 1700 Thoroughbred horses.
  • The results demonstrated unique insertion and deletion polymorphisms in the histidine-rich region (HRR) of eHRG.
  • Two types of polymorphisms were reported: deletion type 1 (D1) and deletion type 2 (D2). These respectively involve either a 45 base pair or 90 base pair deletion in the HRR of eHRG.
  • The study also revealed five distinct genotypes or genetic variations of eHRG among the Thoroughbred horses examined.

Genotypes and Their Frequencies

  • The allele frequency (the frequency of a particular gene variant) for each genotype (I, D1, and D2) was also reported in the study.
  • A corresponding percentage of horses displaying each genotype was also noted – II: 23.4%, ID1: 46.2%, ID2: 3.6%, D1D1: 23.1%, and D1D2: 3.7%.
  • The researchers were also able to detect the distinct molecular weights of the eHRG protein collected from the plasma of horses with each genotype.

Potential Impact of eHRG on Horse Performance and Health

  • The research found that the deletion of D1 or D2 eHRG reduced the nickel-binding affinity, implying a loss of function at the site.
  • Since eHRG proteins regulate a wide range of biological and immunological activities in vivo (in a living organism), the active center, HRR, could be instrumental in determining horse performance and susceptibility to diseases.
  • Therefore, the unique genetic variability in the horse’s eHRG may have crucial implications on the horse’s athletic ability, productivity, and vulnerability to infectious diseases.

Cite This Article

APA
Muko R, Sunouchi T, Urayama S, Toishi Y, Kusano K, Sato H, Muranaka M, Shin T, Oikawa MA, Ojima Y, Ali M, Nomura Y, Matsuda H, Tanaka A. (2023). Unique insertion/deletion polymorphisms within histidine-rich region of histidine-rich glycoprotein in Thoroughbred horses. Sci Rep, 13(1), 300. https://doi.org/10.1038/s41598-023-27374-0

Publication

Scientific reports
ISSN: 2045-2322
NlmUniqueID: 101563288
Country: England
Language: English
Volume: 13
Issue: 1
Pages: 300
PII: 300

Researcher Affiliations

Muko, Ryo
  • Institute of Global Innovation Research, Tokyo University of Agriculture and Technology, Tokyo, Japan.
Sunouchi, Tomoya
  • Laboratory of Comparative Animal Medicine, Division of Animal Life Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo, 183-8509, Japan.
Urayama, Shuntaro
  • Race Horse Clinic, Ritto Training Center, Japan Racing Association, Shiga, Japan.
Toishi, Yuko
  • Shadai Stallion Station, Shadai Corporation, Hokkaido, Japan.
Kusano, Kanichi
  • Race Horse Clinic, Ritto Training Center, Japan Racing Association, Shiga, Japan.
Sato, Hiroaki
  • Race Integrity Section, Stewards Department, Japan Racing Association, Tokyo, Japan.
Muranaka, Masanori
  • Race Horse Clinic, Ritto Training Center, Japan Racing Association, Shiga, Japan.
Shin, Taekyun
  • Department of Veterinary Anatomy, College of Veterinary Medicine and Veterinary Medical Research Institute, Jeju National University, Jeju, South Korea.
Oikawa, Masa-Aki
  • Diagnostic Laboratory, Equine Veterinary Medical Center, Education City, Doha, Qatar.
Ojima, Yoshinobu
  • Institute of Global Innovation Research, Tokyo University of Agriculture and Technology, Tokyo, Japan.
Ali, Mohammad
  • Diagnostic Laboratory, Equine Veterinary Medical Center, Education City, Doha, Qatar.
Nomura, Yoshihiro
  • Scleroprotein and Leather Research Institute, Faculty of Agriculture, Tokyo University of Agriculture and Technology, Tokyo, Japan.
Matsuda, Hiroshi
  • Laboratory of Comparative Animal Medicine, Division of Animal Life Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo, 183-8509, Japan.
Tanaka, Akane
  • Institute of Global Innovation Research, Tokyo University of Agriculture and Technology, Tokyo, Japan. akane@cc.tuat.ac.jp.
  • Laboratory of Comparative Animal Medicine, Division of Animal Life Science, Faculty of Agriculture, Tokyo University of Agriculture and Technology, 3-5-8 Saiwai-cho, Fuchu, Tokyo, 183-8509, Japan. akane@cc.tuat.ac.jp.
  • Cooperative Major in Advanced Health Science, Graduate School of Bio-Applications and System Engineering, Tokyo University of Agriculture and Technology, Tokyo, Japan. akane@cc.tuat.ac.jp.

MeSH Terms

  • Animals
  • Horses / genetics
  • Histidine
  • Amino Acid Sequence
  • Blood Proteins
  • Polymorphism, Genetic

Conflict of Interest Statement

The authors declare no competing interests.

References

This article includes 38 references
  1. Librado P, Khan N, Fages A, Kusliy MA, Suchan T, Tonasso-Calvière L, Schiavinato S, Alioglu D, Fromentier A, Perdereau A, Aury JM, Gaunitz C, Chauvey L, Seguin-Orlando A, Der Sarkissian C, Southon J, Shapiro B, Tishkin AA, Kovalev AA, Alquraishi S, Alfarhan AH, Al-Rasheid KAS, Seregély T, Klassen L, Iversen R, Bignon-Lau O, Bodu P, Olive M, Castel JC, Boudadi-Maligne M, Alvarez N, Germonpré M, Moskal-Del Hoyo M, Wilczyński J, Pospuła S, Lasota-Kuś A, Tunia K, Nowak M, Rannamäe E, Saarma U, Boeskorov G, Lōugas L, Kyselý R, Peške L, Bălășescu A, Dumitrașcu V, Dobrescu R, Gerber D, Kiss V, Szécsényi-Nagy A, Mende BG, Gallina Z, Somogyi K, Kulcsár G, Gál E, Bendrey R, Allentoft ME, Sirbu G, Dergachev V, Shephard H, Tomadini N, Grouard S, Kasparov A, Basilyan AE, Anisimov MA, Nikolskiy PA, Pavlova EY, Pitulko V, Brem G, Wallner B, Schwall C, Keller M, Kitagawa K, Bessudnov AN, Bessudnov A, Taylor W, Magail J, Gantulga JO, Bayarsaikhan J, Erdenebaatar D, Tabaldiev K, Mijiddorj E, Boldgiv B, Tsagaan T, Pruvost M, Olsen S, Makarewicz CA, Valenzuela Lamas S, Albizuri Canadell S, Nieto Espinet A, Iborra MP, Lira Garrido J, Rodríguez González E, Celestino S, Olària C, Arsuaga JL, Kotova N, Pryor A, Crabtree P, Zhumatayev R, Toleubaev A, Morgunova NL, Kuznetsova T, Lordkipanize D, Marzullo M, Prato O, Bagnasco Gianni G, Tecchiati U, Clavel B, Lepetz S, Davoudi H, Mashkour M, Berezina NY, Stockhammer PW, Krause J, Haak W, Morales-Muñiz A, Benecke N, Hofreiter M, Ludwig A, Graphodatsky AS, Peters J, Kiryushin KY, Iderkhangai TO, Bokovenko NA, Vasiliev SK, Seregin NN, Chugunov KV, Plasteeva NA, Baryshnikov GF, Petrova E, Sablin M, Ananyevskaya E, Logvin A, Shevnina I, Logvin V, Kalieva S, Loman V, Kukushkin I, Merz I, Merz V, Sakenov S, Varfolomeyev V, Usmanova E, Zaibert V, Arbuckle B, Belinskiy AB, Kalmykov A, Reinhold S, Hansen S, Yudin AI, Vybornov AA, Epimakhov A, Berezina NS, Roslyakova N, Kosintsev PA, Kuznetsov PF, Anthony D, Kroonen GJ, Kristiansen K, Wincker P, Outram A, Orlando L. The origins and spread of domestic horses from the Western Eurasian steppes.. Nature 2021 Oct;598(7882):634-640.
    doi: 10.1038/s41586-021-04018-9pmc: PMC8550961pubmed: 34671162google scholar: lookup
  2. . Remembering the real war horses.. Vet Rec 2011 Nov 19;169(21):543.
    pubmed: 22102349doi: 10.1136/vr.d7342google scholar: lookup
  3. Sheats MK. A Comparative Review of Equine SIRS, Sepsis, and Neutrophils.. Front Vet Sci 2019;6:69.
    doi: 10.3389/fvets.2019.00069pmc: PMC6424004pubmed: 30931316google scholar: lookup
  4. Kuroda K, Wake H, Mori S, Hinotsu S, Nishibori M, Morimatsu H. Decrease in Histidine-Rich Glycoprotein as a Novel Biomarker to Predict Sepsis Among Systemic Inflammatory Response Syndrome.. Crit Care Med 2018 Apr;46(4):570-576.
    doi: 10.1097/ccm.0000000000002947pubmed: 29303798google scholar: lookup
  5. Kuroda K, Ishii K, Mihara Y, Kawanoue N, Wake H, Mori S, Yoshida M, Nishibori M, Morimatsu H. Histidine-rich glycoprotein as a prognostic biomarker for sepsis.. Sci Rep 2021 May 13;11(1):10223.
    doi: 10.1038/s41598-021-89555-zpmc: PMC8119687pubmed: 33986340google scholar: lookup
  6. Poon IK, Patel KK, Davis DS, Parish CR, Hulett MD. Histidine-rich glycoprotein: the Swiss Army knife of mammalian plasma.. Blood 2011 Feb 17;117(7):2093-101.
    doi: 10.1182/blood-2010-09-303842pubmed: 20971949google scholar: lookup
  7. Wakabayashi S. New insights into the functions of histidine-rich glycoprotein.. Int Rev Cell Mol Biol 2013;304:467-93.
    doi: 10.1016/b978-0-12-407696-9.00009-9pubmed: 23809442google scholar: lookup
  8. Drasin T, Sahud M. Blood-type and age affect human plasma levels of histidine-rich glycoprotein in a large population.. Thromb Res 1996 Nov 1;84(3):179-88.
    doi: 10.1016/0049-3848(96)00174-0pubmed: 8914217google scholar: lookup
  9. Lijnen HR, Hoylaerts M, Collen D. Heparin binding properties of human histidine-rich glycoprotein. Mechanism and role in the neutralization of heparin in plasma.. J Biol Chem 1983 Mar 25;258(6):3803-8.
    doi: 10.1016/S0021-9258(18)32737-6pubmed: 6833231google scholar: lookup
  10. Leung LL. Interaction of histidine-rich glycoprotein with fibrinogen and fibrin.. J Clin Invest 1986 Apr;77(4):1305-11.
    doi: 10.1172/jci112435pmc: PMC424483pubmed: 3958188google scholar: lookup
  11. Silverstein RL, Leung LL, Harpel PC, Nachman RL. Platelet thrombospondin forms a trimolecular complex with plasminogen and histidine-rich glycoprotein.. J Clin Invest 1985 Jun;75(6):2065-73.
    doi: 10.1172/jci111926pmc: PMC425568pubmed: 4008652google scholar: lookup
  12. Priebatsch KM, Kvansakul M, Poon IK, Hulett MD. Functional Regulation of the Plasma Protein Histidine-Rich Glycoprotein by Zn(2+) in Settings of Tissue Injury.. Biomolecules 2017 Mar 2;7(1).
    doi: 10.3390/biom7010022pmc: PMC5372734pubmed: 28257077google scholar: lookup
  13. Manderson GA, Martin M, Onnerfjord P, Saxne T, Schmidtchen A, Mollnes TE, Heinegård D, Blom AM. Interactions of histidine-rich glycoprotein with immunoglobulins and proteins of the complement system.. Mol Immunol 2009 Oct;46(16):3388-98.
    doi: 10.1016/j.molimm.2009.07.011pubmed: 19674792google scholar: lookup
  14. Jones AL, Hulett MD, Parish CR. Histidine-rich glycoprotein: A novel adaptor protein in plasma that modulates the immune, vascular and coagulation systems.. Immunol Cell Biol 2005 Apr;83(2):106-18.
    doi: 10.1111/j.1440-1711.2005.01320.xpubmed: 15748207google scholar: lookup
  15. Wake H, Mori S, Liu K, Morioka Y, Teshigawara K, Sakaguchi M, Kuroda K, Gao Y, Takahashi H, Ohtsuka A, Yoshino T, Morimatsu H, Nishibori M. Histidine-Rich Glycoprotein Prevents Septic Lethality through Regulation of Immunothrombosis and Inflammation.. EBioMedicine 2016 Jul;9:180-194.
    doi: 10.1016/j.ebiom.2016.06.003pmc: PMC4972547pubmed: 27333033google scholar: lookup
  16. Nishibori M, Wake H, Morimatsu H. Histidine-rich glycoprotein as an excellent biomarker for sepsis and beyond.. Crit Care 2018 Aug 17;22(1):209.
    doi: 10.1186/s13054-018-2127-5pmc: PMC6097411pubmed: 30119699google scholar: lookup
  17. Shigekiyo T, Yoshida H, Matsumoto K, Azuma H, Wakabayashi S, Saito S, Fujikawa K, Koide T. HRG Tokushima: molecular and cellular characterization of histidine-rich glycoprotein (HRG) deficiency.. Blood 1998 Jan 1;91(1):128-33.
    doi: 10.1182/blood.V91.1.128pubmed: 9414276google scholar: lookup
  18. Lindgren KE, Nordqvist S, Kårehed K, Sundström-Poromaa I, Åkerud H. The effect of a specific histidine-rich glycoprotein polymorphism on male infertility and semen parameters.. Reprod Biomed Online 2016 Aug;33(2):180-8.
    doi: 10.1016/j.rbmo.2016.05.004pubmed: 27210772google scholar: lookup
  19. Nordqvist S, Kårehed K, Stavreus-Evers A, Akerud H. Histidine-rich glycoprotein polymorphism and pregnancy outcome: a pilot study.. Reprod Biomed Online 2011 Aug;23(2):213-9.
    doi: 10.1016/j.rbmo.2011.04.004pubmed: 21665544google scholar: lookup
  20. Cunningham F, Allen JE, Allen J, Alvarez-Jarreta J, Amode MR, Armean IM, Austine-Orimoloye O, Azov AG, Barnes I, Bennett R, Berry A, Bhai J, Bignell A, Billis K, Boddu S, Brooks L, Charkhchi M, Cummins C, Da Rin Fioretto L, Davidson C, Dodiya K, Donaldson S, El Houdaigui B, El Naboulsi T, Fatima R, Giron CG, Genez T, Martinez JG, Guijarro-Clarke C, Gymer A, Hardy M, Hollis Z, Hourlier T, Hunt T, Juettemann T, Kaikala V, Kay M, Lavidas I, Le T, Lemos D, Marugán JC, Mohanan S, Mushtaq A, Naven M, Ogeh DN, Parker A, Parton A, Perry M, Piližota I, Prosovetskaia I, Sakthivel MP, Salam AIA, Schmitt BM, Schuilenburg H, Sheppard D, Pérez-Silva JG, Stark W, Steed E, Sutinen K, Sukumaran R, Sumathipala D, Suner MM, Szpak M, Thormann A, Tricomi FF, Urbina-Gómez D, Veidenberg A, Walsh TA, Walts B, Willhoft N, Winterbottom A, Wass E, Chakiachvili M, Flint B, Frankish A, Giorgetti S, Haggerty L, Hunt SE, IIsley GR, Loveland JE, Martin FJ, Moore B, Mudge JM, Muffato M, Perry E, Ruffier M, Tate J, Thybert D, Trevanion SJ, Dyer S, Harrison PW, Howe KL, Yates AD, Zerbino DR, Flicek P. Ensembl 2022.. Nucleic Acids Res 2022 Jan 7;50(D1):D988-D995.
    doi: 10.1093/nar/gkab1049pmc: PMC8728283pubmed: 34791404google scholar: lookup
  21. Tripodi A, Chantarangkul V, Martinelli I, Bucciarelli P, Mannucci PM. A shortened activated partial thromboplastin time is associated with the risk of venous thromboembolism.. Blood 2004 Dec 1;104(12):3631-4.
    doi: 10.1182/blood-2004-03-1042pubmed: 15297315google scholar: lookup
  22. Houlihan LM, Davies G, Tenesa A, Harris SE, Luciano M, Gow AJ, McGhee KA, Liewald DC, Porteous DJ, Starr JM, Lowe GD, Visscher PM, Deary IJ. Common variants of large effect in F12, KNG1, and HRG are associated with activated partial thromboplastin time.. Am J Hum Genet 2010 Apr 9;86(4):626-31.
    doi: 10.1016/j.ajhg.2010.02.016pmc: PMC2850435pubmed: 20303064google scholar: lookup
  23. Muko R, Amagai Y, Matsuda K, Matsuda H, Tanaka A. Cloning and detection of equine histidine-rich glycoprotein. J. Equine Vet. Sci. 2019;73:121–126.
    doi: 10.1016/j.jevs.2018.12.009google scholar: lookup
  24. Muko R, Matsuda H, Oikawa MA, Shin T, Matsuda K, Sato H, Sunouchi T, Tanaka A. Histidine-Rich Glycoprotein Functions as a Dual Regulator of Neutrophil Activity in Horses.. J Equine Vet Sci 2021 Jul;102:103620.
    doi: 10.1016/j.jevs.2021.103620pubmed: 34119191google scholar: lookup
  25. Mori S, Takahashi HK, Yamaoka K, Okamoto M, Nishibori M. High affinity binding of serum histidine-rich glycoprotein to nickel-nitrilotriacetic acid: the application to microquantification.. Life Sci 2003 May 23;73(1):93-102.
    doi: 10.1016/s0024-3205(03)00261-3pubmed: 12726890google scholar: lookup
  26. Patel KK, Poon IK, Talbo GH, Perugini MA, Taylor NL, Ralph TJ, Hoogenraad NJ, Hulett MD. New method for purifying histidine-rich glycoprotein from human plasma redefines its functional properties.. IUBMB Life 2013 Jun;65(6):550-63.
    doi: 10.1002/iub.1168pubmed: 23576524google scholar: lookup
  27. Vu TT, Zhou J, Leslie BA, Stafford AR, Fredenburgh JC, Ni R, Qiao S, Vaezzadeh N, Jahnen-Dechent W, Monia BP, Gross PL, Weitz JI. Arterial thrombosis is accelerated in mice deficient in histidine-rich glycoprotein.. Blood 2015 Apr 23;125(17):2712-9.
    doi: 10.1182/blood-2014-11-611319pmc: PMC4416941pubmed: 25691157google scholar: lookup
  28. Kassaar O, Schwarz-Linek U, Blindauer CA, Stewart AJ. Plasma free fatty acid levels influence Zn(2+) -dependent histidine-rich glycoprotein-heparin interactions via an allosteric switch on serum albumin.. J Thromb Haemost 2015 Jan;13(1):101-10.
    doi: 10.1111/jth.12771pmc: PMC4309485pubmed: 25353308google scholar: lookup
  29. Horne MK 3rd, Merryman PK, Cullinane AM. Histidine-proline-rich glycoprotein binding to platelets mediated by transition metals.. Thromb Haemost 2001 May;85(5):890-5.
    doi: 10.1055/s-0037-1615764pubmed: 11372684google scholar: lookup
  30. Priebatsch KM, Poon IK, Patel KK, Kvansakul M, Hulett MD. Divalent metal binding by histidine-rich glycoprotein differentially regulates higher order oligomerisation and proteolytic processing.. FEBS Lett 2017 Jan;591(1):164-176.
    doi: 10.1002/1873-3468.12520pubmed: 27930811google scholar: lookup
  31. Morgan WT. Interactions of the histidine-rich glycoprotein of serum with metals.. Biochemistry 1981 Mar 3;20(5):1054-61.
    doi: 10.1021/bi00508a002pubmed: 7225317google scholar: lookup
  32. Poon IK, Olsson AK, Hulett MD, Parish CR. Regulation of histidine-rich glycoprotein (HRG) function via plasmin-mediated proteolytic cleavage.. Biochem J 2009 Oct 23;424(1):27-37.
    doi: 10.1042/bj20090794pubmed: 19712047google scholar: lookup
  33. Schneider LA, Korber A, Grabbe S, Dissemond J. Influence of pH on wound-healing: a new perspective for wound-therapy?. Arch Dermatol Res 2007 Feb;298(9):413-20.
    doi: 10.1007/s00403-006-0713-xpubmed: 17091276google scholar: lookup
  34. Rydengård V, Olsson AK, Mörgelin M, Schmidtchen A. Histidine-rich glycoprotein exerts antibacterial activity.. FEBS J 2007 Jan;274(2):377-89.
    doi: 10.1111/j.1742-4658.2006.05586.xpubmed: 17229145google scholar: lookup
  35. Kacprzyk L, Rydengård V, Mörgelin M, Davoudi M, Pasupuleti M, Malmsten M, Schmidtchen A. Antimicrobial activity of histidine-rich peptides is dependent on acidic conditions.. Biochim Biophys Acta 2007 Nov;1768(11):2667-80.
    doi: 10.1016/j.bbamem.2007.06.020pubmed: 17655823google scholar: lookup
  36. Rydengård V, Shannon O, Lundqvist K, Kacprzyk L, Chalupka A, Olsson AK, Mörgelin M, Jahnen-Dechent W, Malmsten M, Schmidtchen A. Histidine-rich glycoprotein protects from systemic Candida infection.. PLoS Pathog 2008 Aug 1;4(8):e1000116.
    doi: 10.1371/journal.ppat.1000116pmc: PMC2537934pubmed: 18797515google scholar: lookup
  37. Simantov R, Febbraio M, Crombie R, Asch AS, Nachman RL, Silverstein RL. Histidine-rich glycoprotein inhibits the antiangiogenic effect of thrombospondin-1.. J Clin Invest 2001 Jan;107(1):45-52.
    doi: 10.1172/jci9061pmc: PMC198540pubmed: 11134179google scholar: lookup
  38. Dixelius J, Olsson AK, Thulin A, Lee C, Johansson I, Claesson-Welsh L. Minimal active domain and mechanism of action of the angiogenesis inhibitor histidine-rich glycoprotein.. Cancer Res 2006 Feb 15;66(4):2089-97.
    doi: 10.1158/0008-5472.can-05-2217pubmed: 16489009google scholar: lookup

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