CD31

PECAM-1 is a highly glycosylated protein with a mass of approximately 130 kDa.{{cite journal | vauthors = Simmons DL, Walker C, Power C, Pigott R | title = Molecular cloning of CD31, a putative intercellular adhesion molecule closely related to carcinoembryonic antigen | journal = The Journal of Experimental Medicine | volume = 171 | issue = 6 | pages = 2147–2152 | date = June 1990 | pmid = 2351935 | pmc = 2187965 | doi = 10.1084/jem.171.6.2147 }} The structure of this protein was determined by molecular cloning in 1990, when it was found out that PECAM-1 has an N-terminal domain with 574 amino acids, a transmembrane domain with 19 amino acids and a C-terminal cytoplasmic domain with 118 amino acids. The N-terminal domain consists of six extracellular Ig-like domains.{{cite journal | vauthors = Newman PJ, Berndt MC, Gorski J, White GC, Lyman S, Paddock C, Muller WA | title = PECAM-1 (CD31) cloning and relation to adhesion molecules of the immunoglobulin gene superfamily | journal = Science | volume = 247 | issue = 4947 | pages = 1219–1222 | date = March 1990 | pmid = 1690453 | doi = 10.1126/science.1690453 | bibcode = 1990Sci...247.1219N }}

PECAM-1 is a cell-cell adhesion protein{{cite journal | vauthors = Albelda SM, Muller WA, Buck CA, Newman PJ | title = Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel vascular cell-cell adhesion molecule | journal = The Journal of Cell Biology | volume = 114 | issue = 5 | pages = 1059–1068 | date = September 1991 | pmid = 1874786 | pmc = 2289123 | doi = 10.1083/jcb.114.5.1059 }} which interacts with other PECAM-1 molecules through homophilic interactions or with non-PECAM-1 molecules through heterophilic interactions.{{cite journal | vauthors = DeLisser HM, Newman PJ, Albelda SM | title = Molecular and functional aspects of PECAM-1/CD31 | journal = Immunology Today | volume = 15 | issue = 10 | pages = 490–495 | date = October 1994 | pmid = 7945775 | doi = 10.1016/0167-5699(94)90195-3 }} Homophilic interactions between PECAM-1 molecules are mediated by antiparallel interactions between extracellular Ig-like domain 1 and Ig-like domain 2. These interactions are regulated by the level of PECAM-1 expression. Homophilic interactions occur, only when the surface expression of PECAM-1 is high. Otherwise, when expression is low, heterophilic interactions occur.{{cite journal | vauthors = Sun J, Williams J, Yan HC, Amin KM, Albelda SM, DeLisser HM | title = Platelet endothelial cell adhesion molecule-1 (PECAM-1) homophilic adhesion is mediated by immunoglobulin-like domains 1 and 2 and depends on the cytoplasmic domain and the level of surface expression | journal = The Journal of Biological Chemistry | volume = 271 | issue = 31 | pages = 18561–18570 | date = August 1996 | pmid = 8702505 | doi = 10.1074/jbc.271.31.18561 | doi-access = free }}

CD31 is normally found on endothelial cells, platelets, macrophages and Kupffer cells, granulocytes, lymphocytes (T cells, B cells, and NK cells), megakaryocytes, osteoclasts, and brown adipocytes.{{cite journal | vauthors = Rosso R, Lucioni M | title = Normal and neoplastic cells of brown adipose tissue express the adhesion molecule CD31 | journal = Archives of Pathology & Laboratory Medicine | volume = 130 | issue = 4 | pages = 480–482 | date = April 2006 | pmid = 16594742 | doi = 10.5858/2006-130-480-NANCOB }}

Image:Epithelioid angiosarcoma - CD31 - intermed mag.jpg of an angiosarcoma stained with a CD31 immunostain (dark brown).]]

In immunohistochemistry, CD31 is used primarily to demonstrate the presence of endothelial cells in histological tissue sections. This can help to evaluate the degree of tumor angiogenesis, which can imply a rapidly growing tumor. Malignant endothelial cells also commonly retain the antigen, so that CD31 immunohistochemistry can also be used to demonstrate both angiomas and angiosarcomas. It can also be demonstrated in small lymphocytic and lymphoblastic lymphomas, although more specific markers are available for these conditions.{{cite book|author=Leong, Anthony S-Y|author2=Cooper, Kumarason|author3=Leong, F Joel W-M|year=2003|title=Manual of Diagnostic Cytology|edition=2|publisher=Greenwich Medical Media, Ltd.|page=103|isbn=978-1-84110-100-2}}

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PECAM-1 is found on the surface of platelets, monocytes, neutrophils, and some types of T-cells, and makes up a large portion of endothelial cell intercellular junctions. The encoded protein is a member of the immunoglobulin superfamily and is likely involved in leukocyte transmigration, angiogenesis, and integrin activation.{{cite web | title = Entrez Gene: platelet/endothelial cell adhesion molecule| url = https://www.ncbi.nlm.nih.gov/sites/entrez?Db=gene&Cmd=ShowDetailView&TermToSearch=5175}} CD31 on endothelial cells binds to the CD38 receptor on natural killer cells for those cells to attach to the endothelium.{{cite journal | vauthors = Zambello R, Barilà G, Manni S, Piazza F, Semenzato G | title = NK cells and CD38: Implication for (Immuno)Therapy in Plasma Cell Dyscrasias | journal = Cells | volume = 9 | issue = 3 | pages = 768 | date = March 2020 | pmid = 32245149 | pmc = 7140687 | doi = 10.3390/cells9030768 | doi-access = free }}{{cite journal | vauthors = Glaría E, Valledor AF | title = Roles of CD38 in the Immune Response to Infection | journal = Cells | volume = 9 | issue = 1 | pages = 228 | date = January 2020 | pmid = 31963337 | pmc = 7017097 | doi = 10.3390/cells9010228 | doi-access = free }}

PECAM-1 plays a role in cell signaling. In the cytoplasmic domain of PECAM-1 are serine and tyrosine residues which are suitable for phosphorylation. After the tyrosine is phosphorylated, PECAM-1 recruits Src homology 2 (SH2) domain–containing signaling proteins. These proteins can then initiate signaling pathways. Of all these proteins, the protein most widely reported as interacting with the PECAM-1 cytoplasmic domain is SH2 domain–containing protein-tyrosine phosphatase SHP-2.{{cite journal | vauthors = Newman PJ, Newman DK | title = Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology | journal = Arteriosclerosis, Thrombosis, and Vascular Biology | volume = 23 | issue = 6 | pages = 953–964 | date = June 2003 | pmid = 12689916 | doi = 10.1161/01.ATV.0000071347.69358.D9 | doi-access = free }} Signaling through PECAM-1 leads to the activation of neutrophils, monocytes and leukocytes.{{cite journal | vauthors = Elias CG, Spellberg JP, Karan-Tamir B, Lin CH, Wang YJ, McKenna PJ, Muller WA, Zukowski MM, Andrew DP | title = Ligation of CD31/PECAM-1 modulates the function of lymphocytes, monocytes and neutrophils | journal = European Journal of Immunology | volume = 28 | issue = 6 | pages = 1948–1958 | date = June 1998 | pmid = 9645377 | doi = 10.1002/(SICI)1521-4141(199806)28:06<1948::AID-IMMU1948>3.0.CO;2-C | s2cid = 32378668 | doi-access = free }}

PECAM-1 is involved in migration of monocytes and neutrophils,{{cite journal | vauthors = Muller WA, Weigl SA, Deng X, Phillips DM | title = PECAM-1 is required for transendothelial migration of leukocytes | journal = The Journal of Experimental Medicine | volume = 178 | issue = 2 | pages = 449–460 | date = August 1993 | pmid = 8340753 | pmc = 2191108 | doi = 10.1084/jem.178.2.449 }} natural killer cells,{{cite journal | vauthors = Berman ME, Xie Y, Muller WA | title = Roles of platelet/endothelial cell adhesion molecule-1 (PECAM-1, CD31) in natural killer cell transendothelial migration and beta 2 integrin activation | journal = Journal of Immunology | volume = 156 | issue = 4 | pages = 1515–1524 | date = February 1996 | doi = 10.4049/jimmunol.156.4.1515 | pmid = 8568255 | s2cid = 1741600 | url = https://pubmed.ncbi.nlm.nih.gov/8568255 }} Vδ1+ γδ T lymphocytes{{cite journal | vauthors = Poggi A, Zocchi MR, Carosio R, Ferrero E, Angelini DF, Galgani S, Caramia MD, Bernardi G, Borsellino G, Battistini L | title = Transendothelial migratory pathways of V delta 1+TCR gamma delta+ and V delta 2+TCR gamma delta+ T lymphocytes from healthy donors and multiple sclerosis patients: involvement of phosphatidylinositol 3 kinase and calcium calmodulin-dependent kinase II | journal = Journal of Immunology | volume = 168 | issue = 12 | pages = 6071–6077 | date = June 2002 | pmid = 12055216 | doi = 10.4049/jimmunol.168.12.6071 | s2cid = 82477153 | doi-access = free }} and CD34+ hematopoietic progenitor cells{{cite journal | vauthors = Voermans C, Rood PM, Hordijk PL, Gerritsen WR, van der Schoot CE | title = Adhesion molecules involved in transendothelial migration of human hematopoietic progenitor cells | journal = Stem Cells | volume = 18 | issue = 6 | pages = 435–443 | date = 2000 | pmid = 11072032 | doi = 10.1634/stemcells.18-6-435 | s2cid = 37713443 | doi-access = free }} through the endothelial cells. Moreover, PECAM-1 is involved in transendothelial migration of recent thymic emigrants to the secondary lymphoid organs.{{cite journal | vauthors = Kimmig S, Przybylski GK, Schmidt CA, Laurisch K, Möwes B, Radbruch A, Thiel A | title = Two subsets of naive T helper cells with distinct T cell receptor excision circle content in human adult peripheral blood | journal = The Journal of Experimental Medicine | volume = 195 | issue = 6 | pages = 789–794 | date = March 2002 | pmid = 11901204 | pmc = 2193736 | doi = 10.1084/jem.20011756 }} Mechanism of leukocyte transmigration can be explained by creating a homophilic interaction. In this interaction migrating leukocytes express PECAM-1 on the surface and then they react with PECAM-1 on the surface of endothelial cell.{{cite journal | vauthors = Mamdouh Z, Chen X, Pierini LM, Maxfield FR, Muller WA | title = Targeted recycling of PECAM from endothelial surface-connected compartments during diapedesis | journal = Nature | volume = 421 | issue = 6924 | pages = 748–753 | date = February 2003 | pmid = 12610627 | doi = 10.1038/nature01300 | bibcode = 2003Natur.421..748M | s2cid = 26318819 }}

PECAM-1 is also important for angiogenesis because it enables the formation of new blood vessels through the cell-cell adhesion.{{cite journal | vauthors = DeLisser HM, Christofidou-Solomidou M, Strieter RM, Burdick MD, Robinson CS, Wexler RS, Kerr JS, Garlanda C, Merwin JR, Madri JA, Albelda SM | title = Involvement of endothelial PECAM-1/CD31 in angiogenesis | journal = The American Journal of Pathology | volume = 151 | issue = 3 | pages = 671–677 | date = September 1997 | pmid = 9284815 | pmc = 1857836 }}

PECAM-1 is expressed by many solid tumor cell lines such as hemangioma, angiosarcoma, Kaposi’s sarcoma, breast carcinoma, glioblastoma, colon carcinoma, skin carcinoma and other tumor cell lines.{{cite journal | vauthors = Bergom C, Gao C, Newman PJ | title = Mechanisms of PECAM-1-mediated cytoprotection and implications for cancer cell survival | journal = Leukemia & Lymphoma | volume = 46 | issue = 10 | pages = 1409–1421 | date = October 2005 | pmid = 16194886 | doi = 10.1080/10428190500126091 | s2cid = 25682089 }} On the surface of these tumor cells PECAM-1 mediates the adhesion to endothelial cells.{{cite journal | vauthors = Tang DG, Chen YQ, Newman PJ, Shi L, Gao X, Diglio CA, Honn KV | title = Identification of PECAM-1 in solid tumor cells and its potential involvement in tumor cell adhesion to endothelium | journal = The Journal of Biological Chemistry | volume = 268 | issue = 30 | pages = 22883–22894 | date = October 1993 | doi = 10.1016/S0021-9258(18)41609-2 | pmid = 8226797 | doi-access = free }} PECAM-1 modulates tumor growth by the formation of new endothelial cell tubes. In mice, this process can be inhibited using an anti-PECAM-1 antibody.{{cite journal | vauthors = Zhou Z, Christofidou-Solomidou M, Garlanda C, DeLisser HM | title = Antibody against murine PECAM-1 inhibits tumor angiogenesis in mice | journal = Angiogenesis | volume = 3 | issue = 2 | pages = 181–188 | date = 1999 | pmid = 14517436 | doi = 10.1023/a:1009092107382 | s2cid = 33204411 }}

Recently, it was found out that elderly patients with gastric cancer have high concentration of PECAM-1 in the serum. That suggests that the use of a serum PECAM-1 level can be a good prognostic marker.{{cite journal | vauthors = Li Y, Guo XB, Wei YH, Kang XL | title = Serum CXCL13 and PECAM-1 can be used as diagnostic and prognostic markers in elderly patients with gastric cancer | journal = Clinical & Translational Oncology | volume = 23 | issue = 1 | pages = 130–138 | date = January 2021 | pmid = 32500259 | doi = 10.1007/s12094-020-02403-w | s2cid = 219313556 }}

Inhibition of PECAM-1 leads to a reduction of atherosclerotic lesions in mice.{{cite journal | vauthors = Stevens HY, Melchior B, Bell KS, Yun S, Yeh JC, Frangos JA | title = PECAM-1 is a critical mediator of atherosclerosis | journal = Disease Models & Mechanisms | volume = 1 | issue = 2–3 | pages = 175–81; discussion 179 | date = September 2008 | pmid = 19048083 | pmc = 2562188 | doi = 10.1242/dmm.000547 }} That means that PECAM-1 is involved in atherosclerosis. The exact mechanism, how PECAM-1 contributes to atherosclerosis is not known, but there are some theories. PECAM-1 can act as a mechanoresponsive molecule. Or the pathogenesis can be caused by the infiltration of leukocytes mediated by PECAM-1. Finally, polymorphisms in the PECAM-1 gene can lead to the progression of atherosclerosis.{{cite journal | vauthors = Woodfin A, Voisin MB, Nourshargh S | title = PECAM-1: a multi-functional molecule in inflammation and vascular biology | journal = Arteriosclerosis, Thrombosis, and Vascular Biology | volume = 27 | issue = 12 | pages = 2514–2523 | date = December 2007 | pmid = 17872453 | doi = 10.1161/ATVBAHA.107.151456 | doi-access = free }}

Extensive microvascular thrombosis and increased microvascular permeability are main characteristics of disseminated intravascular coagulation, a fatal complication of sepsis. Patients with this devastating condition have high levels of PECAM-1 in the serum indicating PECAM-1 as a good diagnostic marker. Moreover, PECAM-1 can protect from the development of disseminated intravascular coagulation by inhibiting macrophage pyroptosis.{{cite journal | vauthors = Luo L, Xu M, Liao D, Deng J, Mei H, Hu Y | title = PECAM-1 protects against DIC by dampening inflammatory responses via inhibiting macrophage pyroptosis and restoring vascular barrier integrity | journal = Translational Research | volume = 222 | pages = 1–16 | date = August 2020 | pmid = 32417429 | doi = 10.1016/j.trsl.2020.04.005 | s2cid = 218678428 }}

PECAM-1 contributes to at least two of the nervous system diseases, multiple sclerosis and cerebral ischaemia. First signs of multiple sclerosis are defects in the blood brain barrier and leukocyte migration mediated by adhesion molecules such as PECAM-1. Moreover, monocytes in patients with multiple sclerosis express high level of PECAM-1. Cerebral ischaemia is caused by the accumulation of leukocytes, which then infiltrate brain parenchyma and release toxic compounds such as oxygen radicals. Interactions between leukocyte and endothelium are mediated by PECAM-1. High levels of soluble PECAM-1 can be used to diagnose both diseases. Increased PECAM-1 levels indicate damage in the blood brain barrier in patients with multiple sclerosis and high PECAM-1 levels can be used as a short-term prediction of a stroke in patients with cerebral ischaemia.{{cite journal | vauthors = Kalinowska A, Losy J | title = PECAM-1, a key player in neuroinflammation | journal = European Journal of Neurology | volume = 13 | issue = 12 | pages = 1284–1290 | date = December 2006 | pmid = 17116209 | doi = 10.1111/j.1468-1331.2006.01640.x | s2cid = 22437957 }}

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• {{cite journal | vauthors = Jackson DE | title = The unfolding tale of PECAM-1 | journal = FEBS Letters | volume = 540 | issue = 1–3 | pages = 7–14 | date = April 2003 | pmid = 12681475 | doi = 10.1016/S0014-5793(03)00224-2 | s2cid = 21470915 | doi-access = }}
• {{cite journal | vauthors = Newman PJ, Newman DK | title = Signal transduction pathways mediated by PECAM-1: new roles for an old molecule in platelet and vascular cell biology | journal = Arteriosclerosis, Thrombosis, and Vascular Biology | volume = 23 | issue = 6 | pages = 953–964 | date = June 2003 | pmid = 12689916 | doi = 10.1161/01.ATV.0000071347.69358.D9 | doi-access = free }}
• {{cite journal | vauthors = Ilan N, Madri JA | title = PECAM-1: old friend, new partners | journal = Current Opinion in Cell Biology | volume = 15 | issue = 5 | pages = 515–524 | date = October 2003 | pmid = 14519385 | doi = 10.1016/S0955-0674(03)00100-5 }}
• {{cite journal | vauthors = Wong MX, Jackson DE | title = Regulation of B cell activation by PECAM-1: implications for the development of autoimmune disorders | journal = Current Pharmaceutical Design | volume = 10 | issue = 2 | pages = 155–161 | year = 2004 | pmid = 14754395 | doi = 10.2174/1381612043453504 }}
• {{cite journal | vauthors = Kalinowska A, Losy J | title = PECAM-1, a key player in neuroinflammation | journal = European Journal of Neurology | volume = 13 | issue = 12 | pages = 1284–1290 | date = December 2006 | pmid = 17116209 | doi = 10.1111/j.1468-1331.2006.01640.x | s2cid = 22437957 }}
• {{cite journal | vauthors = Stockinger H, Gadd SJ, Eher R, Majdic O, Schreiber W, Kasinrerk W, Strass B, Schnabl E, Knapp W | title = Molecular characterization and functional analysis of the leukocyte surface protein CD31 | journal = Journal of Immunology | volume = 145 | issue = 11 | pages = 3889–3897 | date = December 1990 | doi = 10.4049/jimmunol.145.11.3889 | pmid = 1700999 | s2cid = 27015871 | doi-access = free }}
• {{cite journal | vauthors = Albelda SM, Muller WA, Buck CA, Newman PJ | title = Molecular and cellular properties of PECAM-1 (endoCAM/CD31): a novel vascular cell-cell adhesion molecule | journal = The Journal of Cell Biology | volume = 114 | issue = 5 | pages = 1059–1068 | date = September 1991 | pmid = 1874786 | pmc = 2289123 | doi = 10.1083/jcb.114.5.1059 }}
• {{cite journal | vauthors = Simmons DL, Walker C, Power C, Pigott R | title = Molecular cloning of CD31, a putative intercellular adhesion molecule closely related to carcinoembryonic antigen | journal = The Journal of Experimental Medicine | volume = 171 | issue = 6 | pages = 2147–2152 | date = June 1990 | pmid = 2351935 | pmc = 2187965 | doi = 10.1084/jem.171.6.2147 }}
• {{cite journal | vauthors = Kirschbaum NE, Gumina RJ, Newman PJ | title = Organization of the gene for human platelet/endothelial cell adhesion molecule-1 shows alternatively spliced isoforms and a functionally complex cytoplasmic domain | journal = Blood | volume = 84 | issue = 12 | pages = 4028–4037 | date = December 1994 | pmid = 7994021 | doi = 10.1182/blood.V84.12.4028.bloodjournal84124028 | doi-access = free }}
• {{cite journal | vauthors = Tang DG, Chen YQ, Newman PJ, Shi L, Gao X, Diglio CA, Honn KV | title = Identification of PECAM-1 in solid tumor cells and its potential involvement in tumor cell adhesion to endothelium | journal = The Journal of Biological Chemistry | volume = 268 | issue = 30 | pages = 22883–22894 | date = October 1993 | pmid = 8226797 | doi = 10.1016/S0021-9258(18)41609-2 | doi-access = free }}
• {{cite journal | vauthors = Behar E, Chao NJ, Hiraki DD, Krishnaswamy S, Brown BW, Zehnder JL, Grumet FC | title = Polymorphism of adhesion molecule CD31 and its role in acute graft-versus-host disease | journal = The New England Journal of Medicine | volume = 334 | issue = 5 | pages = 286–291 | date = February 1996 | pmid = 8532023 | doi = 10.1056/NEJM199602013340502 | doi-access = free }}
• {{cite journal | vauthors = Lu TT, Yan LG, Madri JA | title = Integrin engagement mediates tyrosine dephosphorylation on platelet-endothelial cell adhesion molecule 1 | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 93 | issue = 21 | pages = 11808–11813 | date = October 1996 | pmid = 8876219 | pmc = 38140 | doi = 10.1073/pnas.93.21.11808 | doi-access = free | bibcode = 1996PNAS...9311808L }}
• {{cite journal | vauthors = Almendro N, Bellón T, Rius C, Lastres P, Langa C, Corbí A, Bernabéu C | title = Cloning of the human platelet endothelial cell adhesion molecule-1 promoter and its tissue-specific expression. Structural and functional characterization | journal = Journal of Immunology | volume = 157 | issue = 12 | pages = 5411–5421 | date = December 1996 | doi = 10.4049/jimmunol.157.12.5411 | pmid = 8955189 | s2cid = 6694530 | doi-access = free }}
• {{cite journal | vauthors = Jackson DE, Ward CM, Wang R, Newman PJ | title = The protein-tyrosine phosphatase SHP-2 binds platelet/endothelial cell adhesion molecule-1 (PECAM-1) and forms a distinct signaling complex during platelet aggregation. Evidence for a mechanistic link between PECAM-1- and integrin-mediated cellular signaling | journal = The Journal of Biological Chemistry | volume = 272 | issue = 11 | pages = 6986–6993 | date = March 1997 | pmid = 9054388 | doi = 10.1074/jbc.272.11.6986 | doi-access = free }}
• {{cite journal | vauthors = Famiglietti J, Sun J, DeLisser HM, Albelda SM | title = Tyrosine residue in exon 14 of the cytoplasmic domain of platelet endothelial cell adhesion molecule-1 (PECAM-1/CD31) regulates ligand binding specificity | journal = The Journal of Cell Biology | volume = 138 | issue = 6 | pages = 1425–1435 | date = September 1997 | pmid = 9298995 | pmc = 2132561 | doi = 10.1083/jcb.138.6.1425 }}
• {{cite journal | vauthors = Deaglio S, Morra M, Mallone R, Ausiello CM, Prager E, Garbarino G, Dianzani U, Stockinger H, Malavasi F | title = Human CD38 (ADP-ribosyl cyclase) is a counter-receptor of CD31, an Ig superfamily member | journal = Journal of Immunology | volume = 160 | issue = 1 | pages = 395–402 | date = January 1998 | doi = 10.4049/jimmunol.160.1.395 | pmid = 9551996 | s2cid = 15132619 | url = http://www.jimmunol.org/content/160/1/395.full | doi-access = free }}
• {{cite journal | vauthors = Coukos G, Makrigiannakis A, Amin K, Albelda SM, Coutifaris C | title = Platelet-endothelial cell adhesion molecule-1 is expressed by a subpopulation of human trophoblasts: a possible mechanism for trophoblast-endothelial interaction during haemochorial placentation | journal = Molecular Human Reproduction | volume = 4 | issue = 4 | pages = 357–367 | date = April 1998 | pmid = 9620836 | doi = 10.1093/molehr/4.4.357 | doi-access = free }}
• {{cite journal | vauthors = Cao MY, Huber M, Beauchemin N, Famiglietti J, Albelda SM, Veillette A | title = Regulation of mouse PECAM-1 tyrosine phosphorylation by the Src and Csk families of protein-tyrosine kinases | journal = The Journal of Biological Chemistry | volume = 273 | issue = 25 | pages = 15765–15772 | date = June 1998 | pmid = 9624175 | doi = 10.1074/jbc.273.25.15765 | doi-access = free}}
• {{cite journal | vauthors = Ma L, Mauro C, Cornish GH, Chai JG, Coe D, Fu H, Patton D, Okkenhaug K, Franzoso G, Dyson J, Nourshargh S, Marelli-Berg FM | title = Ig gene-like molecule CD31 plays a nonredundant role in the regulation of T-cell immunity and tolerance | journal = Proceedings of the National Academy of Sciences of the United States of America | volume = 107 | issue = 45 | pages = 19461–19466 | date = November 2010 | pmid = 20978210 | pmc = 2984185 | doi = 10.1073/pnas.1011748107 | doi-access = free | bibcode = 2010PNAS..10719461M }}

{{refend}}

• [http://us.ebioscience.com/resources/human-cd-chart.htm Human CD Antigen Chart (eBioscience)]
• [http://us.ebioscience.com/resources/mouse-cd-chart.htm Mouse CD Antigen Chart (eBioscience)]
• {{UCSC gene info|PECAM1}}
• {{PDBe-KB2|P16284|Platelet endothelial cell adhesion molecule}}

{{Clusters of differentiation}}

{{Cell adhesion molecules}}

{{Clusters of differentiation by lineage}}

Category:Clusters of differentiation