Alternative titles; symbols
HGNC Approved Gene Symbol: ITGB1
Cytogenetic location: 10p11.22 Genomic coordinates (GRCh38): 10:32,900,318-32,958,230 (from NCBI)
Fibronectin receptors contain a beta subunit that appears to be analogous to band-3 of integrin (Pytela et al., 1986; Johansson et al., 1987). Hynes (1987) proposed that there are 3 subfamilies within the family of human adhesion protein receptor heterodimers based upon the number of different beta subunits. The other 2 subfamilies are the platelet and the endothelial cell heterodimers, which use GP IIIa (ITGB3; 173470), and the leukocyte heterodimers, which contain a 95,000 Da beta subunit that is homologous to GP IIIa but is clearly a different protein (ITGB2; 600065).
Zhang et al. (1988) examined human-mouse hybrid cells by indirect immunofluorescence with a monoclonal antibody that recognizes the beta subunit of the human fibronectin receptor. Cells that expressed the antigen at their surface were sorted by FACS and karyotyped. The findings, strengthened by isozyme analysis of markers for chromosomes 9 and 10, suggested that the beta subunit is located on chromosome 10p. Since the gene encoding the beta subunit of the very late activation (VLA) proteins was previously assigned to the same chromosome (Peters et al., 1984), the results provided further evidence for a relationship between the beta subunit of the human fibronectin receptor and the VLA protein family (see ITGA2; 192974).
By Southern blot analysis of mouse/human somatic cell hybrid DNAs and by in situ hybridization, Goodfellow et al. (1989) mapped the FNRB gene to 10p11.2. A monoclonal antibody that recognizes the protein on the cell surface was used to confirm that the sequences present on chromosome 10 correspond to those required for expression of the gene. The location of the gene in the pericentromeric region of chromosome 10 was confirmed by Wu et al. (1989) using RFLPs mapping in that region.
Pseudogenes
Giuffra et al. (1989) described an FNRB-like sequence on chromosome 19 which is probably nonfunctional. The gene, designated FNRBL, shows RFLPs which could be used in corroborating the assignment to chromosome 19. Giuffra et al. (1990) found that a cDNA clone of the beta subunit of human fibronectin receptor not only detected the functional gene which maps to 10p11.2 but also identified a presence/absence polymorphism which, by linkage analysis and biotin-labeled in situ hybridization, mapped to proximal 19p. Giuffra et al. (1990) suggested that the polymorphism is due to the presence or absence of an insertion in chromosome 19 of a 3-prime segment of the FNRB gene. Since some persons do not have the polymorphism, it is unlikely to be functional; it is not a full-length pseudogene since the 5-prime portion of the FNRB gene is not represented. The polymorphism was found in all populations studied, which included Pygmies, Japanese, Druze, Cambodians, Mayans, Chinese, and western Europeans. The polymorphism may be similar to the one reported for one of the DHFR pseudogenes (see 126060).
Arregui et al. (2000) demonstrated that cell-permeable (Trojan) peptides containing the third helix of the antennapedia homeodomain fused to a peptide mimicking the juxtamembrane (JMP) region of the cytoplasmic domain of N-cadherin (CDH2; 114020) result in the inhibition of both CDH2 and ITGB1 function. Microscopic analysis showed that expression of JMP, which binds to the cytoplasmic domain of CDH2, results in a reduction of neurite outgrowth on cadherin substrates. Treatment of cells with JMP resulted in the release of FER (176942) from the cadherin complex and its accumulation in the integrin complex. The accumulation of FER in the integrin complex and the inhibitory effects of JMP could be reversed with a peptide that mimics the first coiled-coil domain of FER. The results suggested that FER mediates crosstalk between CDH2 and ITGB1.
Human herpesvirus-8 (HHV-8) is implicated in the pathogenesis of Kaposi sarcoma. HHV-8 envelope glycoprotein B possesses the RGD amino acid motif known to interact with integrin molecules. Akula et al. (2002) found that HHV-8 infectivity was inhibited by RGD peptides, antibodies against the RGD-dependent integrins ITGA3 (605025) and ITGB1, and by soluble ITGA3/ITGB1. Expression of human ITGA3 increased the infectivity of virus for Chinese hamster ovary cells. Anti-glycoprotein B antibodies immunoprecipitated the virus-ITGA3 and -ITGB1 complexes, and virus-binding studies suggested a role for ITGA3/ITGB1 in HHV-8 entry. Further, HHV-8 infection induced the integrin-mediated activation of focal adhesion kinase (FAK; 600758). These findings implicated a role for ITGA3/ITGB1 and the associated signaling pathways in HHV-8 entry into target cells.
Lu and Cyster (2002) studied the mechanisms that control localization of marginal zone B cells. They demonstrated that marginal zone B cells express elevated levels of the integrins LFA1 (see 153370) and alpha-4 (192975)-beta-1, and that the marginal zone B cells bind to the ligands ICAM1 (147840) and VCAM1 (192225). These ligands are expressed within the marginal zone in a lymphotoxin-dependent manner. Combined inhibition of LFA1 and alpha-4-beta-1 causes a rapid and selective release of B cells from the marginal zone. Furthermore, lipopolysaccharide-triggered marginal zone B cell relocalization involves downregulation of integrin-mediated adhesion. Lu and Cyster (2002) concluded that their studies identified key requirements for marginal zone B cell localization and established a role for integrins in peripheral lymphoid tissue compartmentalization.
By examining the cation dependence of JAM2 (606870) adhesion to a T-cell line, Cunningham et al. (2002) identified a manganese-enhanced binding component indicative of integrin involvement. Using neutralizing integrin antibodies, they showed that the manganese-enhanced binding component was due to an interaction between JAM2 and ITGA4/ITGB1. However, the interaction was only enabled following prior adhesion of JAM2 to JAM3 (606871). Cunningham et al. (2002) determined that the engagement of all these ligands occurs through a nonacidic residue in an Ig-like fold of JAM2. An inhibitor of ITGA4, TBC772, attenuated the manganese-enhanced binding.
Dulabon et al. (2000) showed through immunoprecipitation experiments that alpha-3-beta-1 integrin associates with reelin (RELN; 600514) in mouse embryonic brain. Using immunolabeling, they detected coexpression of alpha-3-beta-1 integrin with Dab1 (603448), a signaling protein acting downstream of reelin, in embryonic cortical neurons. In cerebral cortices of alpha-3-beta-1 integrin-deficient mice, Dulabon et al. (2000) observed reduced levels of Dab1 protein and elevated expression of a reelin fragment. They concluded that reelin may regulate neuronal migration and layer formation through modulation of alpha-3-beta-1 integrin-mediated neuronal adhesion and migration.
In a patient with features of Glanzmann thrombasthenia (see 173470) and leukocyte adhesion deficiency-1 (116920), McDowall et al. (2003) identified a novel form of integrin dysfunction involving ITGB1, ITGB2 (600065), and ITGB3 (173470). ITGB2 and ITGB3 were constitutively clustered. Although all 3 integrins were expressed on the cell surface at normal levels and were capable of function following extracellular stimulation, they could not be activated via the 'inside-out' signaling pathways.
Tadokoro et al. (2003) reported that specific binding of the cytoskeletal protein talin (186745) to integrin beta subunit cytoplasmic tails leads to the conformational rearrangements of integrin extracellular domains that increase their affinity. They found that regulated binding of talin to integrin beta tails is a final common element of cellular signaling cascades that control integrin activation.
Inoue et al. (2003) identified a collagen (see COL1A1; 120150) peptide that bound exclusively to alpha-2 (192974)-beta-1 integrin and generated tyrosine kinase-based intracellular signaling during spreading of human platelets on collagen-coated surfaces. Murine platelets deficient in Gp6 (605546)-Fc receptor gamma chain (FCERIG; 147139) showed a similar response to the collagen peptide. Both responses were inhibited by alpha-2-beta-1 blockade. The intracellular signaling cascade used by alpha-2-beta-1 shared many features of GP6 signaling, including participation of Src kinases (see 190090) and phospholipase C gamma-2 (PLCG2; 600220). Inoue et al. (2003) concluded that alpha-2-beta-1 has a role in platelet activation by collagen and in control of thrombus formation.
Garmy-Susini et al. (2005) demonstrated that integrin alpha-4-beta-1 and its ligand VCAM1 are expressed by proliferating but not quiescent endothelial cells and mural cells, respectively. Antagonists of this integrin-ligand pair blocked the adhesion of mural cells to proliferating endothelia in vitro and in vivo, thereby inducing apoptosis of endothelial cells and pericytes and inhibiting neovascularization. Garmy-Susini et al. (2005) concluded that integrin alpha-4-beta-1 and VCAM1 facilitate a critical cell-cell adhesion event required for survival of endothelial and mural cells during vascularization.
Suzuki et al. (2007) demonstrated that semaphorin 7A (SEMA7A; 607961), which is expressed on activated T cells, stimulates cytokine production in monocytes and macrophages through alpha-1-beta-1 integrin (also known as very late antigen-1) as a component of the immunologic synapse, and is critical for the effector phase of the inflammatory immune response. Sema7A-null mice are defective in cell-mediated immune responses such as contact hypersensitivity and experimental autoimmune encephalomyelitis. Although antigen-specific and cytokine-producing effector T cells could develop and migrate into antigen-challenged sites in Sema7a-null mice, Sema7a-null T cells failed to induce contact hypersensitivity even when directly injected into the antigen-challenged sites. Thus, Suzuki et al. (2007) concluded that the interaction between SEMA7A and alpha-1-beta-1 integrin is crucial at the site of inflammation.
Kwok et al. (2007) found that the Helicobacter pylori (see 600263) adhesin protein CagL was targeted to the bacterial type IV secretion pilus surface, where it bound and activated the ITGA5 (135620)/ITGB1 receptor on gastric epithelial cells through its arg-gly-asp motif. CagL interaction with the integrin receptor triggered delivery of the H. pylori oncoprotein CagA into target cells and activation of FAK and SRC tyrosine kinases. Kwok et al. (2007) suggested that CagL may be used as a molecular tool to better understand integrin signaling and the mechanism by which H. pylori causes gastric ulcer and cancer.
Conrad et al. (2007) showed that blocking the interaction of alpha-1-beta-1 integrin (VLA-1) with collagen prevented accumulation of epidermal T cells and immunopathology of psoriasis (177900). Alpha-1-beta-1 integrin, a major collagen-binding surface receptor, was exclusively expressed by epidermal but not dermal T cells. Alpha-1-beta-1-positive T cells showed characteristic surface markers of effector memory cells and contained high levels of interferon-gamma (147570) but not interleukin-4 (147780). Blockade of alpha-1-beta-1 inhibited migration of T cells into the epidermis in a clinically relevant xenotransplantation model. This was paralleled by a complete inhibition of psoriasis development, comparable to that caused by tumor necrosis factor-alpha (TNFA; 191160) blockers. Conrad et al. (2007) concluded that their results defined a crucial role for alpha-1-beta-1 in controlling the accumulation of epidermal type 1 polarized effector memory T cells in a common human immunopathology and provided the basis for new strategies in psoriasis treatment focusing on T cell-extracellular matrix interactions.
Staniszewska et al. (2007) identified human thrombospondin-1 (THBS1; 188060) as a ligand for alpha-9 (ITGA9; 603963)/beta-1 integrin, and they identified an integrin-binding site within the N-terminal domain (NTD) of THBS1. Binding of the NTD to human dermal microvascular endothelial cells expressing alpha-9/beta-1 integrin activated signaling proteins such as ERK1 (MAPK3; 601795)/ERK2 (MAPK1; 176948) and paxillin (PXN; 602505). Blocking alpha-9/beta-1 integrin by monoclonal antibody or snake venom disintegrin inhibited cell proliferation and NTD-induced cell migration. The THBS1 NTD also induced neovascularization in animal model systems, and this proangiogenic activity was inhibited by alpha-9/beta-1 inhibitors.
Lammermann et al. (2008) studied the interplay between adhesive, contractile, and protrusive forces during interstitial leukocyte chemotaxis in vivo and in vitro. The authors ablated genes encoding integrin heterodimeric partners ITGA5 (135620), ITGB1, ITGB2 (600065), and ITGB7 (147559) from murine leukocytes and demonstrated that functional integrins do not contribute to migration in 3-dimensional environments. Instead, these cells migrate by the sole force of actin network expansion, which promotes protrusive flowing of the leading edge. Myosin II (see 160776)-dependent contraction is required only on passage through narrow gaps, where a squeezing contraction of the trailing edge propels the rigid nucleus.
Friedland et al. (2009) showed that the alpha-5/beta-1 integrin switches between relaxed and tensioned states in response to myosin II-generated cytoskeletal force. Force combines with extracellular matrix stiffness to generate tension that triggers the integrin switch. This switch directly controls the alpha-5/beta-1-fibronectin bond strength through engaging the synergy site in fibronectin and is required to generate signals through phosphorylation of focal adhesion kinase. In the context of tissues, this integrin switch connects cytoskeleton and extracellular matrix mechanics to adhesion-dependent motility and signaling pathways.
Using short interfering RNA, Renz et al. (2015) found that silencing CCM2 (607929) elevated expression of KLF2 (602016) mRNA in human umbilical vein endothelial cells. Elevated expression of KLF2 in CCM2-knockdown cells required activation of cell surface beta-1 integrin.
Lorenz et al. (2018) used the developing liver as a model organ to study angiocrine signals and showed that the growth rate of the liver correlates both spatially and temporally with blood perfusion to this organ. By manipulating blood flow through the liver vasculature, Lorenz et al. (2018) demonstrated that vessel perfusion activates beta-1 integrin and VEGFR3 (136352). Notably, both beta-1 integrin and VEGFR3 are strictly required for normal production of hepatocyte growth factor, survival of hepatocytes, and liver growth. Ex vivo perfusion of adult mouse liver and in vitro mechanical stretching of human hepatic endothelial cells illustrated that mechanotransduction alone is sufficient to turn on angiocrine signals. When the endothelial cells are mechanically stretched, angiocrine signals trigger in vitro proliferation and survival of primary human hepatocytes. Lorenz et al. (2018) concluded that their findings uncovered a signaling pathway in vascular endothelial cells that translates blood perfusion and mechanotransduction into organ growth and maintenance.
Graus-Porta et al. (2001) used Cre/lox-mediated recombination to generate mice with an Itgb1-null allele in the precursors of neurons and glia, thereby inactivating all beta-1-class integrin receptors in the nervous system. The mice died prematurely after birth with severe brain malformations. Using histologic sections of brains at varying ages, Graus-Porta et al. (2001) observed that cortical hemispheres and cerebellar folia fuse, and cortical laminae are perturbed in the knockout mice. These defects result from disorganization of the cortical marginal zone, where Graus-Porta et al. (2001) hypothesized that beta-1-class integrins regulate glial endfeet anchorage, meningeal basement membrane remodeling, and formation of the Cajal-Retzius cell layer. Graus-Porta et al. (2001) concluded that beta-1-class integrins are not essential for neuron-glia interactions and neuronal migration during corticogenesis. They noted that the phenotype of the beta-1-deficient mice resembles pathologic changes observed in human cortical dysplasias, suggesting that defective integrin-mediated signal transduction contributes to the development of some of these diseases.
Feltri et al. (2002) found that mice with Schwann cell-specific disruption of the Itgb1 gene had severe neuropathy with impaired radial sorting of axons. Itgb1-null Schwann cells populated nerves, proliferated, and survived normally, but they did not extend or maintain normal processes around axons. Some Schwann cells developed normal myelin, possibly due to the presence of other laminin receptors.
Aszodi et al. (2003) created mutant mice with a conditionally inactivated Itgb1 gene in chondrocytes. Mutant mice developed a chondrodysplasia of various severity. Itgb1-deficient chondrocytes had an abnormal shape and failed to arrange into columns in the growth plate. The lack of motility was due to loss of adhesion to collagen type II (120140), reduced binding to and impaired spreading on fibronectin (135600), and abnormal F-actin (see 102610) organization. In addition, mutant chondrocytes showed decreased proliferation due to a defect in G1/S transition and cytokinesis. The G1/S defect was associated with overexpression of Fgfr3 (134934), nuclear translocation of Stat1 (600555)/Stat5a (601511), and upregulation of the cell cycle inhibitors p16 (CDKN2A; 600160) and p21 (116899). Aszodi et al. (2003) concluded that ITGB1-dependent motility and proliferation of chondrocytes are mandatory for endochondral bone formation.
Naylor et al. (2005) conditionally deleted Itgb1 in mouse mammary luminal epithelia. Loss of Igb1 impaired alveologenesis and lactation, and mutant cells displayed abnormal focal adhesion and signal transduction and could not form or maintain polarized acini. Mutant cells did not differentiate in response to prolactin (PRL; 176760) due to defective Stat5 activation. Since fewer alveolar defects were seen if Itgb1 was deleted after initiation of mammary differentiation, Naylor et al. (2005) concluded that ITGB1 has a permissive role in prolactin signaling.
DiPersio et al. (1997) studied the skin of integrin alpha-3/beta-1-deficient mice generated by null mutation of the alpha-3 subunit. Immunofluorescence and electron microscopy of alpha-3/beta-1-deficient skin revealed regions of disorganized basement membrane, which first appeared on embryonic day 15.5 and became progressively more extensive. In neonatal skin, matrix disorganization was frequently accompanied by blistering at the dermal-epidermal junction due to rupture of the basement membrane. In culture, alpha-3/beta-1-deficient keratinocytes spread poorly on laminin-5 (see 600805) compared with wildtype, demonstrating a postattachment requirement for alpha-3/beta-1.
Using zebrafish mutants and morpholino-mediated knockdown of genes in zebrafish embryos, Renz et al. (2015) identified a proangiogenic signaling pathway that involved activation of beta-1 integrin, followed by elevated expression of klf2a, klf2b, egfl7 (608582), and vegf (VEGFA; 192240). Ccm2 negatively regulated this pathway. Loss of ccm2 elevated expression of several genes related to angiogenesis, including klf2a and klf2b, and resulted in significant cardiovascular malformations. These defects occurred in the absence of blood flow and did not require mir126a or mir126b (see 611767), the latter of which is located within the egfl7 gene. Knockdown of beta-1 integrin reversed the cardiovascular defects in ccm2 mutant embryos. Knockout of Ccm2 in mice also resulted in elevated Klf2 expression and cardiovascular defects. Renz et al. (2015) concluded that the beta-1 integrin-KLF2-EGFL7 pathway is tightly regulated by CCM2 and that this regulation prevents angiogenic overgrowth and ensures quiescence in endothelial cells.
Akula, S. M., Pramod, N. P., Wang, F.-Z., Chandran, B. Integrin alpha-3/beta-1 (CD 49c/29) is a cellular receptor for Kaposi's sarcoma-associated herpesvirus (KSHV/HHV-8) entry into the target cells. Cell 108: 407-419, 2002. [PubMed: 11853674] [Full Text: https://doi.org/10.1016/s0092-8674(02)00628-1]
Arregui, C., Pathre, P., Lilien, J., Balsamo, J. The nonreceptor tyrosine kinase Fer mediates cross-talk between N-cadherin and beta-1-integrins. J. Cell Biol. 149: 1263-1273, 2000. [PubMed: 10851023] [Full Text: https://doi.org/10.1083/jcb.149.6.1263]
Aszodi, A., Hunziker, E. B., Brakebusch, C., Fassler, R. Beta-1 integrins regulate chondrocyte rotation, G1 progression, and cytokinesis. Genes Dev. 17: 2465-2479, 2003. [PubMed: 14522949] [Full Text: https://doi.org/10.1101/gad.277003]
Conrad, C., Boyman, O., Tonel, G., Tun-Kyi, A., Laggner, U., de Fougerolles, A., Kotelianski, V., Gardner, H., Nestle, F. O. Alpha-1-beta-1 integrin is crucial for accumulation of epidermal T cells and the development of psoriasis. Nature Med. 13: 836-841, 2007. [PubMed: 17603494] [Full Text: https://doi.org/10.1038/nm1605]
Cunningham, S. A., Rodriguez, J. M., Arrate, M. P., Tran, T. M., Brock, T. A. JAM2 interacts with alpha-4/beta-1: facilitation by JAM3. J. Biol. Chem. 277: 27589-27592, 2002. [PubMed: 12070135] [Full Text: https://doi.org/10.1074/jbc.C200331200]
DiPersio, C. M., Hodivala-Dilke, K. M., Jaenisch, R., Kreidberg, J. A., Hynes, R. O. Alpha-3-beta-1 integrin is required for normal development of the epidermal basement membrane. J. Cell Biol. 137: 729-742, 1997. [PubMed: 9151677] [Full Text: https://doi.org/10.1083/jcb.137.3.729]
Dulabon, L., Olson, E. C., Taglienti, M. G., Eisenhuth, S., McGrath, B., Walsh, C. A., Kreidberg, J. A., Anton, E. S. Reelin binds alpha-3-beta-1 integrin and inhibits neuronal migration. Neuron 27: 33-44, 2000. [PubMed: 10939329] [Full Text: https://doi.org/10.1016/s0896-6273(00)00007-6]
Feltri, M. L., Graus Porta, D., Previtali, S. C., Nodari, A., Migliavacca, B., Cassetti, A., Littlewood-Evans, A., Reichardt, L. F., Messing, A., Quattrini, A., Mueller, U., Wrabetz, L. Conditional disruption of beta-1 integrin in Schwann cells impedes interactions with axons. J. Cell Biol. 156: 199-209, 2002. [PubMed: 11777940] [Full Text: https://doi.org/10.1083/jcb.200109021]
Friedland, J. C., Lee, M. H., Boettiger, D. Mechanically activated integrin switch controls alpha-5/beta-1 function. Science 323: 642-644, 2009. [PubMed: 19179533] [Full Text: https://doi.org/10.1126/science.1168441]
Garmy-Susini, B., Jin, H., Zhu, Y., Sung, R.-J., Hwang, R., Varner, J. Integrin alpha-4-beta-1--VCAM-1--mediated adhesion between endothelial and mural cells is required for blood vessel maturation. J. Clin. Invest. 115: 1542-1551, 2005. [PubMed: 15902308] [Full Text: https://doi.org/10.1172/JCI23445]
Giuffra, L. A., Lichter, P., Wu, J., Kennedy, J. L., Pakstis, A. J., Rogers, J., Kidd, J. R., Harley, H., Jenkins, T., Ward, D. C., Kidd, K. K. Genetic and physical mapping and population studies of a fibronectin receptor beta-subunit-like sequence on human chromosome 19. Genomics 8: 340-346, 1990. [PubMed: 1979054] [Full Text: https://doi.org/10.1016/0888-7543(90)90291-2]
Giuffra, L. A., Wu, J., Lichter, P., Kennedy, J. L., Castiglione, C., Pakstis, A. J., Ward, D., Kidd, K. K. Mapping of a fibronectin receptor beta subunit-like sequence to chromosome 19. (Abstract) Am. J. Hum. Genet. 45 (suppl.): A141 only, 1989.
Goodfellow, P. J., Nevanlinna, H. A., Gorman, P., Sheer, D., Lam, G., Goodfellow, P. N. Assignment of the gene encoding the beta-subunit of the human fibronectin receptor (beta-FNR) to chromosome 10p11.2. Ann. Hum. Genet. 53: 15-22, 1989. [PubMed: 2524991] [Full Text: https://doi.org/10.1111/j.1469-1809.1989.tb01118.x]
Graus-Porta, D., Blaess, S., Senften, M., Littlewood-Evans, A., Damsky, C., Huang, Z., Orban, P., Klein, R., Schittny, J. C., Muller, U. Beta-1-class integrins regulate the development of laminae and folia in the cerebral and cerebellar cortex. Neuron 31: 367-379, 2001. [PubMed: 11516395] [Full Text: https://doi.org/10.1016/s0896-6273(01)00374-9]
Hynes, R. O. Integrins: a family of cell surface receptors. Cell 48: 549-554, 1987. [PubMed: 3028640] [Full Text: https://doi.org/10.1016/0092-8674(87)90233-9]
Inoue, O., Suzuki-Inoue, K., Dean, W. L., Frampton, J., Watson, S. P. Integrin alpha-2-beta-1 mediates outside-in regulation of platelet spreading on collagen through activation of Src kinases and PLC-gamma-2. J. Cell Biol. 160: 769-780, 2003. [PubMed: 12615912] [Full Text: https://doi.org/10.1083/jcb.200208043]
Johansson, S., Forsberg, E., Lundgren, B. Comparison of fibronectin receptors from rat hepatocytes and fibroblasts. J. Biol. Chem. 262: 7819-7824, 1987. [PubMed: 2953726]
Kwok, T., Zabler, D., Urman, S., Rohde, M., Hartig, R., Wessler, S., Misselwitz, R., Berger, J., Sewald, N., Konig, W., Backert, S. Helicobacter exploits integrin for type IV secretion and kinase activation. Nature 449: 862-866, 2007. [PubMed: 17943123] [Full Text: https://doi.org/10.1038/nature06187]
Lammermann, T., Bader, B. L., Monkley, S. J., Worbs, T., Wedlich-Soldner, R., Hirsch, K., Keller, M., Forster, R., Critchley, D. R., Fassler, R., Sixt, M. Rapid leukocyte migration by integrin-independent flowing and squeezing. Nature 453: 51-55, 2008. [PubMed: 18451854] [Full Text: https://doi.org/10.1038/nature06887]
Lorenz, L., Axnick, J., Buschmann, T., Henning, C., Urner, S., Fang, S., Nurmi, H., Eichhorst, N., Holtmeier, R., Bodis, K., Hwang, J.-H., Mussig, K., Eberhard, D., Stypmann, J., Kuss, O., Roden, M., Alitalo, K., Haussinger, D., Lammert, E. Mechanosensing by beta-1 integrin induces angiocrine signals for liver growth and survival. Nature 562: 128-132, 2018. [PubMed: 30258227] [Full Text: https://doi.org/10.1038/s41586-018-0522-3]
Lu, T. T., Cyster, J. G. Integrin-mediated long-term B cell retention in the splenic marginal zone. Science 297: 409-412, 2002. [PubMed: 12130787] [Full Text: https://doi.org/10.1126/science.1071632]
McDowall, A., Inwald, D., Leitinger, B., Jones, A., Liesner, R., Klein, N., Hogg, N. A novel form of integrin dysfunction involving beta-1, beta-2, and beta-3 integrins. J. Clin. Invest. 111: 51-60, 2003. [PubMed: 12511588] [Full Text: https://doi.org/10.1172/JCI14076]
Naylor, M. J., Li, N., Cheung, J., Lowe, E. T., Lambert, E., Marlow, R., Wang, P., Schatzmann, F., Wintermantel, T., Schuetz, G., Clarke, A. R., Mueller, U., Hynes, N. E., Streuli, C. H. Ablation of beta-1 integrin in mammary epithelium reveals a key role for integrin in glandular morphogenesis and differentiation. J. Cell Biol. 171: 717-728, 2005. [PubMed: 16301336] [Full Text: https://doi.org/10.1083/jcb.200503144]
Peters, P. M., Kamarck, M. E., Hemler, M. E., Strominger, J. L., Ruddle, F. H. Genetic and biochemical characterization of human lymphocyte cell surface antigens: the A-1A5 and A-3A4 determinants. J. Exp. Med. 159: 1441-1454, 1984. [PubMed: 6201585] [Full Text: https://doi.org/10.1084/jem.159.5.1441]
Pytela, R., Pierschbacher, M. D., Ginsberg, M. H., Plow, E. F., Ruoslahti, E. Platelet membrane glycoprotein IIb/IIIa: member of a family of arg-gly-asp-specific adhesion receptors. Science 231: 1559-1562, 1986. [PubMed: 2420006] [Full Text: https://doi.org/10.1126/science.2420006]
Renz, M., Otten, C., Faurobert, E., Rudolph, F., Zhu, Y., Boulday, G., Duchene, J., Mickoleit, M., Dietrich, A.-C., Ramspacher, C., Steed, E., Manet-Dupe, S., and 9 others. Regulation of beta-1 integrin-Klf2-mediated angiogenesis by CCM proteins. Dev. Cell 32: 181-190, 2015. [PubMed: 25625207] [Full Text: https://doi.org/10.1016/j.devcel.2014.12.016]
Staniszewska, I., Zaveri, S., Del Valle, L., Oliva, I., Rothman, V. L., Croul, S. E., Roberts, D. D., Mosher, D. F., Tuszynski, G. P., Marcinkiewicz, C. Interaction of alpha-9/beta-1 integrin with thrombospondin-1 promotes angiogenesis. Circ. Res. 100: 1308-1316, 2007. [PubMed: 17413041] [Full Text: https://doi.org/10.1161/01.RES.0000266662.98355.66]
Suzuki, K., Okuno, T., Yamamoto, M., Pasterkamp, R. J., Takegahara, N., Takamatsu, H., Kitao, T., Takagi, J., Rennert, P. D., Kolodkin, A. L., Kumanogoh, A., Kikutani, H. Semaphorin 7A initiates T-cell-mediated inflammatory responses through alpha-1-beta-1 integrin. Nature 446: 680-684, 2007. [PubMed: 17377534] [Full Text: https://doi.org/10.1038/nature05652]
Tadokoro, S., Shattil, S. J., Eto, K., Tai, V., Liddington, R. C., de Pereda, J. M., Ginsberg, M. H., Calderwood, D. A. Talin binding to integrin beta tails: a final common step in integrin activation. Science 302: 103-106, 2003. [PubMed: 14526080] [Full Text: https://doi.org/10.1126/science.1086652]
Woods, V. L., Jr., Pischel, K. D., Avery, E. D., Bluestein, H. G. Antigenic polymorphism of human very late activation protein-2 (platelet glycoprotein Ia-IIa): platelet alloantigen Hc(a). J. Clin. Invest. 83: 978-985, 1989. [PubMed: 2646323] [Full Text: https://doi.org/10.1172/JCI113984]
Wu, J. S., Giuffra, L. A., Goodfellow, P. J., Myers, S., Carson, N. L., Anderson, L., Hoyle, L. S., Simpson, N. E., Kidd, K. K. The beta subunit locus of the human fibronectin receptor: DNA restriction fragment length polymorphism and linkage mapping studies. Hum. Genet. 83: 383-390, 1989. [PubMed: 2572537] [Full Text: https://doi.org/10.1007/BF00291386]
Zhang, Y., Saison, M., Spaepen, M., De Strooper, B., Van Leuven, F., David, G., Van den Berghe, H., Cassiman, J.-J. Mapping of human fibronectin receptor beta subunit gene to chromosome 10. Somat. Cell Molec. Genet. 14: 99-104, 1988. [PubMed: 2963381] [Full Text: https://doi.org/10.1007/BF01535053]