Alternative titles; symbols
Other entities represented in this entry:
HGNC Approved Gene Symbol: GP1BA
SNOMEDCT: 128105004, 128115005; ICD10CM: D68.09;
Cytogenetic location: 17p13.2 Genomic coordinates (GRCh38): 17:4,932,277-4,935,023 (from NCBI)
| Location | Phenotype |
Phenotype MIM number |
Inheritance |
Phenotype mapping key |
|---|---|---|---|---|
| 17p13.2 | {Nonarteritic anterior ischemic optic neuropathy, susceptibility to} | 258660 | Autosomal recessive | 3 |
| Bernard-Soulier syndrome, type A1 (recessive) | 231200 | Autosomal recessive | 3 | |
| Bernard-Soulier syndrome, type A2 (dominant) | 153670 | Autosomal dominant | 3 | |
| von Willebrand disease, platelet-type | 177820 | Autosomal dominant | 3 |
Glycoprotein Ib (GP Ib) is a platelet surface membrane glycoprotein that functions as a receptor for von Willebrand factor (VWF; 613160). The main portion of the receptor is a heterodimer composed of 2 polypeptide chains, an alpha chain and a beta chain (GP1BB; 138720), that are linked by disulfide bonds. The GP1BA gene encodes the alpha subunit. The complete receptor complex includes noncovalent association of the alpha and beta subunits with platelet glycoprotein IX (GP9; 173515) and platelet glycoprotein V (GP5; 173511) (review by Lopez et al., 1998).
The alpha subunit of GP Ib is susceptible to cleavage by trypsin or by the calcium-dependent protease calpain, giving rise to a soluble heavily glycosylated N-terminal fragment known as 'glycocalicin.' By screening a human cDNA library with an antibody to glycocalicin, Lopez et al. (1987) isolated a potential alpha subunit cDNA encoding a 610-amino acid protein with a molecular mass of approximately 145 kD. The predicted protein has an extracytoplasmic leucine-rich domain composed of a 24-amino acid motif that contains 7 conserved leucine positions. The extracytoplasmic domain is followed by a 29-amino acid transmembrane domain and a 100-amino acid intracellular domain at the carboxyl end of the molecule. The GP1B beta subunit, GP9, and GP5 have similar leucine-rich domains.
By in situ hybridization using a genomic clone, Wenger et al. (1989) demonstrated that the GP1BA gene is located on chromosome 17pter-p12.
The binding of platelet GP Ib to von Willebrand factor facilitates initial platelet adhesion to vascular subendothelium after vascular injury. The binding of VWF to the GP Ib complex also initiates signaling events within the platelet that lead to enhanced platelet activation, thrombosis, and hemostasis (Lopez et al., 1998). Michelson et al. (1986) presented evidence that a portion of the oligosaccharide chains on glycocalicin contributes to the VWF binding activity of GP Ib. Harmon and Jamieson (1986) found that GP Ib was a receptor for thrombin (176930), and that glycocalicin was the site of thrombin binding. Michelson et al. (1988) showed that there is a large intraplatelet pool of GP Ib.
Andrews and Fox (1992) noted that the GP Ib complex is a major site of attachment of the platelet membrane skeleton to the plasma membrane, mediated by the interaction of actin-binding protein with the receptor complex. They showed that a region between thr536 and phe568 of the cytoplasmic domain of the alpha subunit participates in the interaction.
Steinberg et al. (1987) measured plasma concentration of glycocalicin, as an aid to classification of thrombocytopenia; values were low in situations of bone marrow suppression and normal or elevated when there was accelerated platelet turnover. Beer et al. (1994) also suggested that glycocalicin is a useful platelet marker in certain diseases.
Crystal Structure
Huizinga et al. (2002) presented the crystal structure of the GP1BA amino-terminal domain and its complex with the VWF (613160) domain A1. In the complex, GP1BA wraps around one side of A1, providing 2 contact areas bridged by an area of solvated charge interaction. The structures explain the effects of gain-of-function mutations related to bleeding disorders and provide a model for shear-induced activation.
Celikel et al. (2003) determined that the structure of platelet GP1BA bound to thrombin at 2.3 angstrom resolution and defined 2 sites that bind to exosite II and exosite I of 2 distinct alpha-thrombin molecules, respectively. GP1BA occupancy may be sequential, as the site binding to alpha-thrombin exosite I appears to be cryptic in the unoccupied receptor but exposed when a first thrombin molecule is bound through exosite II. Celikel et al. (2003) suggested that these interactions may modulate alpha-thrombin function by mediating GP1BA clustering and cleavage of protease-activator receptors, which promote platelet activation, while limiting fibrinogen clotting through blockade of exosite I.
Dumas et al. (2003) independently determined the crystal structure of the GP1BA-thrombin complex at 2.6 angstrom resolution. They found that in the crystal lattice, the periodic arrangement of GP1BA-thrombin complexes mirrors a scaffold that could serve as a driving force for tight platelet adhesion.
Bernard-Soulier Syndrome, Autosomal Recessive
In a patient with autosomal recessive Bernard-Soulier syndrome (BSSA1; 231200), Ware et al. (1990) identified a homozygous nonsense mutation in the GP1BA gene (606672.0001).
Bernard-Soulier Syndrome, Autosomal Dominant
In a Caucasian family in which 5 members over 2 generations had an autosomal dominant form of Bernard-Soulier syndrome (BSSA2; 153670), Miller et al. (1992) identified a heterozygous mutation in the GP1BA gene (606672.0004).
von Willebrand Disease, Platelet-Type
Platelet-type von Willebrand disease (VWDP; 177820), also known as pseudo-von Willebrand disease, is an autosomal dominant bleeding disorder characterized by abnormally enhanced binding of von Willebrand factor by patients' platelets. In 7 affected members of a family with pseudo-VWD, Miller et al. (1991) identified a heterozygous mutation in the GP1BA gene (606672.0003).
Nonarteritic Anterior Ischemic Optic Neuropathy, Susceptibility to
Salomon et al. (2004) reported that the presence of the VNTR B allele of GP1BA (606672.0002) confers a significant risk for nonarteritic anterior ischemic optic neuropathy (NAION; 258660), with an odds ratio of 4.25 (95% CI 1.67-10.82, P = 0.013). Nine of 16 patients who bore the VNTR B allele (56.3%) had second eye involvement, whereas only 17 of 72 patients (23.6%) without the allele had second eye involvement (p = 0.009), indicating that the presence of the VNTR B allele may predispose affected patients to second eye involvement.
Polymorphisms
By SDS-PAGE, Moroi et al. (1984) studied GP Ib from 131 Japanese individuals and identified 4 slightly different species of GP Ib corresponding to different molecular masses (see also 606672.0002). On the assumption of a 4-allele system, the gene frequencies calculated were: A, 0.073; B, 0.011; C, 0.561; and D, 0.355. Platelets of different GP Ib phenotypes showed the same functional properties. Furthermore, no individual had more than 2 types; the relative amounts of the 2 bands on SDS-PAGE were about equal in each person; the phenotype was constant on multiple testings and the phenotypes of children were consistent with those of their parents: e.g., the parents of a person with the rare phenotype BC were CC and BD.
Polymorphisms described in the GP1BA gene include the Kozak T/C polymorphism at position -5, the variable number of tandem repeats (VNTR; 606672.0002), and the thr145-to-met polymorphism.
The platelet-specific alloantigen Sib(a), located within the GP Ib alpha subunit, is involved in the pathogenesis of platelet transfusion refractoriness. Murata et al. (1992) identified a threonine/methionine dimorphism at position 145 of the GP Ib-alpha sequence and determined that the Sib(a) antigen corresponds to the molecule containing methionine-145. The diallelic codons were detected by restriction enzyme analysis of amplified genomic DNA fragments from the GP1BA gene. Among 61 healthy blood donors, the allele frequencies were 89% and 11% for the threonine-145 and methionine-145 codons, respectively. A positive correlation existed between platelet reactivity with the anti-Sib(a) antibody and the presence of a methionine-145 encoding allele. The findings provide methods useful in transfusion medicine to match donor and recipient platelets. Baker et al. (2001) referred to the thr145 polymorphism as human platelet antigen-2a (HPA-2a) and met145 as HPA-2b.
T/C polymorphism at the -5 position from the initiator ATG codon of the GP1BA gene was first reported by Kaski et al. (1996) and is located within the 'Kozak' consensus nucleotide sequence. The presence of a cytosine (C) at this position significantly increases the surface expression of the GP Ib/V/IX complex (Afshar-Kharghan et al., 1999). This result prompted Ishida et al. (2000) to examine the presence of Kozak sequence polymorphism of GP1BA in Asian populations and to determine whether this polymorphism has a role in coronary artery disease. The frequency of cytosine was 0.283 and 0.219 in Japanese and Korean populations, respectively. The C allele is linked with human platelet antigen-2a and smaller types of variable number of tandem repeats (VNTR). No association was observed between these alleles and coronary artery disease in a case-control study.
Baker et al. (2001) noted that platelets are pivotal to the process of arterial thrombosis resulting in ischemic stroke and that thrombosis is initiated by the interaction of VWF and GP Ib. They studied whether GP1BA polymorphisms are candidate genes for first-ever ischemic stroke. The frequency (22.8%) of T/C heterozygotes in the Caucasian Australian population studied was similar to that in other populations. The heterozygous genotype was elevated in the stroke group (32.2%) and the increased relative risk was still apparent after adjusting for conventional cardiovascular risk factors such as hypertension, diabetes, hyperlipidemia, smoking, and previous vascular events. CC homozygotes were uncommon and the study was not powered to examine the role of the CC genotype alone. The authors hypothesized that the Kozak polymorphism influences the pathogenesis of ischemic stroke because the C allele increases the level of platelet glycoprotein GP Ib-alpha on the platelet surface.
Bergmeier et al. (2006) generated mice expressing Gp1ba in which the extracellular domain was replaced by that of the human IL4 receptor (IL4R; 147781). Platelet adhesion to ferric chloride-treated mesenteric arteries was virtually absent in transgenic mice compared to avid adhesion in wildtype mice, and resulted in complete inhibition of arterial thrombus formation. When infused into wildtype mice, transgenic IL4R/Gp1ba platelets or wildtype platelets lacking the 45-kD N-terminal domain of Gp1ba failed to incorporate into growing arterial thrombi, even if the platelets were activated before infusion. Bergmeier et al. (2006) concluded that GP1BA is required for recruitment of platelets to both exposed subendothelium and thrombi under arterial flow conditions and that it contributes to arterial thrombosis by adhesion mechanisms independent of binding to VWF.
In a patient with Bernard-Soulier syndrome (231200), Ware et al. (1990) identified a nonsense mutation in the GP1BA gene (W343X). Immunoblotting of the patient's solubilized platelets demonstrated absence of normal GP Ib-alpha but presence of a smaller immunoreactive species. The authors hypothesized that the truncated polypeptide could not be properly inserted into the platelet membrane. The truncated polypeptide was also present, along with normal protein, in platelets from the patient's mother and 2 of his 4 children.
Moroi et al. (1984) described 4 polymorphic variants of platelet von Willebrand factor receptor. Meyer and Schellenberg (1990) showed that the polymorphism is due to size differences in the heavily glycosylated macroglycopeptide region of the alpha chain of GP Ib. Because this region of the alpha subunit contains tandemly repeated sequences (Lopez et al., 1987), Lopez and Ludwig (1991) amplified genomic DNA corresponding to this region from 120 persons of diverse ethnic origins. They found in the group 3 alleles of different sizes which varied in the number of repeats of a 39-bp sequence that led to perfect duplication of the 13-amino acid sequence, ser399 to thr411 (numbering based on published sequence). The smallest isoform contained 1 such sequence, the next larger 2 repeats, and the largest 3 repeats. The repeat sequence contains 5 sites for potential O-glycosylation, which together with the repeated amino acids would result in incremental differences in molecular weight of approximately 6,000 between the different isoforms. Differences in the number of repeats were predicted to change the length of the elongated glycosylated region and to change the distance between the amino-terminal ligand-binding domain and the plasma membrane, an effect that might have a subtle bearing on the binding of VWF or on the sensitivity of this interaction to shear forces.
Salomon et al. (2004) reported that the presence of the VNTR B allele of GP1BA confers a significant risk for nonarteritic anterior ischemic optic neuropathy (NAION; 258660), with an odds ratio of 4.25 (95% CI 1.67-10.82, P = 0.013). Nine of 16 patients who bore the VNTR B allele (56.3%) had second eye involvement, whereas only 17 of 72 patients (23.6%) without the allele had second eye involvement (P = 0.009), indicating that the presence of the VNTR B allele may predispose affected patients to second eye involvement.
Platelet-type von Willebrand disease (177820), also known as pseudo-von Willebrand disease, is an autosomal dominant bleeding disorder characterized by abnormally enhanced binding of von Willebrand factor by patients' platelets. In 7 affected members of a family with pseudo-VWD, Miller et al. (1991) identified a heterozygous mutation in the GP1BA gene resulting in the substitution of gly233-to-val (G233V). The mutation was absent in 6 unaffected family members. To evaluate the functional consequences of the G233V mutation, Murata et al. (1993) constructed a recombinant analog of the alpha subunit of GP Ib containing val233. The recombinant fragment with the val233 substitution reproduced the functional abnormality of the GP Ib-IX complex in platelet-type von Willebrand disease.
In a Caucasian family in which 5 members over 2 generations were affected with an autosomal dominant form of Bernard-Soulier syndrome (153670), Miller et al. (1992) identified a heterozygous leu57-to-phe (L57F) substitution within the highly conserved GP Ib-alpha leucine tandem repeat that segregated with the disease. The proband was a 13-year-old male who was referred for evaluation of thrombocytopenia which had been noted before dental extractions. He had frequent episodes of epistaxis, one of which was severe enough to require hospitalization. The mother had a long history of bleeding problems as did the other affected family members except for one who had 'an essentially negative bleeding history.' The affected individual showed increased mean platelet volume.
In a father and 2 daughters with pseudo-von Willebrand disease (177820), Russell and Roth (1993) demonstrated an A-to-G transition in codon 239 that resulted in substitution of valine for methionine (M239V). The abnormal receptor displayed increased affinity for its ligand, von Willebrand factor.
In a patient with Bernard-Soulier syndrome (231200), Ware et al. (1993) identified a homozygous ala156-to-val substitution (A156V) in the GP Ib alpha protein. This mutation is situated in a leucine-rich repeat of the protein and is associated with a loss of binding with the von Willebrand factor.
In 6 Italian families with autosomal dominant inheritance of mild bleeding symptoms, including petechiae, epistaxis, and mucosal bleeding, Savoia et al. (2001) identified a heterozygous A156V substitution in the GP1BA gene. The findings were consistent with autosomal dominant Bernard-Soulier syndrome (153670). The 6 probands with the A156V mutation and 2 others were found to have a reduction of platelet membrane glycoproteins comparable to that found in a BSS heterozygous condition.
In a 73-year-old male with Bernard-Soulier syndrome (231200) and life-long bleeding problems, Holmberg et al. (1997) found a homozygous trp498-to-ter mutation in the GP1BA gene, resulting in a truncated polypeptide chain. In contrast to previously reported truncated forms, this one contained a portion of the transmembranous domain as well as the juxtamembranous cysteines engaged in a disulfide bond with the beta-polypeptide. The patient had suffered subdural hematomas and severe episodes of gastric hemorrhage. Thrombocytopenia had been diagnosed in childhood. The patient's parents had common ancestors in the late seventeenth century. The diagnosis of Bernard-Soulier syndrome was based on thrombocytopenia with giant platelets, absent ristocetin aggregation, and no detectable GP Ib on the platelets with an enzyme-linked immunosorbent assay (Waldenstrom et al., 1991).
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