Gene/Protein Disease Symptom Drug Enzyme Compound
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Query: UNIPROT:P02774 (Gc-globulin)
 196 document(s) hit in 31,850,051 MEDLINE articles (0.00 seconds)

Group-specific component (GC) subtyping in semen and seminal stains was carried out using isoelectric focusing in carrier ampholyte-generated pH gradients and immunoblotting. In serum samples the anodal bands of GC 1F and of GC 1S disappeared by neuraminidase treatment, but in semen samples these bands remained unchanged after such treatment. The GC 2 type in semen exhibited two bands: the main GC 2 band and another fast band which focused at the position of the cathodic band of GC 1F. These seminal GC bands were unaffected by enzyme digestion. Reliable subtyping was possible in seminal stains stored at 4 degrees C for up to 10 weeks, at room temperature for up to 8 weeks, and at 37 degrees C for up to 5 weeks. The GC subtyping by conventional isoelectric focusing after neuraminidase treatment is simple, economical and useful in medicolegal examination of seminal stains.
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PMID:Group-specific component subtyping in semen and seminal stains by conventional isoelectric focusing. 749 24

The structure and organization of the human vitamin D-binding protein (DBP) gene has been determined. The gene is composed of 13 exons and 12 intervening sequences. With the help of the polymerase chain reaction (PCR) introns were amplified using exon-specific oligonucleotide primers, and were sequenced after subcloning; the exon/intron borders were determined. The introns 2, 5, 7, 9 and 10 were sequenced completely; the introns 1, 3, 4, 6, 8, 11 and 12 were sequenced in part. We designed intron-specific primers for the amplification of each exon by the PCR-method. This permits the analysis of mutational and function-related sites. By comparison with the genes for human albumin and alpha-fetoprotein the gene for DBP/GC is confirmed as a member of this multigene family. The location of the introns in the coding region of the human DBP-gene is identical with the position of the introns in the rat DBP-gene.
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PMID:Sequence and organization of the human vitamin D-binding protein gene. 750 19

1,25-dihydroxyvitamin D3 (1,25(OH)2 D3) has been shown to modulate lymphocyte activation in vitro. Through binding to specific receptors 1,25-(OH)2 D3 inhibits proliferation, immunoglobulin production and the release of cytokines. Moreover, 1,25-(OH)2 D3 is efficiently produced by activated monocytes. These findings suggest that 1,25-(OH)2 D3 may play a role as a regulator of immunological activation. Consequently, we found it of interest to study the serum levels of the two major metabolites of vitamin D3 in patients with systemic lupus erythematosus (SLE) (n = 21), rheumatoid arthritis (RA) (n = 29) and osteoarthritis (n = 12). In patients with SLE the levels of 25-OH D3 were below those of the healthy controls (p = 0.0008) and OA (p = 0.0168). The levels 1,25-(OH)2 D3 corresponded to normal levels. There were no significant correlations between 25-OH D3 levels and clinical or paraclinical disease manifestations. Further, the phenotypic distribution of Gc-globulin, which binds vitamin D3 metabolites in circulation, was normal. The serum concentrations of 1,25-(OH)2 D3 and 25-OH D3 in patients with RA and OA corresponded to those of the controls. Although the cause of the reduced 25-OH D3 levels in SLE patients is unclear, possible beneficial effects of administration of vitamin D to these patients should be considered.
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PMID:Vitamin D3 metabolism in patients with rheumatic diseases: low serum levels of 25-hydroxyvitamin D3 in patients with systemic lupus erythematosus. 758 74

Gc-globulin (vitamin D binding protein) has been shown to augment significantly the leukocyte chemotactic activity of the activated C peptides C5a and C5adesArg (i.e., the co-chemotactic effect). However, the mechanism of chemotaxis enhancement is not known. To investigate the role that the neutrophil plays in this process, cells were co-incubated with Gc-globulin for up to 45 min and washed, and their subsequent chemotactic response to a suboptimal concentration of C5a alone was measured during a 30-min assay. The generation of co-chemotactic activity during the preincubation period was time dependent, showed minimal activity for the first 10 min and a steep rise from 10 to 20 min, and was maximal and stable at 30 min. The binding of radiolabeled Gc-globulin by neutrophils at 37 degrees C mirrored this time-dependent generation of C5a co-chemotactic activity, with stable cellular levels achieved between 30 and 45 min at 36 +/- 4 fmol (2 +/- 0.1 ng)/10(6) cells. The binding of radiolabeled Gc-globulin and the generation of co-chemotactic activity were dependent upon physiologic temperatures (37 degrees C) and levels of Ca2+ (1.3 mM) and Mg2+ (0.8 mM), and were inhibited by an Ab to Gc-globulin. Finally, the C5a co-chemotactic activity of Gc-globulin would decay rapidly if neutrophils were washed and then incubated a second time at 37 degrees C before chemotaxis to C5a. These results demonstrate that neutrophils bind exogenous Gc-globulin and generate C5a co-chemotactic activity in a time-, temperature-, and divalent cation-dependent manner. Moreover, this activity is transient if neutrophils lack a continuous supply of Gc-globulin.
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PMID:Co-chemotactic effect of Gc-globulin (vitamin D binding protein) for C5a. Transient conversion into an active co-chemotaxin by neutrophils. 759 52

The transporter of vitamin D and its metabolites in blood has received increasing attention in recent years, and is recognized to be a member of a gene family that includes albumin and alpha-fetoprotein. Identical to the group specific component (Gc-globulin) of serum, the protein is a single-chain polypeptide constitutively synthesized in liver that circulates in amounts in far excess of normal vitamin D metabolite concentrations in blood. It plays the major role in the egress of endogenously synthesized vitamin D, from skin and appears to restrain D-sterols from too rapid/excessive cell entry. Along with plasma gelsolin, it comprises the plasma actin-scavenger system that facilitates removal of actin, liberated from lysed cells, by depolymerization and prevention of polymerization. Recently, the protein has been shown to behave as a co-chemotaxin specific for the complement peptide C5a, and its sialic acid-free form has been reported to play a role in macrophage activation. The latter functions strongly implicate its participation in inflammation responses. A unifying hypothesis might also suggest the protein to provide focal D-sterol delivery to cells that are important to the resolution of tissue injuries.
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PMID:Plasma vitamin D-binding protein (Gc-globulin): multiple tasks. 762 13

Vitamin D-binding protein (DBP), a multifunctional, highly polymorphic glycoprotein responsible for the transport of vitamin D and for sequestering extracellular actin, was isolated from human serum and crystallized using vapour diffusion methods. The crystals were grown from 7.5% v/v polyethylene glycol 400 and 0.1 M acetate buffer at pH 4.6. These crystals show diffraction patterns consistent with the tetragonal space groups P4(1) and P4(3) with unit cell dimensions a = b = 135.5(4) A and c = 75.9(4) A. They diffract to 2.3 A. Using polyacrylamide gel electrophoresis it was shown that according to their electrophoretic mobility the O-glycosylated isoforms, with a terminal sialic acid residue, are absent in the crystals.
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PMID:Crystallization and X-ray investigation of vitamin D-binding protein from human serum. Identification of the crystal content. 763 9

The distribution of nine genetic markers was studied in a sample of 170 individuals coming from Corte (Corsica, France). The corresponding gene frequencies were as follows: ACP*A = 0.080, ACP*B = 0.887, ACP*C = 0.033; ESD*1 = 0.854; AK*1 = 0.976; PGD*A = 0.991; DIA*1 = 0.994; GLO1*1 = 0.278; PGM1*1S = 0.694, PGM1*1F = 0.100, PGM1*2S = 0.153, PGM182F = -.053; C3*S = 0.793, C3*F = 0.183, C3*V = 0.024; GC*1S = 0.713, GC*1F = 0.079; GC*2 = 0.207. These findings were discussed in the context of other Mediterranean populations. The results showed a relatively high genetic heterogeneity of Corsicans compared to other populations. The genetic differences appeared to be smaller between Corsicans and Sardinians than among Corsicans and other Mediterraneans.
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PMID:A study of several genetic markers in the Corsican population (France). 766 41

The distribution of the HP and GC serum protein polymorphisms in the !Kung San and Kavango (Bantu) populations in Namibia were examined. The obtained allele frequencies of GC marker system were very similar in both populations (GC*1F approximately equal to 0.80, GC*2 approximately equal to 0.10), while the distributions of the HP subtypes in the !Kung San sample (HP*1F = 0.0967, HP*1S = -.1452, HP*2FS = 0.7581) differed markedly from those in the Kavango one (HP*1F = 0.3791, HP*1S = 0.2375, HP*2S = 0.375). These results confirm previously reported allelic distributions in ethnically similar populations.
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PMID:HP and GC subtype distribution in the !Kung San and Kavango in Namibia. 766 42

A population genetic study was undertaken to provide gene frequency data on the additional blood genetic markers in the Semai and to estimate the genetic relations between the Semai and their neighboring and linguistically related populations by genetic distance and principal components analyses. Altogether 10 polymorphic and 7 monomorphic blood genetic markers (plasma proteins and red cell enzymes) were studied in a group of 349 Senoi Semai from 11 aboriginal settlements (villages) in the Pahang State of western Malaysia. Both the red cell glucose-6-phosphate dehydrogenase (G6PD) and 6-phosphogluconate dehydrogenase (PGD) loci reveal the presence of polymorphic frequencies of a nondeficient slow allele at the G6PD locus and a fast allele at the PGD locus. The Semai are characterized by high prevalences of ahaptoglobinemia and G6PD deficiency, high frequencies of HP*1, HB*E, RH*R1, ACP*C, GLO1*1, PGM1*2+, and GC*1F and corresponding low frequencies of ABO*A, HbCoSp, HB*B0, TF*D, CHI, and GC*2. Genetic distance analyses by both cluster and principal components models were performed between the Semai and 14 other populations (Malay; Javanese; Khmer; Veddah; Tamils of Malaysia, Sri Lanka, and India; Sinhalese; Oraon; Toda and Irula of India; Chinese; Japanese; Koreans) on the basis of 30 alleles at 7 polymorphic loci. A more detailed analysis using 53 alleles at 13 polymorphic loci with 10 populations was carried out. Both analyses give genetic evidence of a close relationship between the Semai and the Khmer of Cambodia. Furthermore, the Semai are more closely related to the Javanese than to their close neighbors--the Malay, Chinese, and Tamil Indians. There is no evidence for close genetic relationship between the Semai and the Veddah or other Indian tribes. The evidence fits well with the linguistic relationship of the Semai with the Mon-Khmer branch of the Austro-Asiatic language family.
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PMID:Population genetic study among the Orange Asli (Semai Senoi) of Malaysia: Malayan aborigines. 772 Dec 78

The structure and organization of the human vitamin-D-binding protein gene (DBP, group-specific component, GC) have recently been determined. Each exon may now be amplified by the PCR method using oligonucleotide primers deduced from the intron sequences near their 5' ends and 3' ends. In this study we examined the anodal GC variants 1A1 and 2A9. Genomic DNA of the variant 1A1 was obtained from Australian Aborigines and from South African Bantu-speaking Blacks. Amplification and sequencing of exon 11 of 1A1 revealed a point mutation in codon 429 at the second position. It is remarkable that this mutation was found in the Australian 1A1 variant and in the African 1A1 variant, and raises the question whether the mutation in these two ethnic groups has a common origin. Genomic DNA of the 2A variant called 2A9 was obtained from South Germany and a point mutation also concerning position 429 in exon 11 was found. The nucleotide exchange in this case, however, was at the first position of the codon. The widely distributed genetic polymorphism of DBP/GC is located in exon 11 and is characterized by substitution at amino acid positions 416 and 420. Variant 1A1 is due to a second site mutation of the allele GC*1F; variant 2A9 is due to a mutation in the GC*2 allele.
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PMID:Characterization of mutants of the vitamin-D-binding protein/group specific component: GC aborigine (1A1) from Australian aborigines and South African blacks, and 2A9 from south Germany. 772 72


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