Human group-specific component (Gc) is a member of the albumin family.

Yang, Funmei; Brune, Jill L.; Naylor, Susan L.; Cupples, Rod; Naberhaus, Kathleen H.; Bowman, Barbara H.

doi:10.1073/pnas.82.23.7994

Cited by 139 publications

(50 citation statements)

References 25 publications

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“…Numerous studies detected DBP bound to the surface of several cell types, including human macrophages and lymphocytes, supporting the concept that direct substrate trafficking is pivotal in vitamin D 3 regulation (35)(36)(37). Therefore, we studied DBP uptake in CD4 + T cells and macrophages isolated from male and female MS patients.…”

Section: Gender Influence On Vitamin D 3 Metabolismmentioning

confidence: 99%

“…DBP is a serum glycoprotein that binds and transports vitamin D 3 and its metabolites to target cells (75). Human DBP has been linked to several membrane components of peripheral blood monocytes, lymphocytes, and neutrophils, supporting the concept of a cell surface-binding site for DBP (35)(36)(37). In addition, studies demonstrated that in vivo endocytic uptake of the vitamin D 3 -DBP complex is mediated by megalin and cubilin, two members of the low-density lipoprotein-like receptor protein family (76,77).…”

Section: Foxp3mentioning

confidence: 99%

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Gender Differences in 1,25 Dihydroxyvitamin D3 Immunomodulatory Effects in Multiple Sclerosis Patients and Healthy Subjects

Correale¹,

Ysrraelit²,

Gaitán³

2010

The Journal of Immunology

147

112

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Section: Gender Influence On Vitamin D 3 Metabolismmentioning

confidence: 99%

Section: Foxp3mentioning

confidence: 99%

Gender Differences in 1,25 Dihydroxyvitamin D3 Immunomodulatory Effects in Multiple Sclerosis Patients and Healthy Subjects

Correale¹,

Ysrraelit²,

Gaitán³

2010

The Journal of Immunology

147

112

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“…The most characteristic feature of the albumin sequence is the repetitious pattern of 17 disulfide bridges that organizes the molecule into three homologous, yet distinct, domains. With the cDNA cloning and sequencing of alpha-fetoprotein (human : Law & Dugaiczyk, 1981;Moringa et al, 1983;rat: Jagodzinski et al, 198 1;mouse: Gorin et al, 1981) and vitamin D-binding protein (human: Yang et al, 1985;Schoentgen et al, 1986;rat: Cooke & David, 1985;mouse: Yang et al, 1990), it became evident that these proteins are related to albumin through a series of gene duplications. As such these proteins provide an interesting glimpse into the evolution of a multigene family.…”

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confidence: 99%

Characterization, primary structure, and evolution of lamprey plasma albumin

Gray

Doolittle

1992

Protein Science

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The most abundant protein found in blood plasma from the sea lamprey (Petromyzon marinus) has the hallmarks of a plasma albumin: namely, high abundance, solubility in distilled water, a small number of tryptophans, and a high content of cysteines and charged residues. As in other vertebrate albumins, not all the cysteines are disulfide bonded. An unusual feature of this protein is its molecular weight of 175,000, roughly 2.5 times the size of other vertebrate albumins. Its amino acid sequence, deduced from a series of overlapping cDNA clones, can be aligned with other members of the gene family including plasma albumin, alpha-fetoprotein, and vitamin-D binding protein, confirming that it is indeed an oversized albumin. An unusual feature of the sequence is a 28-amino acid stretch consisting of a serine-threonine repeat with the general motif (STTT). Lamprey albumin contains a 23-amino acid putative signal peptide and a 6-residue putative propeptide, which, when cleaved, yield a mature protein of 1,394 amino acids with a calculated molecular weight of 157,000. The sequence also includes nine potential N-linked glycosylation sites (Asn-X-Ser/Thr), consistent with observation that lamprey albumin is a glycoprotein. If all the potential glycosylation sites were occupied by clusters of 2,000 molecular weight each, the total molecular weight would be 175,000. Like other members of the gene family, lamprey albumin is composed of a series of 190-amino acid repeats, there being seven such domains all together. Quantitative amino acid sequence comparisons of lamprey albumin with the other members of the gene family indicate that it diverged from an ancestral albumin prior to the gene duplications leading to this diverse group. This notion is confirmed by the pattern of amino acid insertions and deletions observed in a consideration of all domains that compose this family. Furthermore, it suggests that the invention of albumin antedates the vertebrate radiation.Keywords: plasma albumin; protein evolution; sea lamprey Plasma albumin is the most abundant protein in vertebrate blood plasma and also among the most readily purified. The ability to secure relatively pure albumin in large quantities has led to it becoming one of the most familiar and extensively studied of all proteins. Its principal role is thought to be that of a transport protein, reversibly binding fatty acids, bilirubin, and a myriad of other molecules, as well as its being a major contributor to the effective osmotic pressure of the plasma. As a result of its ligand-binding properties and high concentration, albumin provides a stabilizing effect on plasma solute levels, buffering the concentration of metabolites. Paradoxically, humans and some other animals appear to be quite capable of surviving with levels of albumin in

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“…Recently, the relationship between the risk of chronic obstructive pulmonary disease (COPD) and the Gc protein allele type, such as Gc*1F, Gc*1S, Gc*2, had been reported. [93][94][95][96][97] Gc*1F increased the COPD risk, while Gc*2 suppressed the risk. Thus, the allele type of Gc protein is an important factor in COPD.…”

Section: Discussionmentioning

confidence: 99%

Exploring Unique Structures: Flexibility is a Significant Factor in Biological Activity

Ohkura

2007

Biological & Pharmaceutical Bulletin

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The effect of molecular flexibility on biological activity was described for soft (e.g. hGH peptides) and hard molecules (e.g. biscoclaurine-type alkaloids). These molecules had a macrocyclic structure during molecular mechanics analysis, and the minimum essential unit, which affects insulin-involved fatty acid synthesis, was observed. The flexibility of the molecular center is concerning with biological activity through the diversification of structural feature, and compared with two types of molecules which have a rigid (haloacetylcarbamoyl-2-nitroimidazole analogs: chiral-TXs) or flexible (bis-quaternary ammonium compounds: bis-QACs) molecular center. Center flexibility reflected the conformation occurrence in TXs and bis-QACs. A parameter (solvation-free energy: dGW), which reflects structural hydrophobicity, was shown, and applied to the molecular design of brefeldin A analog. This hydrophobic index was very useful, and was used for conformational analysis of chiralTXs and bis-QACs. In molecular dynamics analysis of cholesterol-dependent cytolysin (e.g. storeptolysin O) and -independent cytolysin (e.g. intermedilysin), whole molecules moved like a bow and different conformations were shown in every moment. In such situations, the membrane-associated 11mer region in these cytolysins were flexible and could always interact with extramolecular factors (e.g. membrane constitution).

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Human group-specific component (Gc) is a member of the albumin family.

Abstract: The group-specific component (Gc) is the

Cited by 139 publications

References 25 publications

Gender Differences in 1,25 Dihydroxyvitamin D3 Immunomodulatory Effects in Multiple Sclerosis Patients and Healthy Subjects

Gender Differences in 1,25 Dihydroxyvitamin D3 Immunomodulatory Effects in Multiple Sclerosis Patients and Healthy Subjects

Characterization, primary structure, and evolution of lamprey plasma albumin

Exploring Unique Structures: Flexibility is a Significant Factor in Biological Activity

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