Structural Features of the Proteins Participating in Blood Coagulation and Fibrinolysis

Davie, EW; Ichinose, Akitada; Leytus, Steven P.

doi:10.1101/sqb.1986.051.01.062

Cited by 37 publications

(11 citation statements)

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“…Pre-incubation of these cells with a neutralizing antibody against the IL-2Rx chain (mAb 7D4) had no effect on the number of IL-15 binding sites (not shown), confirming previous results indicating that IL-2Rax is not involved in IL-15 binding (Giri et al, 1994;Grabstein et al, 1994). (Davie et al, 1986;Perkins et al, 1988). This homology with IL-2Rx, therefore, suggested that we had cloned the murine IL-15Rx chain.…”

Section: ) Oxford University Presssupporting

confidence: 73%

“…The P and y chains are required for high affinity IL-2 binding and IL-2 signaling and are members of the hematopoietin receptor superfamily. The ox chain (or p55) is a low affinity, non-signaling binding subunit, and the only cytokine receptor member of a large family of binding proteins whose members include complement receptor proteins (Davie et al, 1986;Perkins et al, 1988). We have demonstrated that IL-15 requires the 3 chain of the IL-2R for all the biological activities tested, but that the oc chain of the IL-2R is not required (Giri et al, 1994;Grabstein et al, 1994).…”

Section: Introductionmentioning

confidence: 97%

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Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor.

Giri¹,

Kumaki²,

Ahdieh³

et al. 1995

The EMBO Journal

576

435

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Interleukin-15 (IL-15) is a novel cytokine of the fourhelix bundle family which shares many biological activities with IL-2, probably due to its interaction with the IL-2 receptor 3 and y (IL-2RO and ye) chains.We report here the characterization and molecular cloning of a distinct murine IL-15Ra chain. IL-15Ra alone displays an affinity of binding for IL-15 equivalent to that of the heterotrimeric IL-2R for IL-2. A biologically functional heteromeric IL-15 receptor complex capable of mediating IL-15 responses was generated through reconstruction experiments in a murine myeloid cell line. IL-l5Rca is structurally similar to IL-2Ra; together they define a new cytokine receptor family. The distribution of IL-15 and IL15Ra mRNA suggests that IL-15 may have biological activities distinct from IL-2.

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Section: ) Oxford University Presssupporting

confidence: 73%

Section: Introductionmentioning

confidence: 97%

Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor.

Giri¹,

Kumaki²,

Ahdieh³

et al. 1995

The EMBO Journal

576

435

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“…ApoH is a single chain polypeptide of 326 amino acids (Lozier et al 1984;Steinkasserer et al 1991;Mehdi et al 1991;Kristensen et al 1991) and belongs to the short (~ 60 amino acids) consensus repeats (SCR) or complement control protein(CCP) superfamily consisting of five repeats referred to as: GP-I domains (Davie et al 1986), Sushi domains (Ichinose et al 1990), SCRs or CCP repeats (Lozier et al 1984;Klickenstein et al 1987;Kristensen et al 1987). Based upon the predicted structure of apoH protein from its cDNA sequence, 22 cysteine residues that occur in human apoH are conserved in bovine (Kato and Enjyoji 1991) and rat (Aoyama et al 1989).…”

Section: Introductionmentioning

confidence: 98%

Genetic variation in the apolipoprotein H (β2-glycoprotein I) gene affects plasma apolipoprotein H concentrations

et al. 1999

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Apolipoprotein H (apoH, protein; APOH, gene) is a single chain glycoprotein that exists in plasma both in a free form and in combination with lipoprotein particles. ApoH has been implicated in several physiologic pathways, including lipid metabolism, coagulation, and the production of antiphospholipid antibodies. The wide range of interindividual variation in plasma apoH levels is thought to be under genetic control, but its molecular basis is unknown. APOH displays a common structural polymorphism with the occurrence of three common alleles (APOH*1, APOH*2, and APOH*3), the APOH*2 allele being the most frequent in all populations. The relationship between the APOH polymorphism and plasma apoH levels is unknown. In this study, we have determined the impact of this APOH polymorphism on apoH levels in 455 normoglycemic non-Hispanic Whites (220 men and 235 women) from the San Luis Valley, Colorado. Mean plasma apoH levels, determined by capture enzyme-linked immunosorbent assay, were 20.0 +/- 0.2 mg/dl (range: 3.4-31.2 mg/dl) with no significant difference between men and women. In women, but not in men, age had a significant effect on plasma apoH levels explaining 3.4% of its phenotypic variance. ApoH levels also correlated positively with cholesterol (P = 0.015), HDL-cholesterol (P = 0.044), and triglyceride (P = 0.037) in women, but not in men. An analysis of variance (ANOVA) of adjusted plasma apoH levels showed significant association with the APOH polymorphism in both men and women (P < 0.0001), and the APOH polymorphism accounted for 11.4% and 13.6% of the variation in apoH levels in men and women, respectively. Compared with the APOH*1 and APOH*2 alleles, the APOH*3 allele was associated with significantly lower plasma apoH levels. At the molecular level, APOH*3 can be further subdivided into two distinct forms, called APOH*3W and APOH*3B. The APOH*3W form is more common in US Whites and is the result of a missense mutation at codon 316. An ANOVA for the codon 316 polymorphism revealed that this polymorphism is a major determinant of plasma apoH variation (P < 0.0001). This study indicates that common genetic variation in the APOH gene is a significant determinant of plasma apoH levels in non-Hispanics Whites and should be useful in evaluating the role of the APOH genetic variation in various metabolic pathways in which apoH has been implicated.

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“…1). Such domains are observed in a number of complement and non-complement proteins (Davie et al, 1986). The three-dimensional structure analyses of various apolipoproteins (Wilson et al, 1991;Breiter et al, 1991;Borhani et al, 1997) suggest that elongated amphiphatic helical bundles are common structural motifs for apolipoproteins.…”

Section: Introductionmentioning

confidence: 99%

“…It has a high carbohydrate content of about 16% by weight (Finlayson & Mushinsky, 1967). Apo-H shows extensive internal homology, with ®ve consecutive domains of 60 amino-acid residues each, referred to as the GP-I domain (Davie et al, 1986), sushi domain (Ichinose et al, 1990) and complement-control protein (CCP) repeats (Kristensen et al, 1987) (Fig. 1).…”

Section: Introductionmentioning

confidence: 99%

Crystallization and preliminary X-ray crystallographic studies on apolipoprotein H (β2-glycoprotein-I) from human plasma

Saxena

Gries

Schwarzenbacher

et al. 1998

Acta Crystallogr D Biol Cryst

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Apolipoprotein-H (Apo-H, M w 9 50 kDa) is a carbohydraterich human-plasma protein which exists in blood serum in the free form as well as distributed between several classes of lipoproteins. Single crystals of apo-H have been obtained and crystallographic data sets have been collected. The crystals belong to the orthorhombic space group C222 1 , with cell dimensions a = 158.47, b = 169.25, c = 113.28 A Ê (at 100 K). The data indicate that the crystallographic asymmetric unit contains one tetramer of the protein.

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Structural Features of the Proteins Participating in Blood Coagulation and Fibrinolysis

Cited by 37 publications

References 0 publications

Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor.

Identification and cloning of a novel IL-15 binding protein that is structurally related to the alpha chain of the IL-2 receptor.

Genetic variation in the apolipoprotein H (β2-glycoprotein I) gene affects plasma apolipoprotein H concentrations

Crystallization and preliminary X-ray crystallographic studies on apolipoprotein H (β2-glycoprotein-I) from human plasma

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