Nucleotide sequence and expression of the human gene encoding apolipoprotein H (β2-glycoprotein I)

Mehdi, Haider; Nunn, Michael; Steel, D. M.; Whitehead, Alexander S.; Perez, Mary; Walker, L E; Peeples, Mark E.

doi:10.1016/0378-1119(91)90449-l

Cited by 76 publications

(50 citation statements)

References 19 publications

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“…This has been interpreted to be a part of the low-grade inflammation present in these patients (Pickup 2004;Sjöholm and Nyström 2006), which could also explain both lowered TTR levels in T2DM serum. Lowering of albumin and ApoH are other characteristic changes in inflammation (Gabay and Kushner 1999;Mehdi, et al 1991). Both these alterations could be explained by the low-grade inflammatory response, which has been suggested to be a part of the pathogenesis of T2DM (Pickup 2004).…”

Section: Many Individual Serum Proteins Have Been Shown To Vary Betwementioning

confidence: 99%

Proteomics in diabetes research

Sundsten

Ortsäter

2009

Molecular and Cellular Endocrinology

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SummaryBoth type 1 and type 2 diabetes mellitus are heterogeneous diseases with alterations in many genes and their products. Not all transcriptional alterations lead to protein changes, which makes it very important to, in conjunction with mRNA expression studies, also address changes in cellular protein levels. Various proteomic techniques are available for measuring many protein changes simultaneously. Many proteomic studies have been performed in the context diabetes research, with the aims of both describing the healthy tissue and to unravel the complex pathophysiology behind the disease. In addition, effects on proteins induced by different treatments have also been investigated using proteomic approaches. In this paper the field of diabetes proteomics today will be reviewed. Findings from proteomic studies investigating pancreatic islets and β-cells as well as serum, fat, skeletal muscle and liver are described.

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Section: Many Individual Serum Proteins Have Been Shown To Vary Betwementioning

confidence: 99%

Proteomics in diabetes research

Sundsten

Ortsäter

2009

Molecular and Cellular Endocrinology

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“…ApoH has been extensively characterized at amino acid and nucleotide levels from a number of species including human (24)(25)(26), rat (27), mouse (28,29), dog (30), cattle (31)(32)(33) and chimpanzee (34).…”

Section: Introductionmentioning

confidence: 99%

RT-PCR and in situ hybridization analysis of apolipoprotein H expression in rat normal tissues

Ragusa

Costa²,

Cefalù³

et al. 2006

Int J Mol Med

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Abstract. In this study, by using different techniques (i.e. Northern blot hybridization, RT-PCR and Southern blot hybridization) on various normal rat tissues, we were able to identify liver, kidney, heart, small intestine, brain, spleen, stomach and prostate as tissues in which the ApoH gene is transcribed. Moreover, for some of these tissues, by in situ hybridization, we found a specific localization of apoH transcripts. For instance epithelial cells of the bile ducts in liver and of the proximal tubules in kidney are the major sites of apoH synthesis. Our data suggest that some of the different physiological roles proposed for apoH could correlate with its direct expression, while others could correlate with its absorption from bloodstream or adjacent cells.

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“…This seeretion suggests that the signal peptide is cleaved and ihe /f-GPl protein is properly refolded. Frc m the results of cDNA cloning and sequencing, the amino aeid sequence derived from /y7-GPI cDNA has 19 amino acids in N-terminal region over the number in the published protein sequence [2][3][4][5] signal peptide bas also been noted for the epidermal growth factor (EGF) receptor [33] and buman WN-ji. Tbe SDS-PAGE analysis of the purified fiyGP] produced IVom insect cells showed ihc protein band contained several molecular species of nearly identical migration (Fig.…”

Section: Discussionmentioning

confidence: 99%

“…[1[. The complete amino acid sequence ofthe protein was determined by peptide sequencing [2] and the complete nucleotides sequence, by cDNA cloning, has bcL-n reported [3][4][5]. These sequencing analyses show that the protein is composed of 326 amino acids of mature protein of/i:-GPI and 19 amino acids of a putative leader sequence.…”

Section: Introductronmentioning

confidence: 99%

Expression of anticardiolipin cofactor, human β2-glycoprotein I, by a recombinant baculovirus/insect cell system

Igarashi

Matsuura

Igarashi

et al. 1993

Clinical and Experimental Immunology

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SUMMARYA full-length cDNA coding a human /i^-glycoprotein I (ji^-GPl) was introduced into the baculovirus genome to construct a recombinant baculovirus. Spodopterafiugiperda {Sf 9) ccWs were infected with the recombinant baculovirus-A protein (moL wt 43 000) reactive with anti-//:-GPI aniisera was produced in the insect cells and secreted into the culture medium. The recombinant /^..-GPl was purified from the culture supernatant by sequential cardiolipin (CL)-afTinity column chromatography and gel filtration. The N-terminal amino acid sequenee ofthe protein was identical to that of the native /(:-GPI purified irom human sera, and ii puUitive signal peptide was cleaved from ihe secreted form ofthe recombinanl protein. The purified recombinanl protein had a eofactor activity whieh enhances CL binding of anticardiolipin antibodies (aCL) in systemic lupus erythematosus (SLE) patients, as well as the native /?;-GPL Thus, the /i:-GPI expressed in insect eells is an immunologically active cofactor.

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Nucleotide sequence and expression of the human gene encoding apolipoprotein H (β2-glycoprotein I)

Cited by 76 publications

References 19 publications

Proteomics in diabetes research

Proteomics in diabetes research

RT-PCR and in situ hybridization analysis of apolipoprotein H expression in rat normal tissues

Expression of anticardiolipin cofactor, human β2-glycoprotein I, by a recombinant baculovirus/insect cell system

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