Two distinct forms of ? 2-microglobulin in different races of owl monkey (Aotus trivirgatus)

Smith, Karen Kaye; Parham, Peter; Nancy, Starobinas

doi:10.1007/bf00345620

Cited by 7 publications

(1 citation statement)

References 18 publications

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“…Conversely, true ,n2m alleles have been described in mice, with a polymorphism in position 85 [21,22]. A genetic polymorphism has also been suggested in monkeys but the two forms have not been sequenced [23]. In guinea pigs [24], two forms of fl2m proteins have been described, the more acidic one being derived from the other by proteolytic cleavage between residues 98 and 99.…”

Section: Discussionmentioning

confidence: 99%

Molecular variants of β2-microglobulin in renal insufficiency

Vincent

Dennoroy²,

Révillard

1994

Biochemical Journal

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Many patients with renal insufficiency treated by dialysis for more than 10 years have tissue deposits of amyloid material containing polymerized beta 2-microglobulin (beta 2m). The mechanisms of beta 2m polymerization and degradation remain unknown. In biological fluids (serum and urine) from haemodialysis patients and in dialysis fluids from patients treated by chronic ambulatory peritoneal dialysis (CAPD), we have characterized different molecular forms of beta 2m, including proteolytic split products. beta 2m isoforms of pI 5.7, 5.3 and 4.5-5.0 were isolated from urine and CAPD fluid. The pI 5.3 beta 2m, but not the other forms, was recovered both as monomers and as dimers. Such dimers were also detected in serum from patients but not from healthy controls. pI 5.3 and 5.7 beta 2m isoforms were found to be nearly identical by mass spectrometry and by their amino acid sequences. The amino acid sequence of the 43 N-terminal amino acids of beta 2m of pI 5.0 showed identity with the corresponding region of pI 5.7 beta 2m. Fragments recovered from CAPD fluid were similar to proteolytic fragments generated from pure pI 5.7 beta 2m by incubation in mouse ascitic fluid at acidic pH. Furthermore, pure pI 5.7 beta 2m was converted into more acidic forms of 12 kDa upon incubation in mouse ascitic fluid at acid pH. beta 2m dimers found in serum may represent a precursor of amyloid fibrils.

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Section: Discussionmentioning

confidence: 99%

Molecular variants of β2-microglobulin in renal insufficiency

Vincent

Dennoroy²,

Révillard

1994

Biochemical Journal

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Major histocompatibility complex class I molecules of nonhuman primates

et al. 1988

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The usefulness of nonhuman primates in immunologically relevant research has until now been limited by difficulties in characterizing the major histocompatibility (MHC) gene products of these species. We have now biochemically characterized the MHC-encoded class I molecules from four different species of nonhuman primates using antibodies directed against human MHC class I structures and one-dimensional isoelectric focusing (1-D IEF). We demonstrated the functional relevancy of this technique of MHC typing by generating virus-specific cytotoxic T cells and assaying their cytotoxic activity against a panel of virus-transformed cells that expressed the same or differing class I structures. Only virus-infected cell lines expressing MHC class I antigens identical to those of the cytotoxic T lymphocyte population were lysed. This simple method of MHC class I typing using 1-D IEF will be useful in immunological research involving nonhuman primates and in nonhuman primate colony management.

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MHC Class I Genes in Nonhuman Primates

Cadavid¹,

Watkins²

1997

Molecular Biology and Evolution of Blood Group and MHC Antigens in Primates

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Two distinct forms of ? 2-microglobulin in different races of owl monkey (Aotus trivirgatus)

Cited by 7 publications

References 18 publications

Molecular variants of β2-microglobulin in renal insufficiency

Molecular variants of β2-microglobulin in renal insufficiency

Major histocompatibility complex class I molecules of nonhuman primates

MHC Class I Genes in Nonhuman Primates

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