Expansion of humoral donor-specific alloreactivity after renal transplantation correlates with impaired graft outcome.

IgG human leukocyte antigen (HLA) antibodies were investigated retrospectively after transplantation in 264 primary renal graft recipients. All patients who developed de novo donor-specific antibodies (DSA) and non-DSA (NDSA) (n = 40, 15.1%) were divided into two groups. Group A consisted of patients (n = 20) with stable good graft function (GGF), and group B consisted of patients (n = 20) who developed rejection and/or graft failure (R/GF). DSA were detected in 23 patients (57.5%). Expansion of humoral alloreactivity with the presence of DSA to more than one graft mismatched antigens and coexistence of HLA class I and II DSA were significantly correlated only with R/GF (p = 0.01). Limitation of alloreactivity to one graft-mismatched antigen was detected mainly in patients with GGF. HLA-DQ DSA alone was found only in patients with GGF (p = 0.1). No significant differences were found between the two patient groups with NDSA. Expansion of the humoral alloreactivity to more than one graft molecule in renal transplant recipients identifies patients at high risk of rejection or graft failure. Limitation of humoral alloreactivity to one graft antigen perhaps associates the presence of regulatory mechanisms with GGF only in specific cases.

A high mobility group protein from the Dipteran insects Ceratitis capitata and Bactrocera oleae.

Nuclei from Bactrocera oleae and Ceratitis capitata larvae contain a major protein that shares most of the characteristics of vertebrate high mobility group (HMG) proteins. Proteins are extracted from nuclei with 0.35 M NaCl, are soluble in 5% perchloric acid, are relatively small (molecular weight in the range of 10-16 kDa), and have both a high basic and a high acidic amino acid content. The amino acid constitution of these proteins is similar to that of the HMGB protein family of vertebrates. The proteins cross-react with antibodies raised against the HMGD chromosomal protein of Drosophila melanogaster. The possible relatedness of these proteins to high mobility group proteins is discussed.

High mobility group-like proteins of the insect Plodia interpunctella.

Nuclei from Plodia interpunctella larvae contain four major proteins, which are extracted by 5% perchloric acid and 0.35 M NaCl. The proteins have been designated PL1, PL2, PL3, and PL4. The amino acid analyses of these proteins show that they have high proportions of acidic and basic amino acid residues, a property characteristic of the high mobility group (HMG) proteins isolated from vertebrate tissues. Immunological characterication of these proteins clearly shows that PL1, PL2, and PL4 are more closely related to HMG1 dipteran proteins, while PL3 is more closely related to HMG1 dipteran proteins. The possible relatedness of these proteins to HMG proteins is discussed.

A mini review of the high mobility group proteins of insects.

High mobility group (HMG) proteins are an abundant class of chromosomal proteins facilitate assembly of higher order structures. The mammalian HMG proteins have been grouped into three distinct families on the basis of their characteristic functional sequence: the HMGB, the HMGN, and the HMGA family. The HMG proteins of Drosophila melanogaster and Chironomus tentans are the best characterized dipteran insect HMG proteins. Three abundant members of this group of nonhistone proteins were detected in those insects. Two of them belong to the HMGB family and one to the HMGA family. The possible relatedness of these proteins to the formation of higher order nucleoprotein structures and their possible role in the regulation of transcription is discussed.

Presence of alpha1-antitrypsin and transferrin in human follicular fluid--correlation with fertilization.

We purified two proteins with molecular masses of approximately 50 kDa and 80 kDa with N-terminal sequences similar to those of alpha1-antitrypsin (a1AT) and transferrin indicating that they are identical to or highly homologous to these proteins. Proteins from human follicular fluid were purified after ammonium sulfate fractionation followed by water dialysis and High Performance Liquid Chromatography. The fraction of peak 3 showed a single band on electrophoresis and its N-terminal amino acid sequence was similar to that of human serum transferrin. The fraction of peak 10 proved to be a glycoprotein and its N-terminal amino acid sequence was similar to that of human serum a1AT. There are indications that transferrin may be involved in the fertilization process. Sperm motion was assessed employing computer-assisted semen analysis. The addition of purified protein to prepared sperm samples from normospermic men significantly increases the straight-line velocity (VSL), the amplitude of lateral head displacement (ALH) and the number of progressively motile sperm. a1AT does not seem to have a stimulatory effect on sperm motility.