Polyclonal antibodies were raised to synthetic amino acid sequences of the bovine GABAA receptor q-and as-subunits and purified by affinity chromatography on a column coupled with the respective peptide. Anti-peptide %(41&424) and anti-peptide aJ459-467) antibodies immunoprecipitated GABAA receptors and recognized a protein of 53 kDa (PJ and 59 kDa (P& respectively, in Western blots of GABAA receptors purified from the brains of 5-10 day old rats. P,, as well as P,, are specifically photolabeled by PHlflunitrazepam and are recognized by the a-subunit specific monoclonal antibody bd 28.
Genetically diabetic mice (db/db) were given 50 mg/kg body weight/day substance L, a nontoxic basic amino acid and compared to control diabetic mice without treatment. The oral administration of the compound was started at the age of 3 months and the animals were sacrificed at the age of 7 months. No adverse effects were observed in animals given the substance L. Total food consumption, drinking water intake and body weight were comparable between the groups. Nonenzymatic glycosylation of serum proteins and hemoglobin was not significantly different in the groups. Renal pathological lesions in the control diabetic mice showed glomerular mesangial expansion and on electron microscopy thickened glomerular basement membranes with a mean thickness of 3,204 ± 186 Å. Treated animals showed significantly less mesangial crescents and thinner glomerular basement membrane thickness of 2,520 ± 252 Å (p < 0.01). The experimental animals showed in addition a lower mean kidney weight. Glomerular but not tubular proteinuria was reduced in the treated group. Basement membrane collagen type IV isolated from kidneys of experimental animals was more soluble in acidity and showed a lower degree of cross-linking as evaluated by SDS-polyacrylamide gel electrophoresis. We conclude that substance L is beneficial to diabetic renal changes. We suggest that this positive effect could be due to the inhibition of glucose-mediated abnormal cross-linking of collagenous structures by the interaction of substance L with reactive carbonyl residues of glycosylation adducts of collagen. Other possible mechanisms are discussed.
SummaryA new mutation, affecting skin and hair, occurred in an expansion colony of Him:OFl mice. Test crosses showed that a single autosomal recessive gene was responsible for this trait. Homozygotes have sparse greasy fur and lower viability and fertility than normal littermates. Histological observations showed hypertrophy of sebaceous glands, hyperkeratosis, parakeratosis, acanthosis and signs of inflammation. The disease was named 'inherited seborrheic dermatitis' and the gene name seb is proposed.
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