Gene Literature Dashboard

A child was brought to us with multiple anomalies. On examination we found an interstitial deletion in the long arms of chromosome 1. We studied genetic and chromosome markers, comparing our clinical and cytogenetic findings with other reported cases of chromosome 1 interstitial deletion.

Polyestradiol phosphate (PEP) has been used for localization of estrogen receptors in human carcinoma. The nature of PEP binding to the receptor molecule and the ability of antiestradiol antibodies to react with estrogen receptor complexes were investigated, using an animal model system. Castrated adult female rats were injected with PEP, estradiol 17 beta-diethylstilbestrol or saline. An estrogen target organ (uterus) and a non-target organ (diaphragm) were removed from each animal. In each organ, unoccupied cytosolic estrogen receptors were quantified by DCC assay. The tissue sections were processed to ascertain the PEP binding and the ability of antiestradiol antibodies to detect hormone-occupied sites. Comparison of the results obtained by DCC assay and immunohistochemical technique revealed that antiestradiol antibodies do not react with estradiol receptor complexes formed in vitro or in vivo; that PEP cannot compete with estradiol for the receptor sites in vitro; and that PEP binds to proteins other than those measured by DCC as receptor molecules having high affinity for estradiol.

Studies were done to define the coagulation defect that develops in hemodynamically stable anesthetized dogs perfused on our arteriovenous extracorporeal system without added heparin. After 45 min, the dogs developed whole blood clotting times (WBCT) greater than 24 h. There was an associated decrease in ADP-induced platelet aggregation and a drop in factor V, VIII, and X levels of 75.8, 33.5, and 46.8%, respectively. Despite an increase in fibrinogen degradation products, there was no significant change in fibrinogen level or platelet count. An inhibitor of thrombin and factor Xa clotting of plasma appeared that was "heparinlike", because it stimulated the inactivation of factor Xa by antithrombin III (ATIII) but not by O-methyl isoureamodified ATIII. Thrombin inhibition by ATIII was also stimulated. The inhibitor was heat stable, adsorbed by BaSO4, and neutralized by protamine. Infusion of protamine sulfate into two perfused dogs neutralized the inhibitor and brought the WBCT from greater than 24 h to less than control. Six dogs developed inhibitor levels equivalent to 0.98 to 6.15 U/ml heparin. Five eviscerated dogs in which the hepatic artery was ligated developed peak plasma inhibitor levels of 3.2 +/- 1.0 U/ml. Thus, the endogenous heparinlike inhibitor is a major contributor to the anticoagulated state induced with our perfusion system and may have an extrahepatic origin.

A nonhistone chromosomal protein (D-55) of Mr 55000 has been isolated in homogeneous form from calf thymus by using the standard salt-extraction procedures for the isolation of nonhistone chromosomal proteins followed by hydroxyapatite chromatography. D-55 is further characterized as coming from the group of nonhistone chromosomal proteins easily phosphorylated by an endogenous nuclear protein kinase. The kinase incorporates 1 mol of phosphate per mol of protein from [gamma-32P]ATP. The unphosphorylated form of D-55 binds to DNA, histones, and nucleosomes. Phosphorylation of D-55 does not significantly alter the binding of D-55 to DNA but greatly enhances its binding to histones and nucleosomes. Binding of D-55 to reconstituted nucleosomes enhances transcription of the nucleosome DNA by E. coli RNA polymerase by approximately 100-fold, to a level approximately 4 times that observed with naked calf thymus DNA as template. Phosphorylation of D-55 abolishes this enhancement. Binding of D-55 produces no apparent alteration in nucleosome structure as assayed by nuclease digestion patterns. In contrast, phospho-D55 alters nucleosome structure significantly.