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Biomedical subjects

R Herrera

Publications and source records attributed to R Herrera.

At least 73 records · Page 4Linked to original sources
PubMed1984

Advanced prostatic adenocarcinoma: biological aspects and effects of androgen deprivation achieved by castration or agonistic analogues of LHRH.

Twenty-nine patients with advanced prostatic adenocarcinoma were evaluated clinically, biochemically and radiologically and randomly assigned either to orchiectomy or to medical treatment. The latter consisted of the chronic administration of an LHRH agonistic analogue by parenteral and/or intranasal routes. Plasma testosterone levels fell to castrate values and remained so for as long as the follow-up lasted (24 months); estrogen levels fell as well. No change in basal cortisol, thyroxine or prolactin levels was noticed. A decrease in prostate size and improvement in prostatism occurred in all. Bone pain and radiology conventionally or by isotopic scanning, did not parallel the improvement seen in the primary disease locus. Similarly, the changes in alkaline phosphatase were minimal when compared to that of prostatic acid phosphatase. Both enzymes increased prior to or concurrently with relapse of the disease. The longest remission and survival was seen in patients with low enzyme levels, non diffuse bone metastases and high degree of tumor differentiation. Chronic use of agonistic analogues of LHRH induces effective castration in men with prostatic carcinoma and can replace orchiectomy or estrogen administration. The quantitative analysis of androgen receptors (AR) in subcellular fractions of tumor cells; the use of techniques to enhance the number of AR in the cytosol; and the determination of the type II/I regulatory subunit of protein kinase may be used to identify hormone independent clones and spare patients of unnecessary procedures.

Acid Phosphatase↗
PubMed1984

Insulin receptor is an insulin-dependent tyrosine protein kinase: copurification of insulin-binding activity and protein kinase activity to homogeneity from human placenta.

The insulin-binding activity and insulin-dependent tyrosine protein kinase activity of the insulin receptor have been purified 2000-fold to homogeneity from human placental membranes. The purified receptor has one high-affinity binding site for insulin per mol of receptor. Its Vmax for phosphorylating angiotensin is 80 nmol of phosphate per min per mg of protein at 23 degrees C. The procedure used to purify the receptor includes chromatography on wheat germ agglutinin-agarose and on insulin-Sepharose. The purified receptor was eluted from insulin-Sepharose with 0.5 M NaCl and 1 mM dithiothreitol at pH 5.5. The addition of dithiothreitol was essential for recovery of the protein kinase. A silver-stained gel of the reduced purified receptor showed two major bands, Mr 95,000 (beta subunit) and Mr 135,000 (alpha subunit). The component of Mr 95,000 comigrated with the autophosphorylated beta subunit of the receptor. The latter was phosphorylated exclusively on tyrosine residues by an intramolecular process. In the presence of insulin, approximately 2 mol of phosphate was incorporated per mol of beta subunit. Two major beta subunit tryptic phosphopeptides were resolved by high-pressure liquid chromatography after autophosphorylation of the purified receptor in the presence or absence of insulin. It is concluded that the insulin binding and the insulin-dependent protein kinase are intrinsic components of the same oligomer since (i) they copurify to homogeneity, (ii) the purified receptor protein kinase is immunoprecipitated by polyclonal and monoclonal antibodies to the human insulin receptor, and (iii) phosphorylation of the beta subunit of the receptor occurs by an intramolecular reaction.

Female↗
PubMed1983

Phosphorylation activates the insulin receptor tyrosine protein kinase.

Preparations of insulin receptor from cultured 3T3-L1 adipocytes and human placenta previously was found to catalyze the phosphorylation of the 90,000-dalton component of the insulin receptor on tyrosine residues. This insulin-dependent phosphorylation has now been shown to coincide with the generation of an activated, insulin-independent, receptor protein kinase. Activation is dependent upon ATP, divalent cations (Mg2+ and Mn2+), and insulin (half-maximal activation occurs at 6-8 nM insulin). The time required for activation is consistent with that needed for insulin-dependent self-phosphorylation of the receptor present in eluates from wheat germ lectin-agarose columns and in preparations of affinity-purified placental receptor. Activation proceeds unabated in the presence of soybean trypsin inhibitor at 0.1 mg/ml and the activated, insulin-independent, protein kinase sediments in 5-20% sucrose gradients at the same position as the unmodified receptor. Under steady-state conditions, the phosphorylated receptor binds insulin in the same fashion as the unmodified receptor. It is proposed that the self-phosphorylated form of the receptor is the insulin-activated protein kinase that catalyzes the phosphorylation of exogenous protein and peptide substrates. A corollary of this hypothesis is that enzymatic dephosphorylation may be essential for reversibly terminating the activity of the insulin-receptor protein kinase.

Adenosine Triphosphate↗
PubMed1980

[Technic and indication for controlled ultrafiltration].

The isolated ultrafiltration with commercial dialysators gives a possibility of the massive dehydration in a short time without disturbing the well-being of the patient. If in patients undergoing a dialysis a following haemodialysis (sequential ultrafiltration haemodialysis) is necessary, particularly in patients with acute complications hypotonic circulatory conditions may develop. An infusion of a fourfold concentrated human dry plasma during the ultrafiltration may prevent these hypotensions, since reduction of osmolality and losses of circulation-effective substances are prevented during haemodialysis. With the help of this kind of treatment conditions of hyperhydration of different genesis may be removed also in patients with inclination to hypotension.

Acute Kidney Injury↗
PubMed1978

Significance of leaf orientation for leaf temperature in an Amazonian sclerophyll vegetation.

The influence of leaf orientation on leaf temperature has been studied in an sclerophyll vegetation of the Amazon basin, which grows on white sandy soils of very low water retention capacity and variable depth of the water table. Leaf size of the species studied is mainly mesophyllous (sensu Raunkiaer). The high degree of leaf inclination in all species is very characteristic; 55% of the leaves present inclination angles (relative to the vertical) smaller than 45 degrees. Water potential is generally high, not being lower than -14 bars. Leaf resistance increases toward noon during the course of sunny days, indicating either water stress at leaf level or the influence of low relative humidity on stomata opening. Leaf temperature under sunny conditions reflects the influence of leaf orientation on the amount of radiation absorbed by the leaf. Temperature differences recorded range from 1.8--5.4 degrees C. The difference depends on leaf angle, leaf color and leaf diffusion resistance during the period of measurement. Analysis of the relationship between leaf angle and leaf temperature, using Gates leaf energy balance, shows that under the conditions prevailing at noon in sunny days, leaf angles smaller than 50 degrees are effective in reducing leaf temperature within a wide range of leaf resistances to water vapor transfer.

Ecology↗