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T R Anderson

Publications and source records attributed to T R Anderson.

At least 37 records · Page 2Linked to original sources
PubMed1984

Prolactin's mitogenic action on the pigeon crop-sac mucosal epithelium involves direct and indirect mechanisms.

It has long been known that prolactin (PRL) induces proliferation of the mucosal epithelial lining of the pigeon crop-sac. This system was used to study possible interactions of other hormones with PRL's mitogenic effect directly on the crop-sac cells. Injection of a sheep pituitary powder into the loose skin between the leg and abdomen of pigeons increased the responsiveness of the crop-sac to direct, local application of PRL. Similar systemic injections of anterior pituitary hormones, ACTH and TSH (alone or together), or a combination of LH and FSH, were without effect on the local response to PRL. However, systemically injected PRL and GH resulted in a dramatic augmentation of the response of the organ to local injection of PRL. PRL was more potent than GH in this regard. These results suggest that PRL has at least two modes of action as a mitogen on this epithelium--its well-known direct action on the cells and an indirect action as well that is possibly mediated by the secretion of another factor into the blood stream. Because it was previously found that somatomedin-like molecules, including proinsulin, act synergistically with PRL to promote proliferation of these cells when coinjected locally with PRL (T. R. Anderson, J. Rodriguez , D. S. Pitts , E. M. Spencer, and C. S. Nicoll , 1983, In "Insulin-like Growth Factors/Somatomedins," de Gruyter , Berlin), The effects of systemic injections of proinsulin were also tested. Proinsulin had a potentiating effect similar to that of the pituitary powder and of GH or PRL. These results are consistent with the following interpretations: When PRL promotes crop-sac proliferation to produce crop-milk in pigeons and doves, the hormone acts through at least two mechanisms. One of these is a direct effect on the crop-sac, which sensitizes the mucosal epithelium to the mitogenic action of a somatomedin-like growth factor. The second effect is an increase in the production and/or secretion of the factor, which then acts synergistically with PRL to promote proliferation of the crop-sac mucosal cells. More direct evidence for this proposal was provided by the finding that serum from saline- or PRL-treated pigeons did not stimulate crop-sac mucosal growth when it was injected locally. However, the serum from PRL-treated birds had a much higher level of an activity that augmented the effects of PRL when the sera were locally injected in combination with PRL.(ABSTRACT TRUNCATED AT 400 WORDS)

Animals↗
PubMed1983

Inhibition by dithionite and reactivation by iron of the tartrate-resistant acid phosphatase in bone of osteopetrotic (ia) rats.

The staining intensity and inhibitor sensitivity of acid phosphatase activity was determined histochemically in various tissues of normal and ia rat pups by the use of freeze-dried whole body sections. Activity was determined using alpha-naphthylphosphate as substrate and hexazonium pararosaniline as coupler. Sections from ia rats (6 and 24 days old) showed markedly higher enzyme activity in bone than sections from normal littermates. However, there were no differences between ia and normal pups in acid phosphatase activity in soft tissues and developing teeth. Preincubation of sections with 1-100 mM sodium dithionite (an iron-binding agent) caused a dose-related inhibition of enzyme activity in bone of ia and normal pups, but only slight inhibition of activity in soft tissues. Partial restoration of the dithionite-inhibited activity in bone was achieved by subsequent preincubation in 1 mM FeCl2. Addition of 100 mM sodium tartrate to the staining solution of non-preincubated sections caused almost complete inhibition of activity in soft tissues and the developing teeth but no inhibition of the activity in bone that was sensitive to sodium dithionite. These data indicate a) that sodium dithionite can be used as a specific histochemical inhibitor of the tartrate-resistant acid phosphatase and b) that the source of increased acid phosphatase activity in bone from ia rats is mostly from the tartrate-resistant acid phosphatase.

Acid Phosphatase↗
PubMed1982

Effects of iron and ascorbic acid on acid phosphatases of the enamel organ of rat molars.

Protein extracts from 6- to 11-day-old rat enamel organs were applied to columns of carboxymethyl-52 cellulose. Protein eluted from the columns was assayed for acid phosphatase activity with substrates para-nitrophenylphosphate (p-NPP), beta-glycerolphosphate (beta-GP), ATP and phosphocasein. A weakly-bound peak of activity (A) emerged first which was insensitive to stimulation by iron and ascorbic acid. This enzyme hydrolysed only the phosphomonoester substrates (p-NPP and beta-GP). A strongly bound peak of activity (B) emerged later and was completely separated from the first activity. It hydrolysed all substrates except beta-GP, and was stimulated at least 10-fold by 0.1 mM ferrous ion (Fe2+) in the presence of a strong reducing agent (1.0 mM ascorbic acid). Both substances were more effective as stimulators when used together than they were when each was used separately. Dependency on these co-factors for the development of full activity increased with purification, especially when phosphocasein was substrate. The results were similar for each age of rat used. These properties of enzyme B are parallel with those of the acid phosphoprotein phosphatases of liver and spleen, and the tartrate-resistant acid phosphatase of rat bone. We conclude that enzyme B requires iron and a reducing agent for full activity and has properties that distinguishes it from the classical acid phosphatases (E.C. 3.1.3.2.).

Acid Phosphatase↗
PubMed1982

Separation and partial purification of acid phosphates of the enamel organ of rat molars.

At least two types of acid phosphatases with markedly different properties were separated from the enamel organ of rat molar tooth buds. One enzyme (A) bound weakly to the CM-cellulose column and was eluted with a combined linear salt and pH gradient; another enzyme (B) bound strongly to the column and was eluted with a second linear salt gradient at constant pH. Enzyme A was identified as a phosphomonoester hydrolase (3.1.3.2) similar to the lysosomal enzyme of soft tissues and the tartrate-sensitive enzyme of bone. Enzyme B did not hydrolyse aliphatic monophosphate ester substrates but, like enzyme A, it did split the aryl monophosphate ester substrate, para-nitrophenylphosphate, as well as the phosphate esters of casein and the acid anhydride substrates, ATP and inorganic pyrophosphate. This enzyme is similar to the low molecular weight tartrate-resistant acid phosphatases of bone and soft tissues.

Acid Phosphatase↗
PubMed1982

Paraplegic use of the Orlau swivel walker: case report.

This case report describes the characteristics, biomechanics, fitting, training, advantages, and disadvantages of the Orlau swivel walker. Advantages of the walker include stability, easy mobility, and the ability of the wearer to ambulate with free hands. Disadvantages include slow velocity of locomotion, comparative metabolic inefficiency, awkwardness of getting into and from the standing position, and inability to be used on uneven surfaces. In a comparison of the metabolic costs and efficiency of the Orlau swivel walker, bilateral knee-ankle-foot orthoses, and a wheelchair, the swivel walker was least efficient (1.9ml O2/kg/m) in comparison to the knee-ankle-foot orthoses (0.9ml O2/kg/m) and the wheelchair (0.18ml O2/kg/m). However, in evaluating a means of locomotion, various factors besides metabolic costs need to be considered; these include efficiency, velocity, the physiologic and psychologic benefits of standing, and the patient's needs. When considering all these factors for an individual patient, the swivel walker may be an effective device for meeting the needs of many individuals with spinal cord injury.

Adult↗
PubMed1981

Cyclic nucleotides and the control of epithelial cell proliferation: cyclic CMP may be a partial mediator of the response of the pigeon crop-sac to prolactin.

The possible role of cyclic nucleotides as second messengers mediating hormone-induced cellular growth in vivo was investigated using the proliferative response of the pigeon crop-sac mucosal epithelium to prolactin (PRL) as a model system. Local injections of cAMP, cCMP, cGMP, cTMP or cUMP alone over the prolactin-responsive cells had no mitogenic effect. When injected along with a small dose of PRL, cAMP at doses above 1 micromole inhibited the response by 10%. While cGMP at a dose of 10 micromoles augmented the response by 47%. In fact, cCMP gave a log-linear dose-response relationship with significant augmentation of the response to PRL observed with doses as low as 0.01 micromole. Cyclic UMP, cTMP and various 5'-nucleotide monophosphates had no effect on the response to the hormone. When the dibutyryl analogs of the cyclic nucleotides were tested for their ability to potentiate the response to PRL, only dibutyryl cCMP was effective. These data suggest that cCMP may be a partial mediator of the proliferative action of PRL in this system, but it is probably not the sole second messenger for prolactin's action in these cells. Our results also indicate that failure of a cyclic nucleotide to mimic a hormone-induced response by itself does not prove that the compound is uninvolved in the hormones's action.

Animals↗
PubMed1979

Purification and partial characterization of two acid phosphatases from rat bone.

Acid phosphatase activity in homogenized tibiae and femora of suckling rats was extracted with 0.3M KCl and 0.1% Triton X-100. A high-speed supernatant was treated with protamine sulfate, dialyzed, and chromatographed on CM-52 cellulose. All of the acid phosphatase activity was eluted with a sodium acetate buffer and combined ionic strength-pH gradient into two peaks (E1 and E2). Both enzyme peaks were further purified with Sephadex G-200, which resulted in 700- and 1000-fold purification for E2 and E1, respectively. A total of 220 units (mumoles substrate/min) of E2 with a specific activity of 160 units/mg protein has been obtained in one run by this procedure. E1 has a high molecular weight (greater than 100,000) and shows preference for monophosphate ester substrates, is markedly inhibited by tartrate, and has a pH optimum near 5. E2 has a lower molecular weight (greater than 40,000) and shows negligible activity with monophosphate esters [except with p-nitrophenyl phosphate (p-NPP)], but high activity with ADP and ATP. E2 is unaffected by tartrate and shows a pH optimum near 6. Both enzymes are competitively inhibited by inorganic phosphate, and E2, but not E1, is markedly inhibited by p-chloromercuribenzoate. With p-NPP as substrate, E1 and E2 have distinctly different values for Km. E1 appears similar to the high molecular weight acid phosphatases of soft tissues. However, E2 appears to differ from the low molecular weight phosphatases in soft tissues with regard to substrate specificity.

Acid Phosphatase↗
PubMed1977

Chromatographic separation of two acid phosphatases from rat bone.

Extracts of tibiae of suckling rats were prepared with 0.3 M KCl containing 0.1% Triton X-100 and were chromatographed with CM-52 cellulose. Most of the acid phosphatase activity determined with p-nitrophenylphosphate (p-NPP) was bound to the cellulose and could be eluted with a sodium acetate buffer gradient in 2 distinct peaks. The major peak, E2, was bound strongly to the cellulose and showed high activity with p-NPP and inorganic pyrophosphate (P-Pi), but only slight activity with beta-glycerophosphate (beta-GP) and was unaffected by tartrate. The minor peak, E1, was weakly bound to the adsorbent, showed equal activity with p-NPP and beta-GP, but negligible activity with P-Pi and was completely inhibited by tartrate. These results support earlier evidence suggesting that bone contains at least 2 different acid phosphatases and that the more abundant enzyme may function as a pyrophosphatase.

4-Nitrophenylphosphatase↗
PubMed1976

Effects of prenatal reserpine administration on development of the rat adrenal medulla and central nervous system.

Reserpine (1 mg/kg s.c.) was administered to pregnant rats at different periods of gestation. Rats born to mothers who received reserpine on days 6, 5 and 4 or 4, 3 and 2 before delivery showed early postnatal adrenal catecholamine depletion, an effect which can be attributed to a direct action of the drug; however, at no time was induction of tyrosine hydroxylase or dopamine beta-hydroxylase observed. Administration of reserpine on days 9, 8 and 7 before delivery did not alter postnatal adrenal catecholamine levels in the offspring but produced permanent elevations in enzyme activities and vesicular amine uptake beginning at 10 days of age. Studies utilizing direct stimulation with nicotine indicated that the inherent responsiveness of the adrenal medulla itself was the same in control and reserpine-exposed pups. These data all suggest that sympathoadrenal tone has been permanently increased in the offspring of rats which have been exposed to reserpine early in gestation. In the brain, administration of reserpine on days 6, 5 and 4 before delivery resulted in a delay in early postnatal development of brain weight and synaptosomal uptake mechanisms, and at later stages subnormal tyrosine hydroxylase activities. When reserpine was given on days 9, 8 and 7 before delivery, only the deficiency in tyrosine hydroxylase was seen. These studies indicate that long-lasting changes in both peripheral and central nervous system catecholamine disposition can be produced by prenatal reserpine administration.

Adrenal Medulla↗