Inhibition of long-acting thyroid stimulator by thyroid particulate fractions.

Beall, Gildon N.; Solomon, David H.

doi:10.1172/jci105369

Cited by 57 publications

(19 citation statements)

References 17 publications

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“…When the microsome fraction was solubilized by sonification, absorption was evident in the supernatant and precipitate. These results differ, for unknown reasons, from those in the report of Beall and Solomon (1966b) sonication. Deoxycholate solubilized microsomal fraction was salted out by 45% saturated potassium phosphate buffer.…”

Section: Absorption Of Lats By Thyroid Cell Fractionscontrasting

confidence: 99%

“…It is interesting that the assay response to LATS still showed a "long acting type," in spite of a diminished thyroid stimulating activity due to partial denaturation of LATS molecule. Beall and Solomon (1966b) showed that thyroid microsomes absorbed both LATS and TSH. Dorrington, et al (1966b) observed that the thyroid microsomal fraction absorbed LATS, but could not demonstrate absorption of human TSH, either by thyroid homogenates or subcellular particles.…”

Section: Immunofluorescent Localization Of Latsmentioning

confidence: 99%

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Comparative Studies on the Properties of LATS and TSH

Ochi

DeGroot

1970

Endocrinol Japon

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LATS activity was neutralized by pretreatment of mice with anti-IgG in vivo. Simultaneous injection of epsilon-amino caproic acid and hydrocortisone does not inhibit LATS action. Human thyroid-microsomal fractions neutralize LATS activity and TSH activity. The decrease in activity of LATS and TSH caused by thyroid microsomes correlates positively. Calf thyroid microsomes are much less active than human thyroid microsomes in absorbing LATS activity. Deoxycholate and sonification solubilize the LATS neutralizing activity. No visible precipitate formed between these solubilized fraction and LATS-IgG, using the Ouchterlony agar diffusion method. LATS did not differ from TSH in heat stability, and partially heat denatured LATS still had a long acting type response. Dissociation of a small rapidly acting molecule from LATS could not be obtained in high molar NaCI solution. LATS-IgG fragments digested by proteolytic enzymes (papain, pepsin, trypsin, and ficin) had a prolonged response like LATS. However, these fragments, in the presence of cysteine, either gave the same response after 2 hr and 8 hr, or gave a short acting response like TSH. The thyroid stimulating active site of the LATS active gamma globulin may be situated in Fab or Fab fragments having the antibody combining site. LATS did not stimulate the chicken thyroid, although TSH had this action. The proteolytic fractions of LATS-IgG also did not stimulate the chicken thyroid. No increase of gammaglobulin and/or IgG was found in some sera with a high LATS activity. Binding of LATS-IgG to mouse or human thyroid could not be visualized using the Coon's immunofluorescent method. These data support the concept that LATS is an IgG having a high specific activity of thyroid stimulating action.

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Section: Absorption Of Lats By Thyroid Cell Fractionscontrasting

confidence: 99%

Section: Immunofluorescent Localization Of Latsmentioning

confidence: 99%

Comparative Studies on the Properties of LATS and TSH

Ochi

DeGroot

1970

Endocrinol Japon

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“…Beall and Solomon (1966) reported reasonably the consistent inactivation of TSH by human thyroid particulate fraction.…”

Section: Resultssupporting

confidence: 59%

Inactivation of human thyroid stimulator by human thyroid extract.

1979

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“…In contrast, Berumen, Lobsenz, and Utiger found no inhibition of LATS by fractions of liver, kidney, or muscle (29). Furthermore, Beall and Solomon found microsomes of these tissues, as well as those of the pancreas, adrenals, and lymph nodes, to be inactive (30).…”

Section: Resultsmentioning

confidence: 98%

In vitro stimulation by long-acting thyroid stimulator of thyroid glucose oxidation and 32P incorporation into phospholipids

Field¹,

Remer²,

Bloom³

et al. 1968

J. Clin. Invest.

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AB s T R A C T Long-acting thyroid stimulator (LATS) increased glucose oxidation and 32P incorporation into phospholipids in in vitro experiments with dog thyroid slices. The time course of the response was different from that obtained with thyroid-stimulating hormone (TSH), but was very similar to the delayed effect observed in vivo. During a 45 min incubation, TSH, but not LATS increased glucose oxidation, whereas in longer experiments up to 6 hr, both substances augmented 14CO2 production. Amounts of pooled human gamma globulin equivalent to LATS were inactive. Although TSH stimulated 32P incorporation into phospholipids during a 2 hr incubation, LATS was ineffective. In longer incubations, from 41 to 8 hr. LATS did increase 32P incorporation.The stimulatory effect of LATS was not abolished by anti-TSH antibody capable of neutralizing human TSH. Effects of LATS were also obtained with beef and pig thyroid slices. In addition to stimulation of glucose oxidation in dog thyroid slices, LATS occasionally also stimulated glucose oxidation in dog spleen and liver slices. Despite a 54-fold increase in LATS concentration, a satisfactory dose-response curve could not be demonstrated when 14C02 production was measured.

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Inhibition of long-acting thyroid stimulator by thyroid particulate fractions.

Cited by 57 publications

References 17 publications

Comparative Studies on the Properties of LATS and TSH

Comparative Studies on the Properties of LATS and TSH

Inactivation of human thyroid stimulator by human thyroid extract.

In vitro stimulation by long-acting thyroid stimulator of thyroid glucose oxidation and 32P incorporation into phospholipids

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