Influence of proteinase inhibitors on glucocorticoid receptor properties: recent progress and future perspectives

Hubbard, John R.; Kalimi, Mohammed

doi:10.1007/bf00220777

Cited by 13 publications

(3 citation statements)

References 40 publications

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“…We conclude that protease inhibitors and Na2Mo04 not only stabilize the steroid-binding proteins (receptors) but yield more stable preparations of nontransformed receptors. Thus our work concurs with that of Hubbard and Kalimi (1985) that protease inhibitors block dissociation of receptors.…”

Section: Discussionsupporting

confidence: 93%

A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors

Tai¹,

Maeda²,

Nakao³

et al. 1986

Biochemistry

239

109

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Section: Discussionsupporting

confidence: 93%

A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors

Tai¹,

Maeda²,

Nakao³

et al. 1986

Biochemistry

239

109

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“…Protease inhibitors and substrates were found to inhibit steroid molecules binding to their cognate receptors (Baker et al 1978;Hubbard and Kalimi 1985;Puca et al 1986). These findings have been extended for TRs, showing that various protease inhibitors and protease substrates inhibit T 3 binding to nuclear TRs (Brtko et al 1993).…”

Section: From T 3 Binding Sites In Nucleus To T 3 Receptorsmentioning

confidence: 99%

Thyroid hormone and thyroid hormone nuclear receptors: History and present state of art

Brtko

2021

Endocrine Regulations

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The present review traces the road leading to discovery of L-thyroxine, thyroid hormone (3,5,3´-triiodo-L-thyronine, T3) and its cognate nuclear receptors. Thyroid hormone is a pleio-tropic regulator of growth, differentiation, and tissue homeostasis in higher organisms. The major site of the thyroid hormone action is predominantly a cell nucleus. T3 specific binding sites in the cell nuclei have opened a new era in the field of the thyroid hormone receptors (TRs) discovery. T3 actions are mediated by high affinity nuclear TRs, TRalpha and TRbeta, which function as T3-activated transcription factors playing an essential role as transcription-modulating proteins affecting the transcriptional responses in target genes. Discovery and characterization of nuclear retinoid X receptors (RXRs), which form with TRs a heterodimer RXR/TR, positioned RXRs at the epicenter of molecular endocrinology. Transcriptional control via nuclear RXR/TR heterodimer represents a direct action of thyroid hormone. T3 plays a crucial role in the development of brain, it exerts significant effects on the cardiovascular system, skeletal muscle contractile function, bone development and growth, both female and male reproductive systems, and skin. It plays an important role in maintaining the hepatic, kidney and intestine homeostasis and in pancreas, it stimulates the beta-cell proliferation and survival. The TRs cross-talk with other signaling pathways intensifies the T3 action at cellular level. The role of thyroid hormone in human cancers, acting via its cognate nuclear receptors, has not been fully elucidated yet. This review is aimed to describe the history of T3 receptors, starting from discovery of T3 binding sites in the cell nuclei to revelation of T3 receptors as T3-inducible transcription factors in relation to T3 action at cellular level. It also focuses on milestones of investigation, comprising RXR/TR dimerization, cross-talk between T3 receptors, and other regulatory pathways within the cell and mainly on genomic action of T3. This review also focuses on novel directions of investigation on relationships between T3 receptors and cancer. Based on the update of available literature and the author’s experimental experience, it is devoted to clinicians and medical students.

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“…di-isopropyl fluorophosphate or tosylphenylalanylchloromethane) and substrates (e.g. tryptophan methyl ester or tosylphenylalanine methyl ester) can inhibit the binding of steroids to SBP (M. E. Baker, unpublished work), rat az-foetoprotein and intracellular receptors (Hunziker et al, 1980;Lukola & Punnonen, 1982;Baker, 1985Baker, , 1986Baker et al, 1985;Hubbard & Kalimi, 1985;Puca et al, 1986). One explanation for these findings is that the tertiary structure of steroid-binding proteins has some chemistry in common with proteinases (Baker, 1985(Baker, , 1986Baker et al, 1985).…”

Section: Imentioning

confidence: 99%

Vitamin K-dependent protein S is similar to rat androgen-binding protein

Baker

French

Joseph

1987

Biochemical Journal

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Vitamin K-dependent protein S belongs to the family of clotting factors (e.g. Factors IX and X, and protein C). Unlike the other clotting factors, the C-terminal half (residues 250-634) of protein S is not a serine proteinase. In fact, the function of residues 250-634 of protein S is unknown. By using computer programs designed to detect evolutionary relationships between proteins, we find that this part of protein S is similar to rat androgen-binding protein, a protein produced and secreted by testicular Sertoli cells. The homology between protein S and androgen-binding protein suggests new approaches for elucidating their functions.

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Influence of proteinase inhibitors on glucocorticoid receptor properties: recent progress and future perspectives

Cited by 13 publications

References 40 publications

A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors

A 59-kilodalton protein associated with progestin, estrogen, androgen, and glucocorticoid receptors

Thyroid hormone and thyroid hormone nuclear receptors: History and present state of art

Vitamin K-dependent protein S is similar to rat androgen-binding protein

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