Subcellular distribution of particle-bound neutral peptidases capable of hydrolyzing gonadoliberin, thyroliberin, enkephalin and substance P

Horsthemke, Bernhard; Leblanc, Pierre; Kordon, C.; Coninck, Simone Wattiaux‐De; Wattiaux, Robert; Bauer, Karl

doi:10.1111/j.1432-1033.1984.tb08009.x

Cited by 44 publications

(17 citation statements)

References 38 publications

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“…In a study of the subcellular distribution of peptidases hydrolysing neuropeptides in rat anterior pituitary, Horsthemke et al (1984) concluded that no LH-RHdegrading activity was associated with plasma membranes but rather that LH-RH-degrading activity was associated with mitochondria-rich fractions. In a subsequent study, this activity was shown to be located in the mitochondria1 matrix space and could cleave LH-RH to give LH-RH1_*, LH-RHI-3, LH-RH,-4, LH-RHI_=,, and LH-RH1_6.…”

Section: Degradation Of Lh-rh By Enzymes In Particulate Fractions Of mentioning

confidence: 99%

Degradation of Thyrotropin‐Releasing Hormone and Luteinising Hormone‐Releasing Hormone by Enzymes of Brain Tissue

O'cuinn

O’Connor

Elmore

1990

Journal of Neurochemistry

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In this article, the enzymes of brain and associated tissues that can degrade thyrotropin-releasing hormone (TRH) and luteinising hormone-releasing hormone (LH-RH) are reviewed. As both TRH and LH-RH are considered to act as neurotransmitters or neuromodulators in the CNS, attention is paid to the subcellular location of the enzymes described and how their topographies and substrate specificities fit them to playing roles as inactivating agents for TRH and LH-RH or as regulators of intracellular concentrations of TRH and LH-RH. Consideration is also given to enzymes involved in biotransformation of TRH to secondary metabolites that exhibit biological activity and to enzymes involved in the metabolism of secondary metabolites.

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Section: Degradation Of Lh-rh By Enzymes In Particulate Fractions Of mentioning

confidence: 99%

Degradation of Thyrotropin‐Releasing Hormone and Luteinising Hormone‐Releasing Hormone by Enzymes of Brain Tissue

O'cuinn

O’Connor

Elmore

1990

Journal of Neurochemistry

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“…An increased density of receptors for TRH has been found in the ade nohypophysis of old rats, concomitant with a marked accumulation of TRH in the gland, and these alterations are not associated with changes in the pituitary concen tration of TSH, suggestive that the increased availability of TRH in the adenohypophysis of old rats is not affect ing TSH production [55]. Further studies are needed to investigate possible age-related changes in the intracellu lar processing of TRH in the adenohypophysis [57,58] as well as in the degradation of TRH by specific pituitary enzymes [59,60]. Moreover, variant forms of TSH have been described in the serum and pituitary gland of old rats [61,62], as shown for gonadotrophins.…”

Section: Aging and Thyroid Functionmentioning

confidence: 99%

Neuroendocrine Aspects of Aging: Experimental Data

Reymond¹,

Donda²,

Lemarchand-Béraud³

1989

Horm Res

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Aging is characterized by changes in neuroendocrine/endocrine functions which are manifest in female reproductive physiology and less perceptible in other functions such as thyroid, adrenal or growth/metabolic functions. The contribution of each level of the axis – hypothalamus, adenohypophysis or peripheral tissues – is not clearly established. Functional impairments with age are recognized in the peripheral glands (gonad, thyroid, adrenal) as well as in the pituitary, but increasing evidence is accumulating for a marked contribution of the hypothalamus in the age-associated endocrine changes observed in animals and humans. In old rats, multineuronal dysfunctions are demonstrated in the hypothalamus, with a documented decline in the activity of the neurons producing dopamine and thyrotropin-releasing hormone, and to a lesser extent luteinizing hormone- and growth hormone-releasing hormones, and alterations in regulatory mechanisms of these neurons are disclosed. Moreover, impairments are observed in the processing – binding, accumulation and intracellular distribution – of hypothalamic hormones in the adenohypophysis of old rats. Taken together, these observations are supportive of the view that the neuroendocrine/endocrine changes appearing with age result from a complex balance of functional alterations occurring at each level – central and peripheral – of the axis.

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“…10) that exhibits, among other unusual characteristics, a very high degree of substrate specificity (11)(12)(13), as does the TRH-degrading serum enzyme (14). The particulate peptidase is localized in synaptosomal (11) and adenohypophyseal (15) membrane fractions. In brain-derived cells in culture, it is found only on the surface of neuronal cells but not on glial cells (16)(17)(18).…”

mentioning

confidence: 99%

Cloning of a cDNA encoding an ectoenzyme that degrades thyrotropin-releasing hormone.

Schauder

Schomburg

Köhrle

et al. 1994

Proc. Natl. Acad. Sci. U.S.A.

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Thyrotropin-releasing hormone (TRH) is an important extracellular signal substance that acts as a hypothalamic-releasing factor, which stimulates the release of adenohypophyseal hormones and functions as a neurotransmitter/neuromodulator in the central and peripheral nervous system. The Inactivation ofTRH after its release is catalyzed by an ectoenzyme localized preferentially on (14). The particulate peptidase is localized in synaptosomal (11) and adenohypophyseal (15) membrane fractions. In brain-derived cells in culture, it is found only on the surface of neuronal cells but not on glial cells (16-18). In the pituitary the enzyme is localized preferentially on lactotrophs (17), and recent studies have demonstrated that the activity of the adenohypophyseal enzyme is regulated by estradiol (19) and is stringently controlled by thyroid hormones (20)(21)(22).After solubilization by limited proteolysis under very mild conditions, we recently succeeded in purifying the enzyme from rat and pig brain (about 200,000-fold) to electrophoretic homogeneity. In this report we describe the isolation and sequence of a cDNA encoding the TRH-degrading ectoenzyme.J Furthermore, we present information on the transcriptional regulation of the adenohypophyseal enzyme by thyroid hormones as well as on the functional expression of this peptidase in transfected mammalian cells.MATERIALS AND METHODS Enzyme Fragmentation and Peptide Sequencing. After isolation from rat or pig brain as described elsewhere (23)

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Subcellular distribution of particle-bound neutral peptidases capable of hydrolyzing gonadoliberin, thyroliberin, enkephalin and substance P

Cited by 44 publications

References 38 publications

Degradation of Thyrotropin‐Releasing Hormone and Luteinising Hormone‐Releasing Hormone by Enzymes of Brain Tissue

Degradation of Thyrotropin‐Releasing Hormone and Luteinising Hormone‐Releasing Hormone by Enzymes of Brain Tissue

Neuroendocrine Aspects of Aging: Experimental Data

Cloning of a cDNA encoding an ectoenzyme that degrades thyrotropin-releasing hormone.

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