The Tissue Distribution of the mRNA of Ghrelin and Subtypes of Its Receptor, GHS-R, in Humans

Gnanapavan, Sharmilee; Kola, Blerina; Bustin, Stephen A.; Morris, Damian; McGee, Patrick; Fairclough, Peter D.; Bhattacharya, Satya; Carpenter, R; Grossman, Ashley; Korbonits, M

doi:10.1210/jcem.87.6.8739

Cited by 995 publications

(363 citation statements)

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“…In addition, when activated, T cells also express the preproghrelin protein and produce and secrete both acylated and unacylated ghrelin (Baatar et al 2011;Dixit et al 2004). Besides lymphocytes, ghrelin mRNA was also found in human spleen, lymph nodes, and thymus (Dixit et al 2004;Gnanapavan et al 2002). In thymus, ghrelin and the GHS-R1a decline with age.…”

Section: Ghrelin and Ghs-r1a Mrna Expression And Distribution In The mentioning

confidence: 99%

“…Also GHS-R1a is widely expressed in the lymphoid system, and its expression was reported in the same cells expressing ghrelin (Dixit et al 2004;Hattori et al 2001), as well as in the spleen (Gnanapavan et al 2002). A truncated inactive GHS-R1b has been shown in various immune tissues, although ghrelin does not bind to and activate it and the role of this receptor is still unknown (Taub 2008).…”

Section: Ghrelin and Ghs-r1a Mrna Expression And Distribution In The mentioning

confidence: 99%

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Ghrelin Gene Products in Acute and Chronic Inflammation

Prodam,

Filigheddu

2014

Arch. Immunol. Ther. Exp.

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Ghrelin gene products-the peptides ghrelin, unacylated ghrelin, and obestatin-have several actions on the immune system, opening new perspectives within neuroendocrinology, metabolism and inflammation. The aim of this review is to summarize the available evidence regarding the less known role of these peptides in the machinery of inflammation and autoimmunity, outlining some of their most promising therapeutic applications.

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Section: Ghrelin and Ghs-r1a Mrna Expression And Distribution In The mentioning

confidence: 99%

Section: Ghrelin and Ghs-r1a Mrna Expression And Distribution In The mentioning

confidence: 99%

Ghrelin Gene Products in Acute and Chronic Inflammation

Prodam,

Filigheddu

2014

Arch. Immunol. Ther. Exp.

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“…2002). Rather, AG is thought to potentially interact with the corticotropin‐releasing factor (CRF‐2) receptor in muscle (Filigheddu et al.…”

Section: Resultsmentioning

confidence: 99%

Acylated and unacylated ghrelin do not directly stimulate glucose transport in isolated rodent skeletal muscle

Cervone

Dyck

2017

Physiol Rep

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Emerging evidence implicates ghrelin, a gut‐derived, orexigenic hormone, as a potential mediator of insulin‐responsive peripheral tissue metabolism. However, in vitro and in vivo studies assessing ghrelin's direct influence on metabolism have been controversial, particularly due to confounding factors such as the secondary rise in growth hormone (GH) after ghrelin injection. Skeletal muscle is important in the insulin‐stimulated clearance of glucose, and ghrelin's exponential rise prior to a meal could potentially facilitate this. This study was aimed at elucidating any direct stimulatory action that ghrelin may have on glucose transport and insulin signaling in isolated rat skeletal muscle, in the absence of confounding secondary factors. Oxidative soleus and glycolytic extensor digitorum longus skeletal muscles were isolated from male Sprague Dawley rats in the fed state and incubated with various concentrations of acylated and unacylated ghrelin in the presence or absence of insulin. Ghrelin did not stimulate glucose transport in either muscle type, with or without insulin. Moreover, GH had no acute, direct stimulatory effect on either basal or insulin‐stimulated muscle glucose transport. In agreement with the lack of observed effect on glucose transport, ghrelin and GH also had no stimulatory effect on Ser473 AKT or Thr172 AMPK phosphorylation, two key signaling proteins involved in glucose transport. Furthermore, to our knowledge, we are among the first to show that ghrelin can act independent of its receptor and cause an increase in calmodulin‐dependent protein kinase 2 (CaMKII) phosphorylation in glycolytic muscle, although this was not associated with an increase in glucose transport. We conclude that both acylated and unacylated ghrelin have no direct, acute influence on skeletal muscle glucose transport. Furthermore, the immediate rise in GH in response to ghrelin also does not appear to directly stimulate glucose transport in muscle.

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“…However, the mechanisms by which ghrelin may influence muscle function may not only be related to an indirect endocrine action GHmediated. It has recently been described that ghrelin, either acyl and des-acyl ghrelin, may act at the muscle level through direct mechanisms not involving GHSR1a receptor which is not present in myocytes (Baldanzi et al 2002;Filigheddu et al 2007;Gnanapavan et al 2002;Sheriff et al 2012). Filigheddu et al (2007) have shown that both ghrelin and des-acyl ghrelin stimulate tyrosine phosphorylation of several muscle proteins and activate ERK-1/2 and Akt, indicating that both ghrelin isoforms could exert a biological activity on muscle cells.…”

Section: Discussionmentioning

confidence: 99%

Obestatin is associated to muscle strength, functional capacity and cognitive status in old women

Mora

Granada

Palomera

et al. 2013

AGE

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Obestatin has been proposed to have anorexigenic and anti-ghrelin actions. The objective was to study obestatin concentrations in relation to handgrip strength, functional capacity and cognitive state in old women. The prospective study included 110 women (age, 76.93±6.32) from the Mataró Ageing Study. Individuals were characterized by anthropometric variables, grip strength, Barthel and assessment of cognitive impairment [Mini Cognoscitive Examination (MCE) Spanish version], depressive status by the Geriatric Depression Scale (GDS) and frailty by the Fried criteria. Obestatin was measured by IRMA. Obestatin showed negative correlation to handgrip at basal time point (r= −0.220, p=0.023) and at 2-year follow-up (r=−0.344, p=0.002). Obestatin, divided into quartiles, showed a negative lineal association with handgrip: 11.03 ± 4.88 kg in first, 8.75±4.08 kg in second, 8.11±3.66 kg in third and 7.61±4.08 kg in fourth quartile (p=0.018). Higher obestatin levels were associated to increased weakness (categorized by handgrip of frailty criteria): 2.24±0.42 ng/ml in weak vs. 1.87±0.57 ng/ml in nonweak (p=0.01). The decrease of either MCE or Barthel scores at 2-year follow-up was significantly higher in individuals in the fourth quartile of obestatin in comparison with individuals in the first quartile (p=0.046 and p=0.019, respectively). No association was found between obestatin and GDS score and neither with frailty as a condition. Obestatin is associated to low muscle strength, and impaired functional and cognitive capacity in old women participating in the Mataró Ageing Study.

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The Tissue Distribution of the mRNA of Ghrelin and Subtypes of Its Receptor, GHS-R, in Humans

Cited by 995 publications

References 0 publications

Ghrelin Gene Products in Acute and Chronic Inflammation

Ghrelin Gene Products in Acute and Chronic Inflammation

Acylated and unacylated ghrelin do not directly stimulate glucose transport in isolated rodent skeletal muscle

Obestatin is associated to muscle strength, functional capacity and cognitive status in old women

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