Activin A and follistatin: their role in the acute phase reaction and inflammation

Kretser, David Morritz de; Hedger, Mark P.; Phillips, David J.

doi:10.1677/joe.0.1610195

Cited by 61 publications

(42 citation statements)

References 23 publications

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“…While earlier work on activins and FS concentrated mainly on the effects of both proteins in endocrine and especially gonadal tissues, recent research has shown that both factors participate in the regulation of non-reproductive functions such as tissue repair and inflammation (28,29). Since the actions of activin are neutralized by binding to FS, the physiological balance of both polypeptides is most important in activin-responsive tissues.…”

Section: Discussionmentioning

confidence: 99%

“…Since then the expression of FS-and activin-mRNA has been detected in many non-gonadal tissues throughout the organism, and this has increased the interest in non-gonadal effects of the FS/activin system. Recent results showed the regulation of FS and activin in inflammation, acute phase response and tissue repair (28,29), arteriosclerosis (30), pulmonary fibrosis (31), liver cirrhosis (32) and ischemic brain injury (33). Although a wealth of data has been accumulated about FS/activin expression in different organs, the source of circulating FS and activin protein in serum has not yet been determined and the naturally occurring ratios of FS-and activinsubunit-mRNAs under physiological conditions are still unknown.…”

Section: Introductionmentioning

confidence: 99%

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Comparative analysis of follistatin-, activin beta A- and activin beta B-mRNA steady-state levels in diverse porcine tissues by multiplex S1 nuclease analysis

Schneider

Nau²,

Michel

2000

European Journal of Endocrinology

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Objective: The relation of activins (dimers of the beta-subunits of inhibin) and follistatin (FS) (their binding protein) affect the growth and differentiation of many cell types. Activin-and FS-mRNAs show a widespread co-expression throughout the organism, indicating an essential role for the FS/activin system in diverse physiological processes. The present study was performed to investigate FS-, activin beta A-, and activin beta B-mRNA expression in porcine tissues and to compare the relative mRNA tissue distribution by a newly developed multiplex S1 nuclease protection assay. Methods: Twenty micrograms total RNA from different porcine tissues were subjected to multiplex S1 analysis. Specific mRNA expression was determined by measurements of optical densities on autoradiographs. Results: Activin beta A-mRNA expression was abundant in the ovary, adrenal gland, fat, vein, artery and uterus, activin beta B-mRNA was highly expressed in the ovary, pituitary, uterus, placenta, aorta and cerebellum. FS-mRNA showed a widespread expression with high levels in ovary, uterus, cerebellum, placenta and fat. The comparison of relative activin beta A-, activin beta B-and FSmRNA expression within a certain tissue showed a predominance of activin beta A-mRNA in the adrenal gland, fat, artery, spinal cord, cerebrum and colon and of activin beta B-m RNA in pituitary, testis and placenta, while FS-mRNA levels exceeded those of activin subunits in epididymis, liver, lymphoid tissue, muscle, intestine, cerebellum, ovary and uterus. Conclusions: The presented data provide an overview of FS-, activin beta A-, and activin beta B-mRNA steady state levels in porcine tissues.

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Section: Discussionmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

Comparative analysis of follistatin-, activin beta A- and activin beta B-mRNA steady-state levels in diverse porcine tissues by multiplex S1 nuclease analysis

Schneider

Nau²,

Michel

2000

European Journal of Endocrinology

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“…Neuropsin is a serine protease that may affect synaptic architecture by proteolytic degradation of extracellular matrix proteins, such as fibronectin (Tomimatsu et al, 2002), and has been suggested to be neuroprotective to hyperexcitability (Davies et al, 2001). Activin is protective in some models of excitotoxic/ischemic brain injury Mattson, 2000;Tretter et al, 2000), and antiinflammatory actions, resembling those of TGF␤, have been shown (de Kretser et al, 1999). These molecules may play a role in the phenomenon of kindling-induced protection against kainate seizure-induced neuronal degeneration (Kelly and McIntyre, 1994).…”

Section: Laminar and Cellular Analysismentioning

confidence: 99%

Activin mRNA induced during amygdala kindling shows a spatiotemporal progression that tracks the spread of seizures

Foster

Puchowicz

McIntyre

et al. 2004

J of Comparative Neurology

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The progressive development of seizures in rats by amygdala kindling, which models temporal lobe epilepsy, allows the study of molecular regulators of enduring synaptic changes. Neurotrophins play important roles in synaptic plasticity and neuroprotection. Activin, a member of the transforming growth factor-␤ superfamily of growth and differentiation factors, has recently been added to the list of candidate synaptic regulators. We mapped the induction of activin ␤A mRNA in amygdala and cortex at several stages of seizure development. Strong induction, measured 2 hours after the first stage 2 (partial) seizure, appeared in neurons of the ipsilateral amygdala (confined to the lateral, basal, and posterior cortical nuclei) and insular, piriform, orbital, and infralimbic cortices. Activin ␤A mRNA induction, after the first stage 5 (generalized) seizure, had spread to the contralateral amygdala (same nuclear distribution) and cortex, and the induced labeling covered much of the convexity of neocortex as well as piriform, perirhinal, and entorhinal cortices in a nearly bilaterally symmetrical pattern. This pattern had filled in by the sixth stage 5 seizure. Induced labeling in cortical neurons was confined mainly to layer II. A similar temporal and spatial pattern of increased mRNA expression of brain-derived neurotrophic factor (BDNF) was found in the amygdala and cortex. Activin ␤A and BDNF expression patterns were similar at 1, 2, and 6 hours after the last seizure, subsiding at 24 hours; in contrast, c-fos mRNA induction appeared only at 1 hour throughout cortex and then subsided. In double-label studies, activin ␤A mRNA-positive neurons were also BDNF mRNA positive, and they did not colocalize with GAD67 mRNA (a marker of ␥-aminobutyric acidergic neurons). The data suggest that activin and BDNF transcriptional activities accurately mark excitatory neurons participating in seizure-induced synaptic alterations and may contribute to the enduring changes that underlie the kindled state.

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“…In addition, a soluble activinbinding protein, follistatin, has been discovered which binds with high affinity to activin A and B and thereby inhibits its biological effects (for review see . Activins/inhibins are evolutionarily conserved, broadly distributed, 48 and influence many other processes, including inflammation, acute phase reaction, 49 proliferation and cell growth, 50 nerve cell survival and differentiation, 51,52 tissue repair and wound healing, 53,54 angiogenesis 55 and matrix and bone remodeling via BMPs (eg inhibition of osteoclastic cathepsin K-mediated bone reabsorption). [56][57][58][59][60][61] A role of activin in the pathogenesis of inflammatory arthropathies has been suggested by Yu et al 62 The latter demonstrated significantly elevated levels of activin A in the synovial fluid of patients with rheumatoid arthritis and gout, relative to those with osteoarthritis.…”

Section: Figure 5 Real-time Pcr For Activin and Follistatin Real-timmentioning

confidence: 99%

Inhibition of cartilage destruction by double gene transfer of IL-1Ra and IL-10 involves the activin pathway

et al. 2002

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Activin A and follistatin: their role in the acute phase reaction and inflammation

Cited by 61 publications

References 23 publications

Comparative analysis of follistatin-, activin beta A- and activin beta B-mRNA steady-state levels in diverse porcine tissues by multiplex S1 nuclease analysis

Comparative analysis of follistatin-, activin beta A- and activin beta B-mRNA steady-state levels in diverse porcine tissues by multiplex S1 nuclease analysis

Activin mRNA induced during amygdala kindling shows a spatiotemporal progression that tracks the spread of seizures

Inhibition of cartilage destruction by double gene transfer of IL-1Ra and IL-10 involves the activin pathway

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