Cited by 114Adipose Tissue and MetabolismAdipokines, Inflammation, and Metabolic DiseasesExercise and Physiological Responses

The DOI matches its Crossref record; 75 of the 75 references it cites were found in a registry or an index.

Irisin and Myonectin Regulation in the Insulin Resistant Muscle: Implications to Adipose Tissue: Muscle Crosstalk

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Gamas, Luis, Matafome, Paulo, Seiça, Raquel·2015·Journal of Diabetes Research

Abstract

Myokines are peptides produced and secreted by the skeletal muscle, with autocrine, paracrine, and endocrine actions. Many of them are overexpressed during physical exercise and appear to contribute to the benefits of exercise to metabolic homeostasis. Irisin, resulting from the cleavage of the membrane protein FNDC5, was shown to induce adipocyte browning, with increased lipid oxidation and thermogenesis. Myonectin was only recently discovered and initial studies revealed a role in fatty acid uptake and oxidation in adipose tissue and liver. However, the mechanisms of their regulation by exercise are not entirely established. Impaired secretion and action of myokines, such as irisin and myonectin, may have a role in the establishment of insulin resistance. On the other hand, several studies have shown that insulin resistance in the skeletal muscle may change myokines expression and secretion. This may have consequences on lipid and glucose metabolism in adipose tissue and lead to a vicious cycle between impaired myokines production and insulin resistance. This review summarizes the current knowledge about the influence of skeletal muscle insulin resistance on the secretion of irisin and myonectin, as well as its impact on adipose tissue metabolism.

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Crossref · 10.1155/2015/359159

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Figures

Figure 1 Stimulation of irisin secretion by cold and exercise. Irisin secretion results from PGC-1a activation, which leads to FNDC5 expression. FNDC5 present in the membrane is in turn cleaved and irisin is secreted to the blood, acting on the adipose tissue in order to stimulate the formation of brite adipocytes and UCP-1 expression. Irisin also seems to induce AMPK phosphorylation in the skeletal muscle itself. AMPK: AMP-activated protein kinase; FNDC5: fibronectin type-III domain containing protein 5; PGC-1α: peroxisome proliferator-activated receptor gamma coactivator 1-α; UCP-1: uncoupling protein-1.
Figure 1 Stimulation of irisin secretion by cold and exercise. Irisin secretion results from PGC-1a activation, which leads to FNDC5 expression. FNDC5 present in the membrane is in turn cleaved and irisin is secreted to the blood, acting on the adipose tissue in order to stimulate the formation of brite adipocytes and UCP-1 expression. Irisin also seems to induce AMPK phosphorylation in the skeletal muscle itself. AMPK: AMP-activated protein kinase; FNDC5: fibronectin type-III domain containing protein 5; PGC-1α: peroxisome proliferator-activated receptor gamma coactivator 1-α; UCP-1: uncoupling protein-1.CC BY · PubMed Central
Figure 2 Stimulation of myonectin secretion by exercise, lipids, and glucose. The activation of unknown myocyte mediators by exercise and nutrients, which may include the Akt/PI3K pathway increases myonectin secretion. Myonectin increases the expression of fatty acids transporter and binding proteins in adipose tissue and liver, which promotes fatty acid uptake and storage. FABP: fatty acid binding protein; FATP: fatty acid transporter protein; PI3K: phosphatidylinositol-3-kinase.
Figure 2 Stimulation of myonectin secretion by exercise, lipids, and glucose. The activation of unknown myocyte mediators by exercise and nutrients, which may include the Akt/PI3K pathway increases myonectin secretion. Myonectin increases the expression of fatty acids transporter and binding proteins in adipose tissue and liver, which promotes fatty acid uptake and storage. FABP: fatty acid binding protein; FATP: fatty acid transporter protein; PI3K: phosphatidylinositol-3-kinase.CC BY · PubMed Central

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Research works printed but not linked: 2

  1. 10.1172/jci200525102 · DOI · Paper page
  2. 2014, European Review for Medical and Pharmacological Sciences, 18, 1567

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Metadata

Authors
Gamas, L., Matafome, P., & Seiça, R.
Affiliations
  • Laboratory of Physiology, Institute for Biomedical Imaging and Life Sciences (IBILI), Faculty of Medicine, University of Coimbra, 3000-548 Coimbra, Portugal
  • Universidade Politécnica de Coimbra (PT)
  • University of Coimbra (PT)
Corresponding author
Matafome, Paulo
Venue
Journal of Diabetes Research
Publisher
Wiley
Published
2015
Volume
2015
Pages
1-8
ISSN
  • 2314-6745 (ISSN-L)
  • 2314-6753
OpenAlex
W1496273172
Cited by
114
References
75
Citations by year
2026: 3 · 2025: 6 · 2024: 12 · 2023: 6 · 2022: 11 · 2021: 11 · 2020: 17 · 2019: 14 · 2018: 9 · 2017: 8 · 2016: 15 · 2015: 2
FWCI
1.39
Type
journal article
Language
en
Open access
Locations
  • Journal of Diabetes Research (publishedVersion, cc-by)
  • Europe PMC (PubMed Central) (publishedVersion, cc-by)
  • PubMed Central (publishedVersion, cc-by)
  • PubMed (publishedVersion)
  • DOAJ (DOAJ: Directory of Open Access Journals) (submittedVersion, cc-by-sa)
  • Portuguese National Funding Agency for Science, Research and Technology (RCAAP Project by FCT) (submittedVersion, cc-by)
Topics
  • Health Sciences › Medicine › Physiology (medical) › Adipose Tissue and Metabolism
  • Health Sciences › Medicine › Endocrinology, Diabetes and Metabolism › Adipokines, Inflammation, and Metabolic Diseases
  • Health Sciences › Medicine › Physiology (medical) › Exercise and Physiological Responses
Keywords
irisin, myonectin, myokines, skeletal muscle insulin resistance, FNDC5, adipose tissue metabolism, physical activity, adipocyte browning, thermogenesis, fatty acid oxidation, lipid metabolism, glucose metabolism
MeSH terms
Adipose Tissue, Animals, Cell Communication, Collagen, Diabetes Mellitus, Type 2, Fibronectins, Humans, Insulin Resistance, Obesity, Exercise, Muscle, Skeletal

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