Experimental Physiology

Cover image for Vol. 101 Issue 2

Edited By: Paul McLoughlin

Impact Factor: 2.669

ISI Journal Citation Reports © Ranking: 2014: 33/83 (Physiology)

Online ISSN: 1469-445X

Associated Title(s): The Journal of Physiology

Featured

  • Interleukin-1 as a pharmacological target in acute brain injury

    Interleukin‐1 as a pharmacological target in acute brain injury

    The pathways of cell death and inflammation in the brain are complex and appear to be regulated by multiple inflammasomes, as depicted here. The involvement of multiple inflammasomes may reflect peripheral versus central inflammation, cell-type-specific cell death and also directly inflammatory versus direct cell death effects. Abbreviations: AIM2, absent in melanoma 2; ASC, apoptosis-associated speck-like protein containing a CARD; DAMPs, damage-associated molecular patterns; IL, interleukin; IL-1Ra, anti-inflammatory IL-1 receptor antagonist; NLRC4, NLR family, CARD domain containing 4; NLRP1, NLR family, pyrin domain containing 1; and NLRP3, NLR family, pyrin domain containing 3.

  • Glucocorticoids as regulatory signals during intrauterine development

    Glucocorticoids as regulatory signals during intrauterine development

    Data are from Fowden & Forhead (, ), Forhead & Fowden () and Fowden et al. (, ). Abbreviations: GR, glucocorticoid receptor; MR, mineralocorticoid receptor; PNMT, phenylethanolamine-N-methyl-transferase; and UCP, uncoupling protein.

  • Insights from physiology into myometrial function and dysfunction

    Insights from physiology into myometrial function and dysfunction

    An altered pattern of gene expression in twin myometrium increases expression of genes favouring contraction and short cervix. The increased contractility in twins decreases the response totocolytics. The underlying mechanisms are a combination of increased oxytocin receptor (OTR), Ca2+ channels, cell–cell coupling via gapjunctions and decreased progesterone receptor expression. With increased membrane stretch, this facilitates Ca2+ entry and increased filling of the sarcoplasmic reticulum (SR). Together, this leads to increased riskfor preterm birth. Drawn by Dr Sarah Arrowsmith and reproduced with permission.

  • Advances in genetic therapeutic strategies for Duchenne muscular dystrophy

    Advances in genetic therapeutic strategies for Duchenne muscular dystrophy

    A, structure of the dystrophin-associated protein complex (DAPC) at the muscle membrane. The DAPC acts as a link between myofibres and the extracellular matrix to provide stability at the sarcolemma. The central rod domain of dystrophin contains 24 spectrin repeats and four hinges. The N-terminal domain (NTD) and specific spectrin repeats bind to cytosolic F-actin to aid in shock absorbance that results from elastic recoil during muscle contraction or stretch. The cysteine-rich domain (CRD) links dystrophin to the sarcolemmal-bound β-dystroglycan, which in turn binds to α-dystroglycan to form the dystroglycan complex. This complex is further strengthened by binding to the sarcoglycans (α, β, δ and γ) and sarcospan at the sarcolemma as well as laminin α2 at the extracellular matrix. The C-terminal domain (CTD) of dystrophin binds several cytosolic proteins, such as α-dystrobrevin and syntrophins (α and β). These syntrophins can recruit neuronal nitric oxide synthase (nNOS) to the sarcolemma via their PDZ domains to regulate blood flow to the muscle. In addition, spectrin repeats 16/17 in dystrophin are also able to recruit nNOS. Dystrophin interacts indirectly with microtubules through ankyrin-B and directly via spectrin repeats 20–23. Together, dystrophin and its associated proteins protect the sarcolemma from contraction-induced injury. B, structure of the utrophin-associated protein complex (UAPC) at the neuromuscular junction. The UAPCs have similar protective functions compared with the DAPCs, because utrophin shows 80% sequence homology to dystrophin. However, utrophin lacks the sequence corresponding to spectrin-like repeats 15 and 19 of dystrophin and binds actin only through the NTD. Utrophin is unable to recruit nNOS directly via its spectrin repeats, although nNOS can still be recruited indirectly through the syntrophins. At the neuromuscular junction, UAPC also binds to Raspyn and is involved in the clustering of acetylcholine receptors (AChRs) to the membrane. In addition, the CTD of utrophin binds to Multiple asters (MAST), which associates with microtubules. The UAPC is linked to the extracellular matrix of the neuromuscular junction via laminins α4, α5 and β2.

  • Taste and move: glucose and peptide transporters in the gastrointestinal tract

    Taste and move: glucose and peptide transporters in the gastrointestinal tract

    Schematic diagram displaying the transepithelial transport of peptides and glucose at intestinal epithelial cellsThe grey dotted arrow illustrates trafficking of GLUT2 to the apical membrane of enterocytes at high luminal glucose concentrations; a phenomenon that is controversially discussed and might depend on species. NHE3: Na+/H+ exchanger; SGLT1: Na+-dependent glucose transporter 1; PEPT1: H+-coupled peptide transporter 1; GLUT2: glucose transporter 2.

  • Interactions between local dilator and sympathetic vasoconstrictor influences in skeletal muscle in acute and chronic hypoxia

    Interactions between local dilator and sympathetic vasoconstrictor influences in skeletal muscle in acute and chronic hypoxia

    Continuous arrows indicate pathways used in presence of endothelial (e) nitric oxide synthase (NOS) activity. Dashed arrows indicate pathways by which adenosine may induce dilatation after NOS inhibition and during restoration of dilator tone with NO donor. Abbreviations: A1: Adenosine A1 receptor, AA, arachidonic acid; AC, adenyl cyclase; COX; cyclo-oxygenase; eNOS: endothelial nitric oxide synthase, ENT1, equilibrative nucleoside transporter; IP, PGI2 receptor; KATP: ATP-sensitive K+ channels; PGI2, prostacyclin; PKA, protein kinase A; PLA2, phospholipase A2.

  • The calcium-sensing receptor: one of a kind

    The calcium‐sensing receptor: one of a kind

    The CaSR is constituted of 1078 amino acids and features three structural domains. The first 612 amino acids form a large amino-terminal, nutrient-binding domain shaped like a Venus flytrap, which is characteristic of the family C GPCRs (Khan & Conigrave, ). This region is followed by seven transmembrane (250 amino acids) and C-terminal domains (216 amino acids). The CaSR post-translational modifications include glycosylation (Ray et al. ), cleavage of the signal peptide at the N-terminus (Goldsmith et al. ) and protein kinase C (PKC) phosphorylation (Bai et al. ). The former two participate in CaSR maturation, while the latter modulates CaSR activity. Activating (orange) and inactivating (blue) mutations demonstrate the pivotal role of the CaSR in mineral ion metabolism. Several polymorphisms have also been detected (yellow). Modified from CaSR Database (D'Souza-Li, ).

  • Interleukin‐1 as a pharmacological target in acute brain injury
  • Glucocorticoids as regulatory signals during intrauterine development
  • Insights from physiology into myometrial function and dysfunction
  • Advances in genetic therapeutic strategies for Duchenne muscular dystrophy
  • Taste and move: glucose and peptide transporters in the gastrointestinal tract
  • Interactions between local dilator and sympathetic vasoconstrictor influences in skeletal muscle in acute and chronic hypoxia
  • The calcium‐sensing receptor: one of a kind

Recently Published Issues

See all

Keyword search & F1000

Get Adobe Flash player




Faculty of 1000

Read the latest evaluations from Faculty of 1000 members recommending articles published in Experimental Physiologyhere.

Journal App

Journal App

Readers of Experimental Physiology now have the opportunity to read the journals via these new iPad apps.

Download the journal apps for free from iTunes and then launch the apps in your Newsstand.

The Physiological Society

Visit The Physiological Society website for:

  • Membership
  • Conferences
  • Grants
  • Physiology jobs

and much more...


Connect with us

Follow us on Twitter

twitter logo

Like us on Facebook

facebook logo


SEARCH

SEARCH BY CITATION