Caveolae are submicroscopic, plasma membrane pits that are abundant in many mammalian cell types. The past few years have seen a quantum leap in our understanding of the formation, dynamics and functions of these enigmatic structures. Caveolae have now emerged as vital plasma membrane sensors that can respond to plasma membrane stresses and remodel the extracellular environment. Caveolae at the plasma membrane can be removed by endocytosis to regulate their surface density or can be disassembled and their structural components degraded. Coat proteins, called cavins, work together with caveolins to regulate the formation of caveolae but also have the potential to dynamically transmit signals that originate in caveolae to various cellular destinations. The importance of caveolae as protective elements in the plasma membrane, and as membrane organizers and sensors, is highlighted by links between caveolae dysfunction and human diseases, including muscular dystrophies and cancer.

Caveolae as plasma membrane sensors, protectors and organizers

Progress in Nuclear Magnetic Resonance Spectroscopy Vol. 2. Edited by J. W. Emsley, J. Feeney and L. H. Sutcliffe. Pp. vii + 269. (Oxford, London and New York: Pergamon Press, Ltd, 1967.) 90s. net. Advances in Magnetic Resonance Vol. 2. By John S. Waugh. Pp. xii + 269. (New York: Academic Press, Inc.; London: Academic Press, Inc. (London), Ltd, 1966.) $12.00. Guide to the NMR Empirical Method A Workbook. By Roy H. Bible jun.. Pp. xi + 305. (New York: Plenum Press, 1967.) $9.50.

/pdf/nuclear-magnetic-resonance-m75j2z9fc0.pdf

Nuclear Magnetic Resonance

The protein tyrosine phosphatase (Ptp) family dephosphorylates target proteins and counters the activities of protein tyrosine kinases. Accumulating evidence indicates that some PTPs have an important role in the inhibition or control of growth, whereas some PTPs exert oncogenic functions. This Review discusses the relevance of PTPs to cancer biology and their potential as therapeutic targets.

Inside the human cancer tyrosine phosphatome

Considerable research has been done to better understand the basis for gel formation by myofibrillar proteins (MPs) in effort to manufacture acceptable processed meats with lower cost and more desirable nutritional characteristics. Results from research available indicate that there is no substitute for the myofibrillar protein myosin in gel formation by proteins from a wide variety of animal and fish species. This report consolidates information on determinants of protein gel formation, examining types of muscles and fibers, the species influence, and interactions of the MPs actin and myosin with each other and with fat, gelatin, starch, hydrocolloids, some protein soy, whey, and nonprotein additives such as phosphates and acidifiers, and the influences of pH, ionic strength, rates of heating, and its absence, protein oxidation, as well as the use of transglutaminase and high hydrostatic pressure. It is of interest that myosin alone will form acceptable gels. Gel formation by MPs is optimized at pH 6, an ionic strength of 0.6 M, and at 60 to 70 °C. The observations that collagen-derived gelatin can reduce the rubbery texture of low-fat products and that solubilization of MPs is not always essential for gel formation, and the observation that good gels can be formed in the absence of salt, are exciting developments that should be considered as pressure mounts to continue to reduce fat and salt in the diet.

https://onlinelibrary.wiley.com/doi/pdf/10.1111/j.1541-4337.2010.00137.x

Factors Influencing Gel Formation by Myofibrillar Proteins in Muscle Foods

Salt and fluid absorption and secretion are two processes that are fundamental to epithelial function and whole body fluid homeostasis, and as such are tightly regulated in epithelial tissues. The CFTR anion channel plays a major role in regulating both secretion and absorption in a diverse range of epithelial tissues, including the airways, the GI and reproductive tracts, sweat and salivary glands. It is not surprising then that defects in CFTR function are linked to disease, including life-threatening secretory diarrhoeas, such as cholera, as well as the inherited disease, cystic fibrosis (CF), one of the most common life-limiting genetic diseases in Caucasian populations. More recently, CFTR dysfunction has also been implicated in the pathogenesis of acute pancreatitis, chronic obstructive pulmonary disease (COPD), and the hyper-responsiveness in asthma, underscoring its fundamental role in whole body health and disease. CFTR regulates many mechanisms in epithelial physiology, such as maintaining epithelial surface hydration and regulating luminal pH. Indeed, recent studies have identified luminal pH as an important arbiter of epithelial barrier function and innate defence, particularly in the airways and GI tract. In this chapter, we will illustrate the different operational roles of CFTR in epithelial function by describing its characteristics in three different tissues: the airways, the pancreas, and the sweat gland.

/pdf/role-of-cftr-in-epithelial-physiology-3rp15os61u.pdf

Role of CFTR in epithelial physiology

Dimerization and Actin-bundling Properties of Villin and Its Role in the Assembly of Epithelial Cell Brush Borders

Potential molecular mechanism for c-Src kinase-mediated regulation of intestinal cell migration.

From roughly 1985 through the start of the new millennium, the cutting edge of solution protein nuclear magnetic resonance (NMR) spectroscopy was to a significant extent driven by the aspiration to determine structures. Here we survey recent advances in protein NMR that herald a renaissance in which a number of its most important applications reflect the broad problem-solving capability displayed by this method during its classical era during the 1970s and early 1980s.

The Quiet Renaissance of Protein Nuclear Magnetic Resonance

Bilayered detergent–lipid assemblies known as bicelles have been widely used as model membranes in structural biological studies and are being explored for wider applications, including pharmaceutical use. Most studies to date have involved the use of concentrated bicelle mixtures, such that little is known about the capacity of bicellar mixtures to be diluted without unwanted transitions to nonisotropic phases. Here, different detergent/lipid mixtures have been explored, leading to the identification of two different families of bicelles for which it is possible to lower the total amphiphile (detergent + lipid) concentration to <1% (w/v) while retaining isotropic assemblies. These include a novel family of bicelles based on mixtures of 6-cyclohexyl-1-hexylphosphocholine (Cyclofos-6) and the lipid dimyristoylphosphatidylcholine (DMPC). Bicelles formed by these mixtures can be diluted to <0.5% and also have attractive biochemical properties. However, a caveat of our results is that the diffusion coefficien...

Bicelles at low concentrations

The kidney develops from direct interactions between the ureteric bud and the metanephric mesenchyme. The ureteric bud gives rise to the collecting system and the metanephric mesenchyme to the nephrons. The complex process of renal development which occurs between these embryologically distinct structures is mediated by numerous factors, including the communication of cells with their surrounding extracellular matrix. Integrins are the principal cellular receptors for extracellular matrix proteins, and they play a role in organ and tissue development. In this review we focus on how integrins regulate renal development.

Sijo Mathew

Papers

Dimerization and Actin-bundling Properties of Villin and Its Role in the Assembly of Epithelial Cell Brush Borders

Potential molecular mechanism for c-Src kinase-mediated regulation of intestinal cell migration.

The Quiet Renaissance of Protein Nuclear Magnetic Resonance

Bicelles at low concentrations

Integrins in renal development