A structural perspective on lactoferrin function1This article is part of a Special Issue entitled Lactoferrin and has undergone the Journal's usual peer review process.

2012 ◽  
Vol 90 (3) ◽  
pp. 320-328 ◽  
Author(s):  
Heather M. Baker ◽  
Edward N. Baker

The 3-D structure of human lactoferrin was first solved in atomic detail in 1987. Since that time, a variety of proven and postulated activities have been added to the original annotation of lactoferrin as an iron-binding protein. Structural studies have also expanded to include iron-bound and iron-free (apo) forms, mutants, and the lactoferrins of different species. In this review, we take the current information on both structure and function and show that the 3-D structure provides a useful framework for understanding some activities and also points to productive research directions that could help elucidate other reported functions. Some functions relate to iron binding where the role of lactoferrin is to scavenge and retain iron across a wide pH range. We specifically focus on functions that depend on the surface structure of the molecule, identifying features that may determine the many other protective properties of this multifunctional protein.

Cells ◽  
2020 ◽  
Vol 9 (3) ◽  
pp. 705 ◽  
Author(s):  
Emilie Picard ◽  
Alejandra Daruich ◽  
Jenny Youale ◽  
Yves Courtois ◽  
Francine Behar-Cohen

Iron is essential for cell survival and function. It is a transition metal, that could change its oxidation state from Fe2+ to Fe3+ involving an electron transfer, the key of vital functions but also organ dysfunctions. The goal of this review is to illustrate the primordial role of iron and local iron homeostasis in retinal physiology and vision, as well as the pathological consequences of iron excess in animal models of retinal degeneration and in human retinal diseases. We summarize evidence of the potential therapeutic effect of iron chelation in retinal diseases and especially the interest of transferrin, a ubiquitous endogenous iron-binding protein, having the ability to treat or delay degenerative retinal diseases.


2019 ◽  
Vol 10 (1) ◽  
pp. 43-55
Author(s):  
Nathan C. Donelson ◽  
Richa Dixit ◽  
Israel Pichardo-Casas ◽  
Eva Y. Chiu ◽  
Robert T. Ohman ◽  
...  

Locomotion is an ancient and fundamental output of the nervous system required for animals to perform many other complex behaviors. Although the formation of motor circuits is known to be under developmental control of transcriptional mechanisms that define the fates and connectivity of the many neurons, glia and muscle constituents of these circuits, relatively little is known about the role of post-transcriptional regulation of locomotor behavior. MicroRNAs have emerged as a potentially rich source of modulators for neural development and function. In order to define the microRNAs required for normal locomotion in Drosophila melanogaster, we utilized a set of transgenic Gal4-dependent competitive inhibitors (microRNA sponges, or miR-SPs) to functionally assess ca. 140 high-confidence Drosophila microRNAs using automated quantitative movement tracking systems followed by multiparametric analysis. Using ubiquitous expression of miR-SP constructs, we identified a large number of microRNAs that modulate aspects of normal baseline adult locomotion. Addition of temperature-dependent Gal80 to identify microRNAs that act during adulthood revealed that the majority of these microRNAs play developmental roles. Comparison of ubiquitous and neural-specific miR-SP expression suggests that most of these microRNAs function within the nervous system. Parallel analyses of spontaneous locomotion in adults and in larvae also reveal that very few of the microRNAs required in the adult overlap with those that control the behavior of larval motor circuits. These screens suggest that a rich regulatory landscape underlies the formation and function of motor circuits and that many of these mechanisms are stage and/or parameter-specific.


2002 ◽  
Vol 80 (1) ◽  
pp. 1-6 ◽  
Author(s):  
Jeremy H Brock

This paper reviews our current knowledge of the structure and function of the iron-binding protein lactoferrin. In particular, it attempts to relate the various proposed physiological functions of lactoferrin to its most characteristic biochemical properties, i.e. its ability to bind iron and its highly basic nature. The extent to which various physiological functions can be considered as definitely established is critically reviewed, and suggestions for future research are proposed.Key words: lactoferrin, iron, nutrition, immunology, infection, inflammation.


1978 ◽  
Vol 55 (s4) ◽  
pp. 23s-26s ◽  
Author(s):  
H. Thurston ◽  
B. C. Hurst ◽  
R. F. Bing ◽  
J. D. Swales

1. Aortic homogenate contains renin-like activity which on incubation generates angiotensin I over a wide pH range. 2. Rat aortic renin measured at an incubation pH of 6·5 rose and fell in parallel to plasma renin with salt depletion and salt-loading respectively. Renin measured at an incubation pH of 5·3 showed little relationship with plasma renin. 3. Aortic renin (pH 6·5) was elevated in Goldblatt-two kidney hypertension and slowly fell for 24 h after bilateral nephrectomy whereas the fall in plasma renin was complete by the first hour. Aortic renin (pH 5·3) was also high, but did not fall after bilateral nephrectomy. 4. Aortic renin (pH 6·5) is probably derived from plasma renin whereas renin measured at pH 5·3 is probably a tissue renin. 5. The prolonged half-life of aortic renin (pH 6·5) explains the observation that the renin—angiotensin system appears to be active in maintaining blood pressure for several hours after bilateral nephrectomy whereas the decline in plasma renin is rapid and does not continue significantly beyond 1 h.


2020 ◽  
Vol 06 (03) ◽  
pp. 1-1
Author(s):  
Colin Armstrong ◽  

Progress in technologies, notably in vivo and in situ methods, has equipped scientists with the necessary skills to explore the living human body in increasingly minute detail. This has led to a better understanding of the dynamic interplay between the various elements that make up the living human body. To further understand the interplay, this research focuses on the insights and observations of the founders of osteopathy, who placed great importance on the role of fascia in the body. Modern anatomical investigation still relies heavily on dissection to describe the structural organization of living organisms. Therefore, at present, a major challenge faced by modern anatomists is to move towards a more holistic and integrative understanding of the unity, continuity, and dynamic interplay between the various elements that come together to create the living human form.


1996 ◽  
Vol 134 (1) ◽  
pp. 81-92 ◽  
Author(s):  
M Maroto ◽  
J Arredondo ◽  
D Goulding ◽  
R Marco ◽  
B Bullard ◽  
...  

The Drosophila paramyosin/miniparamyosin gene expresses two products of different molecular weight transcriptionally regulated from two different promoters. Distinct muscle types also have different relative amounts of myosin, paramyosin, and miniparamyosin, reflecting differences in the organization of their thick filaments. Immunofluorescence and EM data indicate that miniparamyosin is mainly located in the M line and at both ends of the thick filaments in Drosophila indirect flight muscles, while paramyosin is present all along the thick filaments. In the tergal depressor of the trochanter muscle, both proteins are distributed all along the A band. In contrast, in the waterbug, Lethocerus, both paramyosin and miniparamyosin are distributed along the length of the indirect flight and leg muscle thick filaments. Two-dimensional and one-dimensional Western blot analyses have revealed that miniparamyosin has several isoforms, focusing over a very wide pH range, all of which are phosphorylated in vivo. The changes in isoform patterns of miniparamyosin and paramyosin indicate a direct or indirect involvement of these proteins in muscle function and flight. This wide spectrum of potential regulatory characteristics underlines the key importance of paramyosin/miniparamyosin and its complex isoform pattern in the organization of the invertebrate thick filament.


1982 ◽  
Vol 37 (11-12) ◽  
pp. 1095-1099 ◽  
Author(s):  
Ute Laudenbach ◽  
Jürgen Kesselmeier

Abstract The accumulation of the steroidal saponins avenacoside A and B in oat was investigated in green and etiolated seedlings and was found to be strictly bound to the growth of the seedlings. No significant differences were detected between green and etiolated seedlings, showing that there is no relation between saponin accumulation and plastid development. As the role of the oat saponins has to be seen as a protective device against fungi and bacteria, the transformation of the inactive avenacosides to their corresponding antibiotic 26-desgluco-avenacosides was tested in dependence of pH and temperature. During disruption of leaves, transformation occurs almost completely over a wide pH-range (pH 4 -pH 10); the degree of transformation exhibits no distinct temperature optimum but a drastic decrease at 70 °C.


2007 ◽  
Vol 85 (4) ◽  
pp. 397-410 ◽  
Author(s):  
Melina M. Musri ◽  
Ramon Gomis ◽  
Marcelina Párrizas

Long considered scarcely more than an uninteresting energy depot, adipose tissue has recently achieved star status. Far from being mere fat droplets, the adipocytes secrete a number of hormones and bioactive peptides, collectively known as adipokines, which participate in the regulation of a variety of functions, from haemostasis to angiogenesis to energy balance. Adipose tissue constitutes a bona-fide endocrine organ whose main dysfunctions, obesity and lipodystrophy, are related to the development of diabetes, hypertension, or dyslipidemia. The renewed interest in this tissue has prompted an escalation in the number of studies focusing on every aspect of the biology of the adipose cell, in the belief that a detailed knowledge of the mechanisms involved in the differentiation and function of adipocytes may contribute new therapeutical approaches to the treatment of such alarming medical problems. Adipogenesis is the result of an intertwined network of transcription factors and coregulators with chromatin-modifying activities that together, are responsible for the establishment of the gene expression pattern of mature adipocytes. Although the exquisitely regulated transcription factor cascade controlling adipogenesis has been extensively studied, the role of chromatin and chromatin-modifying proteins has become apparent only in recent times.


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