scholarly journals Heme Acquisition by trypanosomatids: Evaluation of the hemedependent behavior and its biochemical implications

PubVet ◽  
2020 ◽  
Vol 14 (11) ◽  
pp. 1-7
Author(s):  
Leonardo Marmo Moreira ◽  
Juliana Pereira Lyon
Keyword(s):  
Structure Function ◽  
Heme Proteins ◽  
Complex Diseases ◽  
Biochemical Properties ◽  
Biological Cycle ◽  
Physiological Mechanisms ◽  
Blood Diseases ◽  
Heme Acquisition ◽  
Biochemical Approach ◽  
Molecular Aspects

The inability of some species to produce porphyrin-like compounds induces these species to search for blood to fulfill their heme requirement. The biological cycle of very relevant parasites, such as Leishmania sp. and Trypanossoma sp., is directly related to the search for heme. The understanding of this process in a chemical and biochemical approach is a pre-requisite to obtaining advancements regarding hemoprotein structureactivity relationships as well as molecular aspects of various pathological/physiological mechanisms associated with parasitary and/or blood diseases, between others. The present work presents an overview of the chemical/biochemical properties of porphyrin, heme, heme proteins, and parasitary diseases caused by Trypanossomatidae. We believe that this kind of discussion can contribute significantly to improve the understanding of the structure-function relation of these complex diseases

scholarly journals BECLIN1: Protein Structure, Function and Regulation

Cells ◽  
2021 ◽  
Vol 10 (6) ◽  
pp. 1522
Author(s):  
Sharon Tran ◽  
W. Douglas Fairlie ◽  
Erinna F. Lee
Keyword(s):  
Protein Structure ◽  
Structure Function ◽  
Membrane Trafficking ◽  
Biochemical Properties ◽  
Class Iii ◽  
Form Class ◽  
Protein Interactome ◽  
Protein Functions ◽  
Phosphoinositide 3 Kinase ◽  
Shed Light

BECLIN1 is a well-established regulator of autophagy, a process essential for mammalian survival. It functions in conjunction with other proteins to form Class III Phosphoinositide 3-Kinase (PI3K) complexes to generate phosphorylated phosphatidylinositol (PtdIns), lipids essential for not only autophagy but other membrane trafficking processes. Over the years, studies have elucidated the structural, biophysical, and biochemical properties of BECLIN1, which have shed light on how this protein functions to allosterically regulate these critical processes of autophagy and membrane trafficking. Here, we review these findings and how BECLIN1’s diverse protein interactome regulates it, as well as its impact on organismal physiology.

scholarly journals O-Linked glycans control glycoprotein processing by antigen-presenting cells: a biochemical approach to the molecular aspects of MUC1 processing by dendritic cells

2003 ◽  
Vol 33 (12) ◽  
pp. 3242-3254 ◽  
Author(s):  
Franz-Georg Hanisch ◽  
Tilo Schwientek ◽  
Michael S. Von Bergwelt-Baildon ◽  
Joachim L. Schultze ◽  
Olivera Finn
Keyword(s):  
Dendritic Cells ◽  
Antigen Presenting Cells ◽  
Glycoprotein Processing ◽  
Biochemical Approach ◽  
Molecular Aspects ◽  
Antigen Presenting

Heme protein biosensors

2000 ◽  
Vol 04 (04) ◽  
pp. 358-361 ◽  
Author(s):  
MICHAEL K. CHAN
Keyword(s):  
Nitric Oxide ◽  
Structure Function ◽  
Guanylate Cyclase ◽  
Heme Proteins ◽  
Rhodospirillum Rubrum ◽  
Soluble Guanylate Cyclase ◽  
Heme Protein ◽  
Novel Proteins ◽  
Current State ◽  
Protein Sensors

The recent discovery that heme proteins can serve as molecular biosensors has opened up a new direction in heme biochemistry directed towards elucidating their structure-function relationships. Examples of such sensory heme proteins include the FixL proteins of Rhizobia involved in oxygen sensing, the CooA protein of Rhodospirillum rubrum that senses CO, and the mammalian soluble guanylate cyclase—the only proven nitric oxide receptor. This overview summarizes the current state of knowledge regarding the roles and mechanisms of these novel proteins and discusses the evidence for other putative heme protein sensors. These topics will be presented in the Heme Protein Biosensors Symposium at the First International Conference of Porphyrins and Phthalocyanines in Dijon, France.

Structure-function relations in physiology education: Where’s the mechanism?

2017 ◽  
Vol 41 (2) ◽  
pp. 270-278 ◽  
Author(s):  
Matthew E. Lira ◽  
Stephanie M. Gardner
Keyword(s):  
Biological Sciences ◽  
Structure Function ◽  
Cognitive Processes ◽  
Biological Organization ◽  
Physiological Mechanisms ◽  
Levels Of Organization ◽  
Organ Systems ◽  
Narrow Definition ◽  
Multiple Levels ◽  
Shed Light

Physiology demands systems thinking: reasoning within and between levels of biological organization and across different organ systems. Many physiological mechanisms explain how structures and their properties interact at one level of organization to produce emergent functions at a higher level of organization. Current physiology principles, such as structure-function relations, selectively neglect mechanisms by not mentioning this term explicitly. We explored how students characterized mechanisms and functions to shed light on how students make sense of these terms. Students characterized mechanisms as 1) processes that occur at levels of organization lower than that of functions; and 2) as detailed events with many steps involved. We also found that students produced more variability in how they characterized functions compared with mechanisms: students characterized functions in relation to multiple levels of organization and multiple definitions. We interpret these results as evidence that students see mechanisms as holding a more narrow definition than used in the biological sciences, and that students struggle to coordinate and distinguish mechanisms from functions due to cognitive processes germane to learning in many domains. We offer the instructional suggestion that we scaffold student learning by affording students opportunities to relate and also distinguish between these terms so central to understanding physiology.

scholarly journals MAL, but not MAL2, expression promotes the formation of cholesterol-dependent membrane domains that recruit apical proteins

2011 ◽  
Vol 439 (3) ◽  
pp. 497-504 ◽  
Author(s):  
Sai P. Ramnarayanan ◽  
Pamela L. Tuma
Keyword(s):  
Acyl Chain ◽  
Biochemical Properties ◽  
Membrane Domains ◽  
Lipid Domains ◽  
Hydrophobic Core ◽  
Lipid Domain ◽  
Apical Trafficking ◽  
Biochemical Approach ◽  
Detergent Resistant Membranes ◽  
Membrane Spanning

Our recent studies have been aimed at understanding the mechanisms regulating apical protein sorting in polarized epithelial cells. In particular, we have been investigating how lipid rafts serve to sort apical proteins in the biosynthetic pathway. The recent findings that lipid domains are too small or transient to host apically destined cargo have led to newer versions of the hypothesis that invoke proteins required for lipid domain coalescence and stabilization. MAL (myelin and lymphocyte protein) and its highly conserved family member, MAL2, have emerged as possible regulators of this process in the direct and indirect apical trafficking pathways respectively. To test this possibility, we took a biochemical approach. We determined that MAL, but not MAL2, self-associates, forms higher-order cholesterol-dependent complexes with apical proteins and promotes the formation of detergent-resistant membranes that recruit apical proteins. Such biochemical properties are consistent with a role for MAL in raft coalescence and stabilization. These findings also support a model whereby hydrophobic mismatch between the long membrane-spanning helices of MAL and the short-acyl-chain phospholipids in the Golgi drive formation of lipid domains rich in raft components that are characterized by a thicker hydrophobic core to alleviate mismatch.

The AGO proteins: an overview

2018 ◽  
Vol 399 (6) ◽  
pp. 525-547 ◽  
Author(s):  
Saife Niaz
Keyword(s):  
Protein Binding ◽  
Structure Function ◽  
Small Rnas ◽  
Biological Process ◽  
Biochemical Properties ◽  
The Core ◽  
Binding Partners

AbstractSmall RNAs govern almost every biological process in eukaryotes associating with the Argonaute (AGO) proteins to form the RNA-induced silencing complex (mRISC). AGO proteins constitute the core of RISCs with different members having variety of protein-binding partners and biochemical properties. This review focuses on the AGO subfamily of the AGOs that are ubiquitously expressed and are associated with small RNAs. The structure, function and role of the AGO proteins in the cell is discussed in detail.

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