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International Microbiology : the... Jun 2019Oxysterol-binding protein is an important non-vesicular trafficking protein involved in the transportation of lipids in eukaryotic cells. Oxysterol-binding protein is... (Review)
Review
Oxysterol-binding protein is an important non-vesicular trafficking protein involved in the transportation of lipids in eukaryotic cells. Oxysterol-binding protein is identified as oxysterol-binding protein-related proteins (ORPs) in mammals and oxysterol-binding protein homologue (Osh) in yeast. Research has described the function and structure of oxysterol-binding protein in mammals and yeast, but little information about the protein's structure and function in filamentous fungi has been reported. This article focuses on recent advances in the research of Osh proteins in yeast and filamentous fungi, such as Aspergillus oryzae, Aspergillus nidulans, and Candida albicans. Furthermore, we point out some problems in the field, summarizing the membrane contact sites (MCS) of Osh proteins in yeast, and consider the future of Osh protein development.
Topics: Carrier Proteins; Fungal Proteins; Fungi; Lipid Metabolism; Protein Domains; Receptors, Steroid; Yeasts
PubMed: 30810998
DOI: 10.1007/s10123-019-00056-6 -
Journal of Biomedicine & Biotechnology 2010Myosin binding protein C (MyBP-C) consists of a family of thick filament associated proteins. Three isoforms of MyBP-C exist in striated muscles: cardiac, slow skeletal,... (Review)
Review
Myosin binding protein C (MyBP-C) consists of a family of thick filament associated proteins. Three isoforms of MyBP-C exist in striated muscles: cardiac, slow skeletal, and fast skeletal. To date, most studies have focused on the cardiac form, due to its direct involvement in the development of hypertrophic cardiomyopathy. Here we focus on the slow skeletal form, discuss past and current literature, and present evidence to support that: (i) MyBP-C slow comprises a subfamily of four proteins, resulting from complex alternative shuffling of the single MyBP-C slow gene, (ii) the four MyBP-C slow isoforms are expressed in variable amounts in different skeletal muscles, (iii) at least one MyBP-C slow isoform is preferentially found at the periphery of M-bands and (iv) the MyBP-C slow subfamily may play important roles in the assembly and stabilization of sarcomeric M- and A-bands and regulate the contractile properties of the actomyosin filaments.
Topics: Animals; Carrier Proteins; Humans; Protein Isoforms
PubMed: 20396395
DOI: 10.1155/2010/652065 -
Biochimica Et Biophysica Acta Nov 1999Muscle or heart fatty acid-binding protein is a low molecular weight protein that binds long-chain fatty acids in the cytosol of muscle tissues. The three-dimensional... (Review)
Review
Muscle or heart fatty acid-binding protein is a low molecular weight protein that binds long-chain fatty acids in the cytosol of muscle tissues. The three-dimensional structure of the human, bovine and insect proteins are known, either via X-ray or NMR techniques. The folding of the protein closely resembles that of the other FABPs: ten anti-parallel beta-strands are arranged to form a clam shell, closed at one end by two alpha-helices. This arrangement allows the formation of an internal cavity where the fatty acid can be accommodated, protected and isolated from the external environment. The fatty acid in the protein interior is stabilized by electrostatic and hydrogen bond interactions of its carboxylic head with charged or polar residues of the protein and by interactions of its tail with hydrophobic residues. The three-dimensional structure of different fatty acid-protein complexes along with molecular dynamics simulations are now providing insight into the molecular details of the specificity of the ligand binding.
Topics: Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins; Cattle; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Humans; Models, Molecular; Molecular Sequence Data; Muscles; Myelin P2 Protein; Myocardium; Neoplasm Proteins; Protein Structure, Secondary; Tumor Suppressor Proteins
PubMed: 10570238
DOI: 10.1016/s1388-1981(99)00163-8 -
Journal of Muscle Research and Cell... Mar 2011
Review
Topics: Animals; Carrier Proteins; Humans; Muscle, Skeletal; Myocytes, Cardiac; Protein Isoforms
PubMed: 21229295
DOI: 10.1007/s10974-010-9235-4 -
Current Opinion in Biotechnology Feb 2006The bacterial periplasmic-binding protein (PBP) superfamily members, in particular the maltose-binding protein, have been used extensively to prototype a variety of... (Review)
Review
The bacterial periplasmic-binding protein (PBP) superfamily members, in particular the maltose-binding protein, have been used extensively to prototype a variety of biosensing platforms. Although quite diverse at the primary sequence level, this protein superfamily retains the same basic two-domain structure, and upon binding a recognized ligand almost all PBPs undergo a conformational change to a closed structure. This process forms the basis for most, but not all, PBP-based biosensor signal transduction. Many direct detection or reagentless sensing modalities have been utilized with maltose-binding protein for both in vitro and in vivo detection of target compounds. Signal transduction modalities developed to date include direct fluorescence, electrochemical detection, fluorescence resonance energy transfer (FRET)-based detection, surface-tethered FRET sensing, hybrid quantum dot FRET sensing, and enzymatic detection, each of which have different benefits, potential applications and limitations.
Topics: Biosensing Techniques; Carrier Proteins; Electrochemistry; Fluorescence; Fluorescence Resonance Energy Transfer; Fluorescent Dyes; Maltose-Binding Proteins; Periplasmic Binding Proteins; Protein Conformation; Quantum Dots
PubMed: 16413768
DOI: 10.1016/j.copbio.2006.01.002 -
Biochemical Society Transactions Aug 2016Polypyrimidine tract binding protein (PTBP1) is a heterogeneous nuclear ribonucleoprotein (hnRNP) that plays roles in most stages of the life-cycle of pre-mRNA and mRNAs... (Review)
Review
Polypyrimidine tract binding protein (PTBP1) is a heterogeneous nuclear ribonucleoprotein (hnRNP) that plays roles in most stages of the life-cycle of pre-mRNA and mRNAs in the nucleus and cytoplasm. PTBP1 has four RNA binding domains of the RNA recognition motif (RRM) family, each of which can bind to pyrimidine motifs. In addition, RRM2 can interact via its dorsal surface with proteins containing short peptide ligands known as PTB RRM2 interacting (PRI) motifs, originally found in the protein Raver1. Here we review our recent progress in understanding the interactions of PTB with RNA and with various proteins containing PRI ligands.
Topics: Binding Sites; Carrier Proteins; Heterogeneous-Nuclear Ribonucleoproteins; Humans; Ligands; Models, Genetic; Nuclear Proteins; Peptides; Polypyrimidine Tract-Binding Protein; RNA Precursors; RNA-Binding Proteins; Ribonucleoproteins
PubMed: 27528752
DOI: 10.1042/BST20160080 -
Acta Paediatrica (Oslo, Norway : 1992).... Oct 1996
Review
Topics: Animals; Carrier Proteins; Growth Hormone; Humans
PubMed: 9055926
DOI: 10.1111/j.1651-2227.1996.tb14312.x -
Hormone Research 1996Corticotropin-releasing hormone-binding protein (CRFBP) is a 37-kD protein of 322 amino acids, containing one putative N-glycosylation site and 11 cysteines, 10 of which... (Review)
Review
Corticotropin-releasing hormone-binding protein (CRFBP) is a 37-kD protein of 322 amino acids, containing one putative N-glycosylation site and 11 cysteines, 10 of which remain in the mature molecule (298 amino acids) and result essential for the action. CRFBP protein gene has been cloned and mapped to the distal region of chromosome 13 and loci5q in the mouse and human genomes. CRFBP is the only example of a neuropeptide-binding protein. It is produced in human and rat brain, and in human liver and placenta. In brain, the central distribution of CRFBP shares some regional overlap with CRF receptor-bindings sites. Additionally, in hypothalamic and limbic structures, CRFBP has been identified in association with CRF-expressing cell groups. CRFBP has been also demonstrated in the human placenta and related membranes. Indeed, amniotic epithelium, chorionic cytotrophoblast, and maternal decidua also show intense positive CRFBP mRNA signals. Circulating CRFBP levels in healthy nonpregnant individuals show the same range values as in maternal plasma collected during the first and second trimesters of pregnancy. A rise in CRFBP levels at 30-35 weeks of pregnancy with a dramatic decrease at 38-40 weeks have been shown. At postpartum, CRFBP levels in maternal plasma reach the nonpregnant concentrations. Recombinant and native CRFBP neutralize the ACTH-releasing activity of human CRF in cultured pituitary or placental cells and, additionally, may block the activity of CRF on human pregnant endometrium prostaglandin release and on human myometrium contractility in vitro. These findings suggest that CRFBP may play a role in modulating the functions of CRF in human pregnancy.
Topics: Body Fluids; Carrier Proteins; Female; Humans; Pregnancy; RNA, Messenger; Tissue Distribution
PubMed: 8964581
DOI: 10.1159/000184785 -
Molecular and Cellular BiochemistryAcyl-CoA-binding protein is a 10 Kd protein which binds medium- and long-chain acyl-CoA esters with high affinity. The concentration in liver is 2-4 times the acyl-CoA... (Review)
Review
Acyl-CoA-binding protein is a 10 Kd protein which binds medium- and long-chain acyl-CoA esters with high affinity. The concentration in liver is 2-4 times the acyl-CoA concentration. ACBP has much greater affinity for acyl-CoA than FABP. FABP from bovine heart and liver is unable to compete with multilamellar liposomes, Lipidex and microsomal membrane in binding acyl-CoA esters, whereas ACBP effectively extracts acyl-CoA from all those sources. Previously published results on the effect of FABP on acyl-CoA metabolism need to be reevaluated due to possible contamination with ACBP. Recently it was discovered that ACBP is identical to a putative neurotransmitter diazepam binding inhibitor. The possibility therefore exists that ACBP has more than one function.
Topics: Acyl Coenzyme A; Amino Acid Sequence; Animals; Binding Sites; Carrier Proteins; Diazepam Binding Inhibitor; Fatty Acid-Binding Protein 7; Fatty Acid-Binding Proteins; Humans; Ligands; Liver; Molecular Sequence Data; Neoplasm Proteins; Neuropeptides; Tumor Suppressor Proteins
PubMed: 2266962
DOI: 10.1007/BF00231387 -
Acta Endocrinologica 1991The presence in the serum of several animal species of highly specific binding proteins for growth hormone is now accepted. The major binding protein is a truncated,... (Comparative Study)
Comparative Study Review
The presence in the serum of several animal species of highly specific binding proteins for growth hormone is now accepted. The major binding protein is a truncated, variant form of the target tissue GH receptor and is synthesized by all tissues expressing the full-length GH receptor. The GH receptor and GH binding protein are not co-ordinately expressed, being produced in variable ratios between tissues. Such independence of expression suggests that the synthesis of the GH binding protein is regulated and therefore may be biologically relevant. The GH binding protein has been shown to increase the half-life of circulating GH by decreasing the metabolic clearance rate and degradation rate; to limit the volume of distribution of bound GH to approximately twice the intravascular space; and to inhibit receptor binding and biological actions of GH in in vitro model systems. These observations suggest that circulating GH binding protein does have a functional role in modulating both the circulating concentrations of GH and its availability and effectiveness for target tissue interaction. Other possible, but as yet unproven, functions for the GH binding protein are briefly discussed. The ability to produce GH binding protein by recombinant means should allow additional, more definitive studies to be performed, thereby providing greater opportunity to define the true biological role(s) of the GH binding protein in the metabolism and function of GH.
Topics: Animals; Carrier Proteins; Female; Growth Hormone; Humans; Male; Pregnancy; Tissue Distribution
PubMed: 1853676
DOI: No ID Found