Annexin

Last updated
Annexin
Annexin.png
Structure of human annexin III.
Identifiers
SymbolAnnexin
Pfam PF00191
InterPro IPR001464
PROSITE PDOC00195
SCOP2 2ran / SCOPe / SUPFAM
TCDB 1.A.31
OPM superfamily 41
OPM protein 1w3w
Available protein structures:
Pfam   structures / ECOD  
PDB RCSB PDB; PDBe; PDBj
PDBsum structure summary

Annexin is a common name for a group of cellular proteins. They are mostly found in eukaryotic organisms (animals, plants and fungi).

Contents

In humans, the annexins are found inside the cell. However some annexins (Annexin A1, Annexin A2, and Annexin A5) can be secreted from the cytoplasm to outside cellular environments, such as blood.

Annexin is also known as lipocortin. [1] Lipocortins suppress phospholipase A2. [2] Increased expression of the gene coding for annexin-1 is one of the mechanisms by which glucocorticoids (such as cortisol) inhibit inflammation.

Introduction

The protein family of annexins has continued to grow since their association with intracellular membranes was first reported in 1977. [3] The recognition that these proteins were members of a broad family first came from protein sequence comparisons and their cross-reactivity with antibodies. [4] One of these workers (Geisow) coined the name Annexin shortly after. [5]

As of 2002 160 annexin proteins have been identified in 65 different species. [6] The criteria that a protein has to meet to be classified as an annexin are: it has to be capable of binding negatively charged phospholipids in a calcium dependent manner and must contain a 70 amino acid repeat sequence called an annexin repeat. Several proteins consist of annexin with other domains like gelsolin. [7]

The basic structure of an annexin is composed of two major domains. The first is located at the COOH-terminal and is called the “core” region. The second is located at the NH2 terminal and is called the “head” region. [6] The core region consists of an alpha helical disk. The convex side of this disk has type 2 calcium-binding sites. They are important for allowing interaction with the phospholipids at the plasma membrane. [8] The N terminal region is located on the concave side of the core region and is important for providing a binding site for cytoplasmic proteins. In some annexins it can become phosphorylated and can cause affinity changes for calcium in the core region or alter cytoplasmic protein interaction.

Annexins are important in various cellular and physiological processes such as providing a membrane scaffold, which is relevant to changes in the cell's shape. Also, annexins have been shown to be involved in trafficking and organization of vesicles, exocytosis, endocytosis and also calcium ion channel formation. [9] Annexins have also been found outside the cell in the extracellular space and have been linked to fibrinolysis, coagulation, inflammation and apoptosis. [10]

The first study to identify annexins was published by Creutz et al. (1978). [11] These authors used bovine adrenal glands and identified a calcium dependent protein that was responsible for aggregation of granules amongst each other and the plasma membrane. This protein was given the name synexin, which comes from the Greek word “synexis” meaning “meeting”.

Structure

Several subfamilies of annexins have been identified based on structural and functional differences. However, all annexins share a common organizational theme that involves two distinct regions, an annexin core and an amino (N)-terminus. [9] The annexin core is highly conserved across the annexin family and the N-terminus varies greatly. [6] The variability of the N-terminus is a physical construct for variation between subfamilies of annexins.

The 310 amino acid annexin core has four annexin repeats, each composed of 5 alpha-helices. [9] The exception is annexin A-VI that has two annexin core domains connected by a flexible linker. [9] A-VI was produced via duplication and fusion of the genes for A-V and A-X and therefore will not be discussed in length. The four annexin repeats produce a curved protein and allow functional differences based on the structure of the curve. [6] The concave side of the annexin core interacts with the N-terminus and cytosolic second messengers, while the convex side of the annexin contains calcium binding sites. [12] Each annexin core contains one type II, also known as an annexin type, calcium binding site; these binding sites are the typical location of ionic membrane interactions. [6] However, other methods of membrane connections are possible. For example, A-V exposes a tryptophan residue, upon calcium binding, which can interact with the hydrocarbon chains of the lipid bilayer. [12]

The diverse structure of the N-terminus confers specificity to annexin intracellular signaling. In all annexins the N-terminus is thought to sit inside the concave side of the annexin core and folds separately from the rest of the protein. [6] The structure of this region can be divided into two broad categories, short and long N-termini. A short N-terminus, as seen in A-III, can consist of 16 or less amino acids and travels along the concave protein core interacting via hydrogen bonds. [9] Short N-termini are thought to stabilize the annexin complex in order to increase calcium binding and can be the sites for post-translational modifications. [9] Long N-termini can contain up to 40 residues and have a more complex role in annexin signaling. [6] For example, in A-I the N-terminus folds into an amphipathic alpha-helix and inserts into the protein core, displacing helix D of annexin repeat III. [6] However, when calcium binds, the N-terminus is pushed from the annexin core by conformational changes within the protein. [9] Therefore, the N-terminus can interact with other proteins, notably the S-100 protein family, and includes phosphorylation sites which allow for further signaling. [9] A-II can also use its long N-terminal to form a heterotrimer between a S100 protein and two peripheral annexins. [9] The structural diversity of annexins is the grounds for the functional range of these complex, intracellular messengers.

Cellular localization

Membrane

Annexins are characterized by their calcium dependent ability to bind to negatively charged phospholipids (i.e. membrane walls). [13] They are located in some but not all of the membranous surfaces within a cell, which would be evidence of a heterogeneous distribution of Ca2+ within the cell. [9]

Nuclei

Annexin species (II,V,XI) have been found within the membranes. [9] Tyrosine kinase activity has been shown to increase the concentrations of Annexins II,V within the nucleus. [9] Annexin XI is predominantly located within the nucleus, and absent from the nucleoli. [14] During prophase, annexin XI will translocate to the nuclear envelope. [14]

Bone

Annexins are abundant in bone matrix vesicles, and are speculated to play a role in Ca2+ entry into vesicles during hydroxyapatite formation. [15] The subject area has not been thoroughly studied, however it has been speculated that annexins may be involved in closing the neck of the matrix vesicle as it is endocytosed. [9]

Role in vesicle transport

Exocytosis

Annexins have been observed to play a role along the exocytotic pathway, specifically in the later stages, near or at the plasma membrane. [13] Evidence of annexins or annexin-like proteins are involved in exocytosis has been found in lower organisms, such as the Paramecium . [13] Through antibody recognition, there is evidence of the annexin like proteins being involved in the positioning and attachment of secretory organelles in the organism Paramecium. [13]

Annexin VII was the first annexin to be discovered while searching for proteins that promote the contact and fusion of chromaffin granules. [9] In Vitro studies however have shown that annexin VII does not promote the fusion of membranes, only the close attachment to one another. [11]

Endocytosis

Annexins have been found to be involved in the transport and also sorting of endocytotic events. Annexin one is a substrate of the EGF (epidermal growth factor) tyrosine kinase which becomes phosphorylated on its N terminus when the receptor is internalized. [13] Unique endosome targeting sequences have been found in the N terminus of annexins I and II, which would be useful in sorting of endocytotic vesicles. [9] Annexins are present in several different endocytotic processes. Annexin VI is thought to be involved in clathrin coated budding events, while annexin II participates in both cholesteryl ester internalization and the biogenesis of multi-vesicular endosomes. [9]

Membrane scaffolding

Annexins can function as scaffolding proteins to anchor other proteins to the cell membrane. Annexins assemble as trimers, [8] where this trimer formation is facilitated by calcium influx and efficient membrane binding. This trimer assembly is often stabilized by other membrane-bound annexin cores in the vicinity. Eventually, enough annexin trimers will assemble and bind the cell membrane. This will induce the formation of membrane-bound annexin networks. These networks can induce the indentation and vesicle budding during an exocytosis event. [16]

While different types of annexins can function as membrane scaffolds, annexin A-V is the most abundant membrane-bound annexin scaffold. Annexin A-V can form 2-dimensional networks when bound to the phosphatidylserine unit of the membrane. [17] Annexin A-V is effective in stabilizing changes in cell shape during endocytosis and exocytosis, as well as other cell membrane processes. Alternatively, annexins A-I and A-II bind phosphatidylserine and phosphatidylcholine units in the cell membrane, and are often found forming monolayered clusters that lack a definite shape. [18]

In addition, annexins A-I and A-II have been shown to bind PIP2 (phosphatidylinositol-4,5-bisphosphate) in the cell membrane and facilitate actin assembly near the membrane. [9] More recently, annexin scaffolding functions have been linked to medical applications. These medical implications have been uncovered with in vivo studies where the path of a fertilized egg is tracked to the uterus. After fertilization, the egg must enter a canal for which the opening is up to five times smaller than the diameter of the egg. Once the fertilized egg has passed through the opening, annexins are believed to promote membrane folding in an accordion-like fashion to return the stretched membrane back to its original form. Though this was discovered in the nematode annexin NEX-1, it is believed that a similar mechanism takes place in humans and other mammals. [19]

Membrane organization and trafficking

Several annexins have been shown to have active roles in the organization of the membrane. Annexin A-II has been extensively studied in this aspect of annexin function and is noted to be heavily involved in the organization of lipids in the bilayer near sites of actin cytoskeleton assembly. Annexin A-II can bind PIP2 in the cell membrane in vivo with a relatively high binding affinity. [20]

In addition, Annexin A-II can bind other membrane lipids such as cholesterol, where this binding is made possible by the influx of calcium ions. [21] The binding of Annexin A-II to lipids in the bilayer orchestrates the organization of lipid rafts in the bilayer at sites of actin assembly. In fact, annexin A-II is itself an actin-binding protein and therefore it can form a region of interaction with actin by means of its filamentous actin properties. In turn, this allows for further cell-cell interactions between monolayers of cells like epithelial and endothelial cells. [22] In addition to annexin A-II, annexin A-XI has also been shown to organize cell membrane properties. Annexin A-XI is believed to be highly involved in the last stage of mitosis: cytokinesis. It is in this stage that daughter cells separate from one another because annexin A-XI inserts a new membrane that is believed to be required for abscission. Without annexin A-XI, it is believed that the daughter cells with not fully separate and may undergo apoptosis. [23]

Clinical significance

Apoptosis and inflammation

Annexin A-I seems to be one of the most heavily involved annexins in anti-inflammatory responses. Upon infection or damage to tissues, annexin A-I is believed to reduce inflammation of tissues by interacting with annexin A-I receptors on leukocytes. In turn, the activation of these receptors functions to send the leukocytes to the site of infection and target the source of inflammation directly. [24] As a result, this inhibits leukocyte (specifically neutrophils) extravasation and down regulates the magnitude of the inflammatory response. Without annexin A-I in mediating this response, neutrophil extravasation is highly active and worsens the inflammatory response in damaged or infected tissues. [25]

Annexin A-I has also been implicated in apoptotic mechanisms in the cell. When expressed on the surface of neutrophils, annexin A-I promotes pro-apoptotic mechanisms. Alternatively, when expressed on the cell surface, annexin A-I promotes the removal of cells that have undergone apoptosis. [26] [27]

Moreover, annexin A-I has further medical implications in the treatment of cancer. Annexin A-I can be used as a cell surface protein to mark some forms of tumors that can be targeted by various immunotherapies with antibodies against annexin A-I. [28]

Coagulation

Annexin A-V is the major player when it comes to mechanisms of coagulation. Like other annexin types, annexin A-V can also be expressed on the cell surface and can function to form 2-dimensional crystals to protect the lipids of the cell membrane from involvement in coagulation mechanisms. [9] Medically speaking, phospholipids can often be recruited in autoimmune responses, most commonly observed in cases of fetal loss during pregnancy. In such cases, antibodies against annexin A-V destroy its 2-dimensional crystal structure and uncover the phospholipids in the membrane, making them available for contribution to various coagulation mechanisms. [29]

Fibrinolysis

While several annexins may be involved in mechanisms of fibrinolysis, annexin A-II is the most prominent in mediating these responses. The expression of annexin A-II on the cell surface is believed to serve as a receptor for plasminogen, which functions to produce plasmin. Plasmin initiates fibrinolysis by degrading fibrin. The destruction of fibrin is a natural preventative measure because it prevents the formation of blood clots by fibrin networks. [30]

Annexin A-II has medical implications because it can be utilized in treatments for various cardiovascular diseases that thrive on blood clotting through fibrin networks.

Types/subfamilies

Human proteins containing this domain

ANXA1; ANXA10; ANXA11; ANXA13; ANXA2; ANXA3; ANXA4; ANXA5; ANXA6; ANXA7; ANXA8; ANXA8L1; ANXA8L2; ANXA9;

Related Research Articles

<span class="mw-page-title-main">Endoplasmic reticulum</span> Cell organelle that synthesizes, folds and processes proteins

The endoplasmic reticulum (ER) is a part of a transportation system of the eukaryotic cell, and has many other important functions such as protein folding. It is a type of organelle made up of two subunits – rough endoplasmic reticulum (RER), and smooth endoplasmic reticulum (SER). The endoplasmic reticulum is found in most eukaryotic cells and forms an interconnected network of flattened, membrane-enclosed sacs known as cisternae, and tubular structures in the SER. The membranes of the ER are continuous with the outer nuclear membrane. The endoplasmic reticulum is not found in red blood cells, or spermatozoa.

<span class="mw-page-title-main">Vesicle (biology and chemistry)</span> Any small, fluid-filled, spherical organelle enclosed by a membrane

In cell biology, a vesicle is a structure within or outside a cell, consisting of liquid or cytoplasm enclosed by a lipid bilayer. Vesicles form naturally during the processes of secretion (exocytosis), uptake (endocytosis), and the transport of materials within the plasma membrane. Alternatively, they may be prepared artificially, in which case they are called liposomes. If there is only one phospholipid bilayer, the vesicles are called unilamellar liposomes; otherwise they are called multilamellar liposomes. The membrane enclosing the vesicle is also a lamellar phase, similar to that of the plasma membrane, and intracellular vesicles can fuse with the plasma membrane to release their contents outside the cell. Vesicles can also fuse with other organelles within the cell. A vesicle released from the cell is known as an extracellular vesicle.

<span class="mw-page-title-main">Lipid bilayer</span> Membrane of two layers of lipid molecules

The lipid bilayer is a thin polar membrane made of two layers of lipid molecules. These membranes are flat sheets that form a continuous barrier around all cells. The cell membranes of almost all organisms and many viruses are made of a lipid bilayer, as are the nuclear membrane surrounding the cell nucleus, and membranes of the membrane-bound organelles in the cell. The lipid bilayer is the barrier that keeps ions, proteins and other molecules where they are needed and prevents them from diffusing into areas where they should not be. Lipid bilayers are ideally suited to this role, even though they are only a few nanometers in width, because they are impermeable to most water-soluble (hydrophilic) molecules. Bilayers are particularly impermeable to ions, which allows cells to regulate salt concentrations and pH by transporting ions across their membranes using proteins called ion pumps.

<span class="mw-page-title-main">Phosphatidylinositol 4,5-bisphosphate</span> Chemical compound

Phosphatidylinositol 4,5-bisphosphate or PtdIns(4,5)P2, also known simply as PIP2 or PI(4,5)P2, is a minor phospholipid component of cell membranes. PtdIns(4,5)P2 is enriched at the plasma membrane where it is a substrate for a number of important signaling proteins. PIP2 also forms lipid clusters that sort proteins.

<span class="mw-page-title-main">Phospholipid scramblase</span> Protein

Scramblase is a protein responsible for the translocation of phospholipids between the two monolayers of a lipid bilayer of a cell membrane. In humans, phospholipid scramblases (PLSCRs) constitute a family of five homologous proteins that are named as hPLSCR1–hPLSCR5. Scramblases are members of the general family of transmembrane lipid transporters known as flippases. Scramblases are distinct from flippases and floppases. Scramblases, flippases, and floppases are three different types of enzymatic groups of phospholipid transportation enzymes. The inner-leaflet, facing the inside of the cell, contains negatively charged amino-phospholipids and phosphatidylethanolamine. The outer-leaflet, facing the outside environment, contains phosphatidylcholine and sphingomyelin. Scramblase is an enzyme, present in the cell membrane, that can transport (scramble) the negatively charged phospholipids from the inner-leaflet to the outer-leaflet, and vice versa.

<span class="mw-page-title-main">ADP ribosylation factor</span> Group of proteins

ADP ribosylation factors (ARFs) are members of the ARF family of GTP-binding proteins of the Ras superfamily. ARF family proteins are ubiquitous in eukaryotic cells, and six highly conserved members of the family have been identified in mammalian cells. Although ARFs are soluble, they generally associate with membranes because of N-terminus myristoylation. They function as regulators of vesicular traffic and actin remodelling.

In molecular biology, an annexin A5 affinity assay is a test to quantify the number of cells undergoing apoptosis. The assay uses the protein annexin A5 to tag apoptotic and dead cells, and the numbers are then counted using either flow cytometry or a fluorescence microscope.

<span class="mw-page-title-main">Annexin A2</span> Protein-coding gene in the species Homo sapiens

Annexin A2 also known as annexin II is a protein that in humans is encoded by the ANXA2 gene.

<span class="mw-page-title-main">Annexin A5</span> Protein-coding gene in the species Homo sapiens

Annexin A5 is a cellular protein in the annexin group. In flow cytometry, annexin V is commonly used to detect apoptotic cells by its ability to bind to phosphatidylserine, a marker of apoptosis when it is on the outer leaflet of the plasma membrane. The function of the protein is unknown; however, annexin A5 has been proposed to play a role in the inhibition of blood coagulation by competing for phosphatidylserine binding sites with prothrombin and also to inhibit the activity of phospholipase A1. These properties have been found by in vitro experiments.

<span class="mw-page-title-main">Ezrin</span> Protein-coding gene in the species Homo sapiens

Ezrin also known as cytovillin or villin-2 is a protein that in humans is encoded by the EZR gene.

<span class="mw-page-title-main">Annexin A6</span> Protein-coding gene in the species Homo sapiens

Annexin A6 is a protein that in humans is encoded by the ANXA6 gene.

<span class="mw-page-title-main">S100A10</span> Protein-coding gene in the species Homo sapiens

S100 calcium-binding protein A10 (S100A10), also known as p11, is a protein that is encoded by the S100A10 gene in humans and the S100a10 gene in other species. S100A10 is a member of the S100 family of proteins containing two EF-hand calcium-binding motifs. S100 proteins are localized in the cytoplasm and/or nucleus of a wide range of cells. They regulate a number of cellular processes such as cell cycle progression and differentiation. The S100 protein is implicated in exocytosis and endocytosis by reorganization of F-actin.

<span class="mw-page-title-main">S100A11</span> Protein-coding gene in the species Homo sapiens

S100 calcium-binding protein A11 (S100A11) is a protein that in humans is encoded by the S100A11 gene.

<span class="mw-page-title-main">Annexin A4</span> Protein-coding gene in the species Homo sapiens

Annexin A4 is a protein that in humans is encoded by the ANXA4 gene.

<span class="mw-page-title-main">Annexin A7</span> Protein-coding gene in the species Homo sapiens

Annexin A7 is a protein that in humans is encoded by the ANXA7 gene.

<span class="mw-page-title-main">ANXA8L2</span> Protein

Annexin A8-like protein 2 is a protein that in humans is encoded by the ANXA8L2 gene.

<span class="mw-page-title-main">SCIN</span> Protein-coding gene in the species Homo sapiens

Scinderin is a protein that in humans is encoded by the SCIN gene. Scinderin is an actin severing protein belonging to the gelsolin superfamily. It was discovered in Dr. Trifaro's laboratory at the University of Ottawa, Canada. Secretory tissues are rich in scinderin. In these tissues scinderin, a calcium dependent protein, regulates cortical actin networks. Normally secretory vesicles are excluded from release sites on the plasma membrane by the presence of a cortical actin filament network. During cell stimulation, calcium channels open allowing calcium ions to enter the secretory cell. Increase in intracellular calcium activates scinderin with the consequent actin filament severing and local dissociation of actin filament networks. This allows the movement of secretory vesicles to release sites on the plasma membrane.

<span class="mw-page-title-main">Annexin A9</span> Protein-coding gene in the species Homo sapiens

Annexin A9 is a protein that in humans is encoded by the ANXA9 gene.

<span class="mw-page-title-main">Lipid bilayer fusion</span>

In membrane biology, fusion is the process by which two initially distinct lipid bilayers merge their hydrophobic cores, resulting in one interconnected structure. If this fusion proceeds completely through both leaflets of both bilayers, an aqueous bridge is formed and the internal contents of the two structures can mix. Alternatively, if only one leaflet from each bilayer is involved in the fusion process, the bilayers are said to be hemifused. In hemifusion, the lipid constituents of the outer leaflet of the two bilayers can mix, but the inner leaflets remain distinct. The aqueous contents enclosed by each bilayer also remain separated.

<span class="mw-page-title-main">Ferlins</span> Protein family

Ferlins are an ancient protein family involved in vesicle fusion and membrane trafficking. Ferlins are distinguished by their multiple tandem C2 domains, and sometimes a FerA and a DysF domain. Mutations in ferlins can cause human diseases such as muscular dystrophy and deafness. Abnormalities in expression of myoferlin, a human ferlin protein, is also directly associated with higher mortality rate and tumor recurrence in several types of cancer, including pancreatic, colorectal, breast, cervical, stomach, ovarian, cervical, thyroid, endometrial, and oropharyngeal squamous cell carcinoma. In other animals, ferlin mutations can cause infertility.

References

  1. ↑ Annexins at the U.S. National Library of Medicine Medical Subject Headings (MeSH)
  2. ↑ "lipocortin definition". Archived from the original on 2007-06-14. Retrieved 2007-03-10.
  3. ↑ Donnelly SR, Moss SE (June 1997). "Annexins in the secretory pathway". Cell. Mol. Life Sci. 53 (6): 533–8. doi:10.1007/s000180050068. PMC   11147375 . PMID   9230932. S2CID   36108081.
  4. ↑ Geisow MJ, Fritsche U, Hexham JM, Dash B, Johnson T (April 1986). "A consensus sequence repeat in Torpedo and mammalian calcium-dependent membrane binding proteins". Nature. 320 (6063): 636–38. doi:10.1038/320636a0. PMID   2422556. S2CID   4361070.
  5. ↑ Geisow MJ, Walker JH, Boustead C, Taylor W (April 1987). "Annexins – a new family of Ca2+ -regulated phospholipid-binding protein". Biosci. Rep. 7 (4): 289–98. doi:10.1007/BF01121450. PMID   2960386. S2CID   20709760.
  6. 1 2 3 4 5 6 7 8 Gerke V, Moss S (2002). "Annexins: form structure to function". Physiol. Rev. 82 (2): 331–71. doi:10.1152/physrev.00030.2001. PMID   11917092.
  7. ↑ Ghoshdastider, U; Popp, D; Burtnick, L. D.; Robinson, R. C. (2013). "The expanding superfamily of gelsolin homology domain proteins". Cytoskeleton. 70 (11): 775–95. doi:10.1002/cm.21149. PMID   24155256. S2CID   205643538.
  8. 1 2 Oling F, Santos JS, Govorukhina N, Mazères-Dubut C, Bergsma-Schutter W, Oostergetel G, Keegstra W, Lambert O, Lewit-Bentley A, Brisson A (December 2000). "Structure of membrane-bound annexin A5 trimers: a hybrid cryo-EM – X-ray crystallography study". J. Mol. Biol. 304 (4): 561–73. doi:10.1006/jmbi.2000.4183. PMID   11099380.
  9. 1 2 3 4 5 6 7 8 9 10 11 12 13 14 15 16 17 18 Gerke V, Creutz CE, Moss SE (June 2005). "Annexins: linking Ca2+ signalling to membrane dynamics". Nat. Rev. Mol. Cell Biol. 6 (6): 449–61. doi:10.1038/nrm1661. PMID   15928709. S2CID   37526262.
  10. ↑ van Genderen HO, Kenis H, Hofstra L, Narula J, Reutelingsperger CP (June 2008). "Extracellular annexin A5: functions of phosphatidylserine-binding and two-dimensional crystallization". Biochim. Biophys. Acta. 1783 (6): 953–63. doi: 10.1016/j.bbamcr.2008.01.030 . PMID   18334229.
  11. 1 2 Creutz Carl E.; Pazoles Christopher J.; Pollard Harvey B. (April 1978). "Identification and purification of an adrenal medullary protein (synexin) that causes calcium-dependent aggregation of isolated chromaffin granules". Journal of Biological Chemistry. 253 (8): 2858–66. doi: 10.1016/S0021-9258(17)40901-X . PMID   632306.
  12. 1 2 Concha NO, Head JF, Kaetzel MA, Dedman JR, Seaton BA (September 1993). "Rat annexin V crystal structure: Ca(2+)-induced conformational changes". Science. 261 (5126): 1321–4. Bibcode:1993Sci...261.1321C. doi:10.1126/science.8362244. PMID   8362244.
  13. 1 2 3 4 5 Gerke V, Moss SE (June 1997). "Annexins and membrane dynamics". Biochim. Biophys. Acta. 1357 (2): 129–54. doi: 10.1016/S0167-4889(97)00038-4 . PMID   9223619.
  14. 1 2 Tomas A, Moss S (2003). "Calcium- and Cell Cycle-dependent Association of Annexin 11 with the Nuclear Envelope". J. Biol. Chem. 278 (22): 20210–20216. doi: 10.1074/jbc.M212669200 . hdl: 10044/1/42329 . PMID   12601007.
  15. ↑ Genge BR, Wu LN, Wuthier RE (March 1990). "Differential fractionation of matrix vesicle proteins. Further characterization of the acidic phospholipid-dependent Ca2+–binding proteins". J. Biol. Chem. 265 (8): 4703–10. doi: 10.1016/S0021-9258(19)39619-X . PMID   2155235.
  16. ↑ Kenis H, van Genderen H, Bennaghmouch A, Rinia HA, Frederik P, Narula J, Hofstra L, Reutelingsperger CP (December 2004). "Cell surface-expressed phosphatidylserine and annexin A5 open a novel portal of cell entry". J. Biol. Chem. 279 (50): 52623–9. doi: 10.1074/jbc.M409009200 . PMID   15381697.
  17. ↑ Pigault C, Follenius-Wund A, Schmutz M, Freyssinet JM, Brisson A (February 1994). "Formation of two-dimensional arrays of annexin V on phosphatidylserine-containing liposomes". J. Mol. Biol. 236 (1): 199–208. doi:10.1006/jmbi.1994.1129. PMID   8107105.
  18. ↑ Janshoff A, Ross M, Gerke V, Steinem C (August 2001). "Visualization of annexin I binding to calcium-induced phosphatidylserine domains". ChemBioChem. 2 (7–8): 587–90. doi:10.1002/1439-7633(20010803)2:7/8<587::AID-CBIC587>3.0.CO;2-Q. PMID   11828493. S2CID   23310803.
  19. ↑ Creutz CE, Snyder SL, Daigle SN, Redick J (March 1996). "Identification, localization, and functional implications of an abundant nematode annexin". J. Cell Biol. 132 (6): 1079–92. doi:10.1083/jcb.132.6.1079. PMC   2120750 . PMID   8601586.
  20. ↑ Rescher U, Ruhe D, Ludwig C, Zobiack N, Gerke V (July 2004). "Annexin 2 is a phosphatidylinositol (4,5)-bisphosphate binding protein recruited to actin assembly sites at cellular membranes". J. Cell Sci. 117 (Pt 16): 3473–80. doi: 10.1242/jcs.01208 . PMID   15226372.
  21. ↑ Rescher U, Gerke V (June 2004). "Annexins--unique membrane binding proteins with diverse functions". J. Cell Sci. 117 (Pt 13): 2631–9. doi: 10.1242/jcs.01245 . PMID   15169834.
  22. ↑ Hayes MJ, Rescher U, Gerke V, Moss SE (August 2004). "Annexin-actin interactions". Traffic. 5 (8): 571–6. doi: 10.1111/j.1600-0854.2004.00210.x . PMID   15260827. S2CID   11551148.
  23. ↑ Tomas A, Futter C, Moss SE (2004). "Annexin 11 is required for midbody formation and completion of the terminal phase of cytokinesis". J. Cell Biol. 165 (6): 813–822. doi:10.1083/jcb.200311054. PMC   2172404 . PMID   15197175.
  24. ↑ Prossnitz ER, Ye RD (1997). "The N-formyl peptide receptor: a model for the study of chemoattractant receptor structure and function". Pharmacol. Ther. 74 (1): 73–102. doi:10.1016/S0163-7258(96)00203-3. PMID   9336017.
  25. ↑ Hannon R, Croxtall JD, Getting SJ, Roviezzo F, Yona S, Paul-Clark MJ, Gavins FN, Perretti M, Morris JF, Buckingham JC, Flower RJ (February 2003). "Aberrant inflammation and resistance to glucocorticoids in annexin 1-/- mouse". FASEB J. 17 (2): 253–5. doi: 10.1096/fj.02-0239fje . PMID   12475898. S2CID   18895764.
  26. ↑ Arur S, Uche UE, Rezaul K, Fong M, Scranton V, Cowan AE, Mohler W, Han DK (April 2003). "Annexin I is an endogenous ligand that mediates apoptotic cell engulfment". Dev. Cell. 4 (4): 587–98. doi: 10.1016/S1534-5807(03)00090-X . PMID   12689596.
  27. ↑ Arur, S.; et al. (2003). "Annexin I is an endogenous ligand that mediates apoptotic cell engulfment". Dev. Cell . 4 (4): 587–598. doi: 10.1016/S1534-5807(03)00090-X . PMID   12689596.
  28. ↑ Oh P, Li Y, Yu J, Durr E, Krasinska KM, Carver LA, Testa JE, Schnitzer JE (June 2004). "Subtractive proteomic mapping of the endothelial surface in lung and solid tumours for tissue-specific therapy". Nature. 429 (6992): 629–35. Bibcode:2004Natur.429..629O. doi:10.1038/nature02580. PMID   15190345. S2CID   4386303.
  29. ↑ Rand JH (September 2000). "Antiphospholipid antibody-mediated disruption of the annexin-V antithrombotic shield: a thrombogenic mechanism for the antiphospholipid syndrome". J. Autoimmun. 15 (2): 107–11. doi:10.1006/jaut.2000.0410. PMID   10968894.
  30. ↑ Ling Q, Jacovina AT, Deora A, Febbraio M, Simantov R, Silverstein RL, Hempstead B, Mark WH, Hajjar KA (January 2004). "Annexin II regulates fibrin homeostasis and neoangiogenesis in vivo". J. Clin. Invest. 113 (1): 38–48. doi:10.1172/JCI19684. PMC   300771 . PMID   14702107.

Further reading

This page is based on this Wikipedia article
Text is available under the CC BY-SA 4.0 license; additional terms may apply.
Images, videos and audio are available under their respective licenses.