Редактирование: ANXA5

Annexin A5 (Anchorin CII) (Annexin V) (Annexin-5) (Calphobindin I) (CBP-I) (Endonexin II) (Lipocortin V) (Placental anticoagulant protein 4) (PP4) (Placental anticoagulant protein I) (PAP-I) (Thromboplastin inhibitor) (Vascular anticoagulant-alpha) (VAC-alpha) [ANX5] [ENX2] [PP4]

==Publications==

{{medline-entry
|title=Annexin V, annexin VI, [[S100A1]] and [[S100B]] in developing and adult avian skeletal muscles.
|pubmed-url=https://pubmed.ncbi.nlm.nih.gov/11801372
|abstract=Annexins and S100 proteins constitute two multigenic families of Ca2 -modulated proteins that have been implicated in the regulation of both intracellular and extracellular activities. Some annexins can interact with certain S100 protein dimers thereby forming heterotetramers in which an S100 dimer crosslinks two copies of the partner annexin. It is suggested that S100 protein binding to an annexin might serve the function of regulating annexin function and annexin binding to an S100 protein might regulate S100 function. In the present study, annexin V, annexin VI (or [[ANXA5]] and [[ANXA6]], respectively, according to a novel nomenclature), [[S100A1]] and [[S100B]] were analyzed for their subcellular localization in developing and adult avian skeletal muscles by confocal laser scanning microscopy, immunogold cytochemistry, and western blotting, and for their ability to form annexin-S100 heterocomplex in vivo by immunoprecipitation. These four proteins displayed distinct expression patterns, [[ANXA5]] being the first to be expressed in myotubes (i.e. at embryonic day 8), followed by [[ANXA6]] (at embryonic day 12) and [[S100A1]] and [[S100B]] (between embryonic day 12 and embryonic day 15). The two annexins and the two S100 proteins were found associated to different extents with the sarcolemma, membranes of the sarcoplasmic reticulum, and putative transverse tubules where they appeared to be co-localized from embryonic day 18 onwards. No one of these proteins was found associated with the contractile apparatus of the sarcomeres. Immunoprecipitation studies indicated that [[ANXA6]]/[[S100A1]] and [[ANXA6]]/[[S100B]] complexes formed in vivo. Whereas, [[ANXA5]] was not recovered in [[S100A1]] or [[S100B]] immunoprecipitates. From our data we suggest that: (i) [[ANXA5]] and [[ANXA6]], and [[S100A1]] and [[S100B]] can be used as markers of skeletal muscle development; (ii) [[ANXA6]] and [[S100A1]] and [[S100B]] appear strategically located close to or on skeletal muscle membrane organelles that are critically involved in the regulation of Ca2  fluxes, thus supporting previous in vitro observations implicating [[S100A1]] and [[ANXA6]] in the stimulation of Ca2 -induced Ca2  release; and (iii) [[ANXA6]]/[[S100A1]] and [[ANXA6]]/[[S100B]] complexes can form in vivo thereby regulating each other activities and/or acting in concert to regulate membrane-associated activities.
|mesh-terms=* Aging
* Animals
* Annexin A5
* Annexin A6
* Calcium Signaling
* Calcium-Binding Proteins
* Cell Differentiation
* Chick Embryo
* Chickens
* Gene Expression Regulation, Developmental
* Immunohistochemistry
* Intracellular Membranes
* Microscopy, Confocal
* Microscopy, Electron
* Muscle Fibers, Skeletal
* Muscle, Skeletal
* Nerve Growth Factors
* S100 Calcium Binding Protein beta Subunit
* S100 Proteins
* Subcellular Fractions

|full-text-url=https://sci-hub.do/10.1016/s0306-4522(01)00330-x
}}