LECSTER LECTIN DATABASE










LECSTER is the largest, open-access searchable database of lectin characterizations, clinical correlates and citations on the Internet.


Programmed and curated by Peter D'Adamo.

Copyright 2001-2011.



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Total number of records: 619 Matching records: 1

Homo sapiens :
Annexin I (Lipocortin-1), ANX1



Molecular structure of
:Annexin I (Lipocortin-1), ANX1

Homo sapiens



Lecster ID:355 Edit Entry
Source Organism:
Species:Homo sapiens
Common Nomenclature:Annexin I (Lipocortin-1), ANX1
Class:Annexin
Index Nomenclature:ANNh.Hom.Sap.xx.Xxx1
Characterization Notes:Annexin I (lipocortin 1) has a molecular weight of 37kDa and is found abundantly in mammalian tissues but has a discrete pattern of cellulardistribution which includes secretory epithelium, skin, synovium and blood leukocytes. Convincing evidence now exists that synthesis of this member of the annexin family can be induced in monocytes and differentiated macrophage-like cell lines by glucocorticoids. However the synthesis of annexin I does not appear to be under glucocorticoid control in certain cell lines where its expression appears to be associated withcell differentiation and growth.
Biological Activity:ANX1 induces a dose- and time-dependent decrease in L-selectin expression on both peripheral blood neutrophils and monocytes but has no effect on lymphocytes. The loss of L-selectin from neutrophils is due to shedding that is mediated by a cell surface metalloprotease ("sheddase"). See: J Immunol 2001 May 15;166(10):6294-300 Members of the annexin family of molecules have been attributed with a wide range of potential functions, some of which could affect the responsiveness of immunocompetent cells. Certainannexins (eg annexin VII) have been reported to act as calcium channels in reconstituted phospholipid membranes;annexin I has been implicated in signal transduction pathways through being a substrate for the epidermal growth factor tyrosine kinase. Membrane fusion activities that are potentially important in phagocytosis, includingneutrophil granule aggregation and release,have been reported to involve lipocortins. Also, the ability of annexin I to be cross-linked by transglutaminases in response to glucocorticoids could be a crucial cytoskeletal event in differentiating cells. Several pharmacological studies have indicated a role for the recombinant human protein and derived peptide fragments as inhibitors ofinflammation, cytokine- mediated pyrogenesis and cerebral ischemia. Extracellular actions of recombinant annexin I on cells involved in immune responses are significant and parallel some of the effects of glucocorticoids. Exogenous recombinant annexin I has been demonstrated to mimic glucocorticoid- induced growth arrest in a lung carcinoma-derived epithelial cell line. An indication that the exogenous protein may mediate its effects through specific cell surface receptors come from the identification of specific lipocortin binding molecules on the surface of peripheral blood monocytes and polymorphonuclear leukocytes. The expression of these surface molecules on leukocytes from patients with rheumatoid arthritis is significantly reduced when compared to healthy individuals or patients with psoriasis or ankylosing spondilitis.
Source Tissue:
Specificity:
Inhibitors:
References:Prot Sci 1993, (2) 448-458





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2014-8-1: Current Date 12:15:36 GMT: Current Time

By Peter D'Adamo. Copyright 2001-2011.