Immunohistochemical localization of annexin V (CaBP33) in rat organs.

Abstract

We investigated the cellular distribution of annexin V (CaBP33) in rat tissues by immunohistochemistry. Several cell types were shown to express the protein. Glial cells in the cerebellum and in the optic nerve, the cornea! epitheium, the posterior epitheium in the iris, chondrocytes, skeletal muscle cells and cardiomyocytes, the capillary endotheial cells in many organs, the muscularis mucosae and the muscular layer in the intestinal tract, hepatocytes, Muller cells in the retina, the lens fibers, Sertoi and Leydig cells in the testis, and smooth muscle cells in the epididymis and bronchi displayed intense immunostaining. In the adrenal gland, only the cortex showed inununoreaction product. In the kidney, no apparent staining ofrenal cells was observed, whereas

‘Neuron‐specific’ protein gene product 9.5 (PGP 9.5) is also expressed in glioma cell lines and its expression depends on cellular growth state

“…3). This antiserum decorated cell bodies and the dendritic tree of Purkinje cells in rat cerebellum and no other elements in the cerebellar cortex [20], axons in the cerebellar white matter (not shown), and rat cerebellar Purkinje cells and 1 2 3 4 Fig. 3.…”

Annexin 5 Messenger Ribonucleic Acid Expression in Pituitary Gonadotropes Is Induced by Gonadotropin-Releasing Hormone (GnRH) and Modulates GnRH Stimulation of Gonadotropin Release

“…A high affinity for collagen has been reported, and a role in cellular adhesion to basement membranes has been suggested [10]. Annexin 5 distributes widely among tissues, and the distribution is specific to cell species [11, 12]. Also, annexin 5 can be utilized as a marker protein of ovarian tumors [13], and an autoantibody against annexin 5 is detected in some patients with lupus erythematosus [14].…”

DT40 cells lacking the Ca 2+ -binding protein annexin 5 are resistant to Ca 2+ -dependent apoptosis

“…Annexins are evolutionarily ancient and have undergone extensive diversification during vertebrate evolution, suggesting continuing important cellular roles, although their functions are not clearly defined. Both Anx2 and Anx5 are widely expressed, although Anx5 expression is particularly prominent in skeletal, cardiac, and smooth muscle, Leydig cells, endothelia, chondrocytes, and some neurons (3)(4)(5)(6)(7)(8). Like many annexins, Anx2 and Anx5 are predominantly intracellular, existing both as soluble cytosolic proteins and also in Ca 2ϩ -dependent and Ca 2ϩ -independent association with a range of intracellular membranes (9)(10)(11)(12), including the plasma membrane and early endosomes (13,14).…”