Calcium-binding proteins 33 kDa, 35 kDa, and 65/67 kDa in normal rat and morris hepatoma tissues

Abstract

Polyclonal antibodies were raised against membrane-associated calcium-binding proteins (apparent molecular masses 65000 and 67000 (CBP 65/67) and 33000 and 35000 (CBP 33 and CBP 35)), which were isolated from rat liver and Morris hepatoma. Using immunoblotting, various amounts of CBP 33 and CBP 35 as well as CBP 65/67 were detected in most rat organs. Using alkaline phosphatase and monoclonal-anti-alkaline phosphatase antibodies (APAAP), all the calcium-binding proteins were detected by immunohistochemical techniques in the plasma membranes of many cells, such as vascular endothelial cells, lymphocytes, epididymal principal cells, secretory and excretory duct cells of certain exocrine glands, straight distal tubular cells of the kidney, and in the cytoplasm of muscle cells and fibres as well as nerve cells and chondrocytes, and in connective tissue elements. Immunohistochemical analysis also showed that in polarized epithelial cells, e.g., renal tubular cells, epididymal principal cells or excretory duct cells, these calcium-binding proteins are present exclusively or mostly in the luminal plasma membrane.

Involvement of annexin V in the entry of influenza viruses and role of phospholipids in infection

“…The cruvirus-binding protein we found probably corresponds to ancial question is whether binding of influenza virus to annexin nexin V. Further experiments showed that infection of influ-V (or annexin 33 kDa) is an essential step for infection. Anenza viruses could be inhibited by externally added phosphonexins are thought to be both intracellular and plasma memlipids as well as by antiserum against annexin V. These results brane components [10][11][12]. If the binding of viral phospholisubstantiated our view that annexins may serve as a second pids to the annexins of the plasma membrane is an essential receptor for these viruses, step for infection, externally added phospholipids should compete in this reaction, resulting in the inhibition of virus infec-2.…”

cDNA Cloning and Tissue-specific Regulation of Expression of Rat Calcium-binding Protein 65/67. Identification as a Homologue of Annexin VI

“…Recently a group of calcium binding proteins (CBP) from rat liver was isolated and characterized in our laboratory (JosiC et al, 1990). The biochemical and immunological analysis indicated that these CBPs meet all the valid criteria for annexins.…”

“…CBP 65/67 was isolated from liver plasma membranes by stepwise extraction and subsequent HPLC as reported previously (JosiC et al, 1985(JosiC et al, , 1990. After preparative electrophoresis on a 10% SDS gel, the CBP65 and the CBP67 polypeptides were separated after detection by Scheele staining (Scheele et al, 1981).…”

“…Annexin I11 was recently identified as inositol 1,2-monophosphate 2-phosphohydrolase (Ross et al, 1990), and annexin V stimulates calcium channel activity (Rojas et al, 1990; Hazarika et al, 1991). It has also been shown that annexins bind collagen (Pfaffle et al, 1988; Wirl and Schwartz-Albiez, 1990;Wu et al, 1991).Recently, a group of Ca2+ binding proteins (CBP 65/67, CBP 35 and CBP 33) was isolated from rat liver and Morris hepatoma 7777 (JosiC et al, 1990). Biochemical and immunological analyses indicated that these CBPs meet all the criteria that are valid for annexins.…”

“…Recently, a group of Ca2+ binding proteins (CBP 65/67, CBP 35 and CBP 33) was isolated from rat liver and Morris hepatoma 7777 (JosiC et al, 1990). Biochemical and immunological analyses indicated that these CBPs meet all the criteria that are valid for annexins.…”