Tyrosine kinase substrate annexin II (p36)--biochemical characterization and conservation among species.

نویسنده

  • V Gerke
چکیده

secreted then degraded by endogenous proteases, because placental annexin 4 was not degraded when added to prostate fluid and incubated at 37°C. The collective concentrations of annexin 1 , des-( 1 -29)-annexin 1, and annexin 5 in prostate fluid and seminal plasma were 1.3% and 0.2% of the total protein, respectively. This is consistent with their secretion by the prostate and subsequent dilution of seminal vesicle fluid.

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منابع مشابه

Views and Reviews Tyrosine Protein Kinase Substrate p 36 : A Member of the Annexin Family of Ca 2 - I - / P hosphol ipid - Bindi ng Proteins

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The tyrosine phosphorylation substrate p36 is developmentally regulated in embryonic avian limb and is induced in cell culture

The 36-kD protein-tyrosine kinase substrate p36 has been variously postulated to be involved in membrane-cytoskeletal interactions, membrane traffic, and the regulation of phospholipase A2, and its phosphorylation may play some role in malignant transformation by avian sarcoma viruses. Because embryonic tissues are resistant to transformation by avian sarcoma viruses, we have examined the expre...

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The 46,000-dalton tyrosine protein kinase substrate is widespread, whereas the 36,000-dalton substrate is only expressed at high levels in certain rodent tissues

Proteins of molecular mass 46,000 (p46) and 34,000-39,000 (p36) daltons are phosphorylated at tyrosine in Rous sarcoma virus-transformed chicken and mouse fibroblasts. p46 has recently been identified as an isozyme of enolase but the function of p36 is unknown. The expression of these proteins in various mouse and rat tissues has been examined. In most tissues, except muscle, p46 is found at re...

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Annexin II up-regulates cellular levels of p11 protein by a post-translational mechanisms.

Annexin II (p36) and p11, which belong to two different families of calcium-binding proteins, are able to form a heterotetrameric protein complex (p36)2(p11)2 called calpactin I. As these proteins were detectable only in the presence of each other in a variety of cell lines, we studied the mechanisms of regulation of cellular levels of annexin II and p11. In cells expressing p11 messenger RNA, ...

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عنوان ژورنال:
  • Biochemical Society transactions

دوره 18 6  شماره 

صفحات  -

تاریخ انتشار 1990