Literature DB >> 2946677

An immunological comparison of several novel calcium-binding proteins.

V L Smith, J R Dedman.   

Abstract

Polyclonal antibodies prepared against each of the calcimedins were utilized to determine their tissue distribution. The immunological survey of rat tissues revealed that the levels of the 35-kDa calcimedin varied, while the amount of the 67-kDa calcimedin was relatively constant in the tissues examined. A new immunoreactive species, 52 kDa, was detected with the antibody to the 35-kDa calcimedin; this protein appears to be the predominant immunoreactive species in the tissues examined. Antibodies to the 35-kDa calcimedin were also used to compare many other calcium-binding proteins in order to determine immunological relationships. These comparisons demonstrate that the epidermal growth factor receptor/kinase substrate (p35), the src kinase substrate (pp36), and calregulin are immunologically unrelated to the calcimedins. However, it was found that the 67-kDa calcimedin and the p70 calelectrin are identical, as are the 35-kDa calcimedin and the p32.5 calelectrin. The calimedins are a subset of the chromobindins. In addition, the antibody to the 35-kDa calcimedin also cross-reacts with synexin, which may be related to the new 52-kDa immunoreactive protein identified.

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Year:  1986        PMID: 2946677

Source DB:  PubMed          Journal:  J Biol Chem        ISSN: 0021-9258            Impact factor:   5.157


  16 in total

Review 1.  Evaluation of the annexins as potential mediators of membrane fusion in exocytosis.

Authors:  W J Zaks; C E Creutz
Journal:  J Bioenerg Biomembr       Date:  1990-04       Impact factor: 2.945

2.  An immunological and biochemical comparison of 67 kDa calcimedin and 67 kDa calelectrin.

Authors:  R Kobayashi; Y Tashima
Journal:  Biochem J       Date:  1989-09-15       Impact factor: 3.857

3.  A dimeric form of lipocortin-1 in human placenta.

Authors:  R B Pepinsky; L K Sinclair; E P Chow; B O'Brine-Greco
Journal:  Biochem J       Date:  1989-10-01       Impact factor: 3.857

4.  Regulation of calpactin I phospholipid binding by calpactin I light-chain binding and phosphorylation by p60v-src.

Authors:  M A Powell; J R Glenney
Journal:  Biochem J       Date:  1987-10-15       Impact factor: 3.857

5.  Structural and functional characterization of endonexin II, a calcium- and phospholipid-binding protein.

Authors:  D D Schlaepfer; T Mehlman; W H Burgess; H T Haigler
Journal:  Proc Natl Acad Sci U S A       Date:  1987-09       Impact factor: 11.205

6.  67 k calcimedin (67 kDa) is distinct from p67 calelectrin and lymphocyte 68 kDa Ca2+-binding protein.

Authors:  S S Morse; P B Moore
Journal:  Biochem J       Date:  1988-04-01       Impact factor: 3.857

7.  A 36 kDa monomeric protein and its complex with a 10 kDa protein both isolated from bovine aorta are calpactin-like proteins that differ in their Ca2+-dependent calmodulin-binding and actin-severing properties.

Authors:  F Martin; J Derancourt; J P Capony; A Watrin; J C Cavadore
Journal:  Biochem J       Date:  1988-05-01       Impact factor: 3.857

8.  Developmental regulation of tyrosine kinase substrate p36 (calpactin heavy chain) in rat cerebellum.

Authors:  R D Burgoyne; M A Cambray-Deakin; K M Norman
Journal:  J Mol Neurosci       Date:  1989       Impact factor: 3.444

9.  The pattern of plant annexin gene expression.

Authors:  M F Smallwood; S J Gurr; M J McPherson; K Roberts; D J Bowles
Journal:  Biochem J       Date:  1992-01-15       Impact factor: 3.857

10.  Calcium-binding proteins 33 kDa, 35 kDa, and 65/67 kDa in normal rat and Morris hepatoma tissues. A biochemical and immunohistochemical study.

Authors:  D Josić; R Gossrau; R Habermann; Y P Lim; W Reutter
Journal:  Histochemistry       Date:  1990
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