scholarly journals Purification, immunological and biochemical characterization of rat 28 kDa cholecalcin (cholecalciferol-induced calcium-binding proteins). Identity between renal and cerebellar cholecalcins

1985 ◽  
Vol 231 (1) ◽  
pp. 89-95 ◽  
Author(s):  
S Intrator ◽  
J Elion ◽  
M Thomasset ◽  
A Brehier
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Biochemical Characterization ◽  
Structural Characteristics ◽  
Single Species ◽  
Calcium Binding Proteins ◽  
Significant Difference ◽  
High Concentrations

The cholecalcins are intracellular vitamin D-dependent calcium-binding proteins. High concentrations of 28 kDa cholecalcins have been found in the kidneys and cerebella of birds and mammals. However, whereas the synthesis of the renal protein is vitamin D-dependent, that of the cholecalcin in the cerebella of young growing chicks and rats is apparently not. In the present study a range of immunological, physicochemical and structural characteristics of renal and cerebellar cholecalcins isolated from a single species, the rat, has been examined to ascertain what, if any, differences there are between them, other than the vitamin D-dependence. Both proteins behaved in exactly the same way during purification and showed complete immunocross-reactivity in Ouchterlony double immunodiffusion and radioimmunoassay. No difference could be detected between them on electrophoresis under denaturing conditions or on two-dimensional isoelectric focusing/electrophoresis. Their amino acid compositions were very similar, as were their u.v.-absorption spectra and their chymotryptic and tryptic peptide maps. The N-terminal sequence was found to be Gly-Gly-Val-Ser... for both cholecalcins. We have thus been unable to show any significant difference between the two proteins and suggest that the 28 kDa cholecalcins of the rat cerebellum and kidney are extremely similar, if not identical.

scholarly journals HUMAN FETAL CARTILAGE: PRESENCE OF TWO VITAMIN D-DEPENDENT CALCIUM-BINDING PROTEINS

1985 ◽  
Vol 19 (10) ◽  
pp. 1116-1116
Author(s):  
N Balmain ◽  
A Brehier ◽  
M Thomasset ◽  
P Cuisinier-Gleiaes ◽  
H Mathieu
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins

“Vitamin D dependent” calcium binding proteins in brain: Caracterization and localisation

1985 ◽  
Vol 10 ◽  
pp. 232
Author(s):  
F. Rypens ◽  
A. Roman ◽  
R. Pochet ◽  
M. Parmentier ◽  
L. Surardt ◽  
...  
Keyword(s):  
Vitamin D ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Calcium Binding Proteins

Vitamin D independence of small calcium-binding proteins in nonclassical target tissues

1991 ◽  
Vol 260 (5) ◽  
pp. E794-E800
Author(s):  
M. R. Walters ◽  
M. E. Bruns ◽  
R. M. Carter ◽  
P. C. Riggle
Keyword(s):  
Vitamin D ◽  
Rat Brain ◽  
Blot Analysis ◽  
Calcium Binding ◽  
Binding Proteins ◽  
Immunoblot Analysis ◽  
Calcium Binding Proteins ◽  
Northern Analysis ◽  
Dihydroxyvitamin D3 ◽  
Low Levels

The presence and regulation of Ca-binding proteins (CaBPs) were investigated in newly identified 1,25-dihydroxyvitamin D3 [1,25(OH)2D3] target tissues. 45Ca(2+)-blot analysis of proteins in normal rats yielded a 45Ca2+ band comigrating with authentic calmodulin. Additionally, a parvalbumin-like band (mol mass = 15.4 +/- 0.3 kDa) was prominent in prostate, and a strong unidentified 45Ca2+ band was always evident in the testis (mol mass = 23.5 +/- 0.7 kDa). Lung, bladder, and especially prostate demonstrated 45Ca2+ bands comigrating with the intestinal vitamin D-related CaBP (CaBP-D9K; mol mass = 10.9 +/- 0.5 kDa). Most tissues (including testis, heart, and lung) exhibited low levels of a 45Ca2+ band comigrating with the renal CaBP-D28K (mol mass = 28.3 +/- 0.4 kDa). Importantly, 45Ca2+ binding to all detectable CaBPs was unchanged in these four tissues in vitamin D-deficient rats, despite substantial downregulation of the intestinal CaBP-D9K and renal CaBP-D28K. Neither immunoblot analysis (rabbit anti-rat renal CaBP-D28K) nor Northern analysis (rat brain CaBP-D28K cDNA) provided evidence for coidentity of the 28-kDa 45Ca2+ band with the CaBP-D28K. Conversely, immunoblot analysis of lung, but not prostate, cytosol provided evidence for specific immunocross-reactivity to rabbit anti-rat intestinal CaBP-D9K. Immunoblot analysis of the 9-kDa CaBP in lung further confirmed its vitamin D independence. In conclusion, the vitamin D independence of the CaBPs in these putative new 1,25(OH)2D3 targets suggests the absence of an obligatory relationship between 1,25(OH)2D3 effects and CaBP induction therein.(ABSTRACT TRUNCATED AT 250 WORDS)

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