Vitamin D-Induced Calcium-Binding Protein

The gene mutation in the mouse, ‘arrested development of rightingresponse’, adr, causes a defect of chloride conductance of the muscle fibre membrane leading to the symptoms of myotonia [Mehrke, G., Brinkmeier, H. and Jockusch, H. (1988) Muscle & Nerve 11, 440‐446]. In fast muscle, the myotonic phenotype is accompanied by a drastic reduction of the Ca2+‐binding protein, parvalbumin. Messenger RNA levels in organs of myotonic (ADR) mice were analysed. In fast muscles of the mutant, in‐vitro‐translatable parvalbumin mRNA was strongly reduced, whereas the mRNA for the slow‐muscle‐specific protein, p19/6.8, was increased. In contrast, the parvalbumin mRNA in thecerebellum was not affected by the adr mutation. A reduction of the two parvalbumin mRNA species (700 and 1100 nucleotides) in ADR fast muscle and unaltered prvalbumin cDNA as a probe. The mRNA level for another Ca2+‐binding protein, calmodulin, was low in muscle and high in the central nervous system but was unaffected by the mutation. When adr/adrmice were fed a diet containing the membrane‐stabilising drug, tocainide, the levels inmuscle of the mRNAs for parvalbumin and p19/6.8 were partially normalised.

show abstract

“…3). Likewise, no difference was found in the mRNA levels of vitamin-Ddependent Ca2 ' -binding protein [39] (not shown).…”

Section: Fig 3 Porwrlhumin M R N a Kvc~1s In A D R Und W T M I C Ementioning

confidence: 92%

Opposite regulation of the mRNAs for parvalbumin and p19/6.8 in myotonic mouse muscle

Kluxen¹,

Schöffl

Berchtold

et al. 1988

European Journal of Biochemistry

View full text Add to dashboard Cite

show abstract

“…In the nervous system, calcium ions control a myriad of processes, including fast transport of molecules (1,2), synthesis and release of neurotransmitters, and membrane excitability (3,4). These actions depend largely on calcium-binding proteins, which mediate and modulate the actions of calcium ions (5)(6)(7)(8).…”

mentioning

confidence: 99%

Distribution of calcium-binding proteins in the chick visual system

Pfeiffer

Britto

1997

Braz J Med Biol Res

View full text Add to dashboard Cite

The calcium-binding proteins calbindin (CB), calretinin (CR), and parvalbumin (PV) have been extensively studied over the last decade since they appear to be important as buffers of intracellular calcium. In the present study we investigated the distribution of these proteins in the chick visual system by means of conventional immunocytochemistry. The results indicated that CB, CR, and PV are widely distributed in retinorecipient areas of the chick brain. In some regions, all three calcium-binding proteins were present at different intensities and often in different neurons such as in the dorsolateral thalamic complex. In other areas, such as the nucleus geniculatus lateralis ventralis, only CB and CR were detected, whereas PV was absent. These results show that these three calcium-binding proteins are differentially distributed in the visual system of the chick, with varying degrees of colocalization.

show abstract

“…These proteins are the best known molecular markers of vitamin D action on target cells and have been characterized for a number of species (3). Birds have only one CaBP of 28,000 molecular weight, while two CaBPs have been described in mammals (3,4). A small 9K CaBP having two calcium-binding sites was first located in the absorptive cells of the duodenum (5) but is also found in the placenta (6,7).…”

mentioning

confidence: 99%

“…These findings suggest a role for the hormone not only in the duodenum, placenta and kidney, but during the development of specific organs such as cerebellum, lung and thymus, and in agreement with many recent studies, point to a role of vitamin D in cellular differentiation and growth. ( The vitamin D-dependent CaBP, cholecalcin (1) or calbindin, is one of a group of intracellular proteins that bind calcium with an affinity constant Ka = lo6 M-' (2,3). These proteins are the best known molecular markers of vitamin D action on target cells and have been characterized for a number of species (3).…”

mentioning

confidence: 99%

“…( The vitamin D-dependent CaBP, cholecalcin (1) or calbindin, is one of a group of intracellular proteins that bind calcium with an affinity constant Ka = lo6 M-' (2,3). These proteins are the best known molecular markers of vitamin D action on target cells and have been characterized for a number of species (3). Birds have only one CaBP of 28,000 molecular weight, while two CaBPs have been described in mammals (3,4).…”

mentioning

confidence: 99%

See 1 more Smart Citation

Vitamin D-Dependent Calcium-Binding Proteins (CaBPs) in Human Fetuses: Comparative Distribution of 9K CaBP mRNA and 28K CaBP during Development

et al. 1987

View full text Add to dashboard Cite

ABSTRACT. The vitamin D-dependent calcium-binding protein (CaBP) cholecalcin or calbindin, has been used as a molecular marker of 1,25-dihydroxyvitamin D3 action. Mammals possess two CaBPs: a 9,000 mol wt (9K CaBP) and a 28,000 mol wt (28K CaBP). The distinct localization of each protein in the rat has been previously described with the aid of specific radioimmunoassays developed for each CaBP. Antibodies raised against the rat 28K CaBP can be used to detect this protein in a number of mammalian species including humans. In contrast, antibodies against rat 9K CaBP do not cross react with human 9K CaBP, but human 9K CaBP mRNA can be analyzed using a cDNA probe for rat 9K CaBP mRNA. Such a cross-hybridization between the rat cDNA probe and human CaBP mRNA was demonstrated by Northern analysis. We have documented the distribution and evolution of 28K CaBP and 9K CaBP mRNA in human tissues during fetal development from 14 to 32 wk of gestation. 28K CaBP was only present in kidney and cerebellum, and not detectable in duodenum. There was a 2-fold increase of 28K CaBP in the cerebellum between 14 and 24 wk of gestation. The 9K CaBP mRNA was unevenly distributed in human fetal tissues. 9K CaBP mRNA was present in classical vitamin D target tissues such as duodenum and placenta; high levels of 9K CaBP mRNA also were found in thymus and lung. These findings suggest a role for the hormone not only in the duodenum, placenta and kidney, but during the development of specific organs such as cerebellum, lung and thymus, and in agreement with many recent studies, point to a role of vitamin D in cellular differentiation and growth. (Pediatr Res 21: 362-367, 1987) Abbreviations 1,25(OH)2D3, 1,25-dihydroxyvitamin D3 CaBP, calcium-binding protein 9K CaBP, 9,000 molecular weight calcium-binding protein 28K CaBP, 28,000 molecular weight calcium-binding protein PGFa, prostaglandin DEPC, diethylpyrocarbonate SDS, sodium dodecyl sulfateThe vitamin D-dependent CaBP, cholecalcin (1) or calbindin, is one of a group of intracellular proteins that bind calcium with an affinity constant Ka = lo6 M-' (2, 3). These proteins are the best known molecular markers of vitamin D action on target cells and have been characterized for a number of species (3). Birds have only one CaBP of 28,000 molecular weight, while two CaBPs have been described in mammals (3, 4). A small 9K CaBP having two calcium-binding sites was first located in the absorptive cells of the duodenum (5) but is also found in the placenta (6, 7). A larger 28K CaBP, similar to the chick 28K CaBP (3), possesses four calcium-binding sites and is concentrated in the distal tubules of the kidney (8) and the Purkinje cells of cerebellum (9). Although their exact molecular functions remain unclear, 9K CaBP in the duodenum and the placenta as well as 28K CaBP in the kidney are probably involved in calcium transfer. 28K CaBP has been proposed as a marker of Purkinje cell differentiation and development of the cerebellum (10). Vitamin D-dependence of rat intestinal 9K CaBP gene expression ...

show abstract

Vitamin D-Induced Calcium-Binding Protein

Cited by 60 publications

References 104 publications

Opposite regulation of the mRNAs for parvalbumin and p19/6.8 in myotonic mouse muscle

Opposite regulation of the mRNAs for parvalbumin and p19/6.8 in myotonic mouse muscle

Distribution of calcium-binding proteins in the chick visual system

Vitamin D-Dependent Calcium-Binding Proteins (CaBPs) in Human Fetuses: Comparative Distribution of 9K CaBP mRNA and 28K CaBP during Development

Contact Info

Product

Resources

About